TECHNICAL FIELD 5 The present invention relates to novel antibodies capable of binding specifically to the human c-Met receptor andlor capable of specifically inhibiting the tyrosine kinase activity of said receptor, especially monoclonal antibodies of murine, chimeric and humanized origin, as well as the amino acid and nucleic acid sequences coding for these antibodies. More particularly, antibodies according to the invention are capable of 10 inhibiting the c-Met dimerization. The invention likewise comprises the use of these antibodies as a medicament for the prophylactic andior therapeutic treatment of cancers or any pathology connected with the overexpression of said receptor as well as in processes or kits for diagnosis of illnesses connected with the overexpression of c-Met. The invention fmally comprises products and/or compositions comprising such 15 antibodies in combination with other antibodies and/or chemical compounds directed against other growth factors involved in tumor progression or metastasis and/or compounds andor anti-cancer age~xtso r agents conjugated with toxins and their use for the prevention andlor the treatment of certain cancers. 2 0 BACKGROUND OF THE INVENTION Receptor tyrosine kinase (RTIC) targeted agents such as trastuzunxdb, cetuximab, bevacizumab, imatinib and gefitinib inhibitors have illustrated the intercst of targeting this protein class for treatment of selected cancers. c-Met, is the protoiypic mcmber of a sub-family of RTKs wh~ch also includes 2 5 RON and SEA. The c-Met RTK family is structurally different from other RTI< families and is the only known high-affinity receptor for hepatocyte growth factor (HGF), also called scater factor (SF) [D.P. Bottaro et al., Science 1991, 251: 802-804; L. Naldini et al., Eur. Mol. Biol. Org. J. 1991, 10:2867-28781. c-Met and HGF are widely expressed in a variety of tissue and their expression is normally restricted to cells of epithelial and 30 inesenchymal origin respectively [M.F. Di Rcnzo et al., Oncogene 1991, 6:1997-2003; E. Sonuenberg et al., J. Cell. Biol. 1993, 123:223-2351. They are both required for norn~alm ammalian development and have 'been shown to be particularly important in cell migration, morphogenic differentiation, and organization of the three-dimensional tubular structures as well as growth and angiogenesis [F. Baldt et al., Nature 1995, 376:768-771; C. Schmidt et al., Nature. 1995:373:699-702; Tsarfaty et al., Science 1994,263:98-1011. While the controlled regulation of c-Met and HGF have been shown 5 to be important in mammalian development, tissue maintenance and repair [Nagayama T, Nagayama M, Kohara S, Kamiguchi H, Shibuya M, Katoh Y, Itoh J, Shinohara Y., Brain Res. 2004, 5;999(2):155-66; Tahara Y, Ido A, Yamamoto S, Miyata Y, Uto H, Hori T, Hayashi K, Tsubouchi H., J Pharmacol Exp Ther. 2003, 307(1):146-511, their dysregnlation is implicated in the progression of cancers. 10 Aberrant signalling driven by inappropriate activation of c-Met is one of the most frequent alteration observed in human cancers and plays a crucial role in tumorigenesis and metastasis [Birchmeier et al., Nat. Rev. Mol. Cell Biol. 2003, 4:915- 925; L. Trusolino and Comoglio P. M., Nat Rev. Cancer. 2002,2(4):289-3001. Inappropriate c-Met activation can arise by ligand-dependent and independent 15 mechanisms, which include overexpression of c-Met, andlor paracrine or autocrine activation, or through gain in function mutation [J.G. Christensen, Burrows J. and Salgia R., Cancer Latters. 2005, 226:l-261. However an oligomerization of c-Met receptor, in presence or in absence of the ligand, is required to regulate the binding affinity and binding kinetics of the lcinase toward ATP and tyrosine-containing peptide 2 0 substrates [Hays JL, Watowich SJ, Biochemistry, 2004 Aug 17* 43:10570-81. Activatcd c-Mct recruits signalling effectors to its multidoclcing site located in the cytoplasm domain, resulting in the activation of several lcey signalling pathways, including Ras- MAPIC, P13K, Src and Stat3 [Gao CF, Vande Woude GF, Cell Rcs. 2005, 15(1):49-51; Furge KA, Zbang YW, Vande Woude GF, Oncogene. 2000, 19(49):5582-91. These 2 5 pathways are essential for tunlour cell proliferation, invasion and angiogenesis and for evading apoptosis [Furge IM, Zhang YW, Vande Woude GF, Oncogene, 2000, 19(49):5582-9; Gu El, Nee1 BG, Trends Cell Biol. 2003 Mar, 13(3):122-30; Fan S, Ma YX, Wang JA, Yuan RQ, Meng Q, Cao Y, Laterra JJ, Goldbcrg ID, Rosen EM, Oncogene. 2000 Apr 27, 19(18):2212-231. In addition, a uniquc facet of the c-Met 30 signalling relative to other RTK is its reported interaction with focal adhcsion complexes and non kinase binding partners such as a6P4 intcgrins [Trusolino L, Bertotti A, Comoglio PM, Ccll. 2001, 107:643-541, CD44v6 [Van der Voort R, Taher TE, Wielenga VJ, Spaargaren M, Prevo R, Smit L, David G, Hartmann G, Gherardi E, Pals ST, J Biol Chem. 1999, 274(10):6499-5061, Plexin B1 or semaphorins [Giordano S, Corso S, Conrotto P, Artigiani S, Gilestro G, Barberis D, Tamagnone L, Comoglio PM, Nat Cell Biol. 2002, 4(9):720-4; Conrotto P, Valdembri D, Corso S, Serini G, 5 Tarnagnone L, Comoglio PM, Bussolino F, Giordano S, Blood. 2005, 105(11):4321-9; Conrotto P, Corso S, Gamberini S, Comoglio PM, Giordano S, Oncogene. 2004, 23:5131-71 which may further add to the complexity of regulation of cell function by this receptor. Finally recent data demonstrate that c-Met could be involved in tumor resistance to gefitinib or erlotinib suggesting that combination of compound targeting 10 both EGFR and c-Met might be of significant interest [Engelman JA at al., Science, 2007, 316:1039-431. In the past few years, many different strategies have been developed to attenuate c-Met signalling in cancer cell lines. These strategies include i) neutralizing antibodies against c-Met or HGFISF [Cao B, Su Y, Oslcarsson M, Zhao P, Kort EJ, Fisher W, 15 Wang LM, Vande Woude GF, Proc Natl Acad Sci U S A. 2001, 98(13):7443-8; Martens T, Schmidt NO, Eckerich C, Fillbrandt R, Merchant M, Schwall R, Westphal M, Lamszus K, Clin Cancer Res. 2006, 12(20):6144-521 or the use of HGFISF antagonist NK4 to prevent ligand binding to c-Met [Kuba K, Matsumoto K, Date K, Shimura H, Tanaka M, Nalcamura T, Canccr Res., 2000, 60:6737-431, ii) small ATP 2 0 binding site inhibitors to c-Met that blocli liinase activity [Christensen JG, Schrecli R, Burrows J, Kwuganti P, Chan E, Le P, Chen J, Wang X, Ruslim L, Blalce R, Lipson KE, Ramphal J, Do S, Cui JJ, Cherrington JM, Mendel DB, Cancer Res. 2003,63:7345- 551, iii) engineered SH2 domain polypeptide that interferes with access to the multidocking site and RNAi or ribozyme that reduce receptor or ligand expression. 25 Most of these approaches display a selective inhibition of +Met resulting in tumor inhibitiou and showing that c-Met could be of interest for therapcutic intervention in cancer. Within the molecules generated for c-Met targeting, some are antibodies. The most extensively described is the anti-c-Met 5D5 antibody generated by 30 Genentech [W096/38557] which behavcs as a potent agonist when added alone in various models and as an antagonist when uscd as a Fab fragme~~At. morlovalent engineered form of this antibody described as one armcd 5D5 (OA5D5) and produced as a recombinant protein in E. Cali is also the subject of a patent application [W020061015371] by Genentech. However, this molecule that could not be considered as an antibody because of its particular scarfold, displays also mutations that could be immunogenic in humans. In terms of activity, this unglycosylated molecule is devoided 5 of effector functions and finally, no clear data demonstrate that OA5D5 inhibits dimerization of c-Met. Moreover, when tested in the G55 in vivo model, a glioblastoma cell line that expresses c-Met but not HGF mRNA and protein and that grows independently of the ligand, the one armed anti-c-Met had no significant effect on G55 tumor growth suggesting that OA5D5 acts primarily by blocking HGF binding and is 10 not able to target tumors activated independently of HGF [Martens T. et al, Clin. Cancer Res., 2006, 12(20):6144-61521. Another antibody targeting c-Met is described by Pfizer as an antibody acting "predominantly as c-Met antagonist, and in some instance as a c-Met agonist" [WO 2005/016382]. No data showing any effect of Pfizer antibodies on c-Plet dimerization is 15 described in this application. One of the innovant aspects of the present invention is to generate mouse monoclonal antibodies without intrinsic agonist activity and inhibiting c-Met dimerization. In addition of targeting ligand-dependent tumors, this approach will also impair ligand-independent activations of c-Met due to its overexpression or mutations 20 of the intra cellular domains which remained dependent to oligomcrization for signalling. Another aspect of the activity of such antibodies could be a steric hindrance for c-Met interaction with its partners that will result in impairment of c-Met functions. These antibodies will be humanized and engineered preferentially, but not limited, as human IgGl to get effector functions such as ADCC and CDC in addition to hnctions 2 5 linked to the specific blocltade of the c-Met receptor. DISCLOSURE OF THE INVENTION Surprisingly, for the first time, invcntors have managed to gencrate an antibody capable of binding to c-Met but also capablc of inhibiting the c-Met dimerization. If it is 30 true that, in the prior art, it is sometimes suggested that an antibody capable of inhibiting thc dimerization of c-Met with it6 partners could be an intcresting onc, il has never becn dsclosed, or clcarly suggcsted, an antibody capable of doing so. Moreover, regarding antibody specificity, it was not evident at all to succeed in the generation of such an active antibody. In a first aspect, a subject of the present invention is a process for the generation and the selection of antibodies according to the invention. 5 More particularly, the invention concerns a process for the selection of an anti c- Met antibody, or one of its functional fragments or derivatives, capable to inhibit both ligand-dependent and ligand-independent activation of c-Met, said process comprising the following steps: i) screening the generated antibodies and selecting antibodies capable to bind 10 specifically to c-Met; ii) evaluating in vitro the selected antibodies of step i) and selecting antibodies capable to inhibit at least 50 %, preferably at least 60 %, 70 % or 80 % of tumoral cell proliferation for at least one tumor type; and then iii) testing the selected antibodies of step ii) and selecting antibodies capable to 15 inhibit the c-Met dimerization. As it was explained before, the inhibition of the c-Met dimerization is a capital aspect of the invention as such antibodies will present a real interest for a larger population of patients. Not only ligand-dependent activated c-Met cancer, as it was the case until the present invention, but also ligand-independent activated c-Met cancer 2 0 could be treated with antibodies generated by the proccss of the present invention. The generation of the antibody can be realizcd by any method known by the man skilled in the art, such as for example, fusion of a myeloma cell with spleen cells from immunized mice or other species con~patible with the selected myeloma cells [Kohler & Milstein, 1975, Nature, 256:495-4971. The immunized animals could include 2 5 transgenic nice with human immunoglobulin loci which then directly produce human antibodies. Another possible embodiment could consist in using phage display technologies to screen libraries. The screening step i) can be realized by any method or process linown by the man skilled in thc art. As non limitative examples, can be mentioned ELISA, BIAcore, 30 immunohistochemistly, FACS analysis and fwct~onal screens. A preferred process consists in a screen by ELTSA on the c-Met recombinant protein and then by FACS analysis on at least a tumoral cell llne to be sure that thc produced antibodies will be able to also recognize the native receptor on tumor cells. This process will be described more precisely in the following examples. In the same way, the step ii) can also be realized classically by known method or process such as, for example, using 3H-thymidine or any other DNA staining agent, 5 MTT, ATP evaluation, etc. A preferred tumor cell model in the present invention can consist in the BxPC3 model. By inhibiting c-Met dimerization, it must be understood preferably the c-Met homodimerization. In a preferred embodiment of the step iii) of selection of the process of the 10 invention, said step iii) consists in evaluating antibodies by BRET analysis on cells expressing both c-Met-RLucIc-Met-YFP and selecting antibodies capable to inhibit at least 30 %, preferably 35 %, 40 %, 45 %, 50 %, 55 % and most preferably 60 % of the BRET signal. The technology BRET is a technology known as being representative of the 15 protein dimerization [Angers et al., PNAS, 2000, 97:3684-891. The technology BRET, used in the step iii) of the process, is well known by the man sldll in the art and will be detailed in the following examples. More particularly, BRET (Bioluminescence Resonance Energy Transfer) is a non-radiative energy transfer occurring betwecn a bioluminescent donor (Rcnilla Luciferase (Rluc)) and a fluorescent 20 acceptor, a mutant of GFP (Green Fluorescent Protein) or YFP (Yellow fluorescent protein). In the present case EYFP (Enhanced Yellow Fluorcscent Protein) was used. The efficacy of transfer depends on the orientation and the distance between the donor and the acceptor. Then, the energy transfer can occur only if the two moleculcs are in close proximity (1-10 nm). This property is used to generate protein-protein interaction 2 5 assays. Indeed, in order to study the interaction between two pai-tners, the first one is genetically fused to the Rcnilla Luciferase and the second one to the yellow mutant of the GFP. Fusion proteins are generally, but not obligatoty, expressed in mammalian cclls. In presence of its membrane permeable substrate (coelenterazine), Rluc emits blue light. If the GFP mutant is closer that1 10 nm from the Rluc, an cnergy transfer can 3 0 occur and an additional yellow signal can be detected. The BRET signal is measured as the ratio between the light emitted by the acceptor and the light emittcd by the donor. So the BRET signal will increase as the hvo fusion proteins are brought into proximity or if a conformational change bring Rluc and GFP mutant closer. If the BRET analysis consists in a preferred embodiment, any method known by the man slulled in the art can be used to measure c-Met dimerization. Without limitation, the followmg technologies can be mentioned FRET (Fluorescence 5 Resonance Energy Transfer), HTRF (Homogenous Time resolved Fluorescence), FLIM (Fluorescence Lifetime Imaging Microscopy) or SW-FCCS single wavelength fluorescence cross-correlation spectroscopy). Other classical technologies could also be used, such as Coimmunoprecipitation, Alpha screen, Chemical cross-linking, Doublc-Hybrid, Affinity 10 Chromatography, ELISA or Far western blot. In a second aspect, a subject of the invention is an isolated antibody, or one of its functional fragments or derivatives, being obtained by said process. Said antibody or one of its said fragments or derivatives, is capable of binding specifically to the human c-Met and, if necessary, preferably moreover capable of inhibiting the natural 15 attachment of its ligand HGF andlor capable of specifically iuhibiting the tyrosine kinase activity of said c-Met, said antibody being also capable to inhib c-Met dimerization. More particularly, said antibodies will be capable of inhibiting both ligand-dependent and ligand-independent activation of c-Met. The expressions "functional fragments and derivatives" will be dcfined in details 2 0 later in the present specification. It must be understood here that the invention does not relatc to the antibodies in natural form, that is to say they are not in their natural environment but that they have been able to be isolated or obtained by purification from natural sources, or else obtained by genetic recombination, or by chemical synthesis, and that they can then 2 5 contain unnatural amino acids as will be described further on. More particularly, according to another aspect of the invention, it is claimed an antibody, or one of its functional fragments or derivatives, said antibody bcing characterized in that it comprises at least one complementary determining region CDR chosen from CDRs comprising the amino acid sequence SEQ ID Nos. 1 to 17 and 56 to 30 61. Any antibody, or fragments or derivatives, having at least one CDR whose sequence has at least 80 % identity, preferably 85 %, 90 %, 95 % and 98 % identity, after optimum alignment with the sequences SEQ ID Nos. 1 to 17 and 56 to 61 must be understood as a equivalent and, as a consequence, as being part of the invention. By CDR regions or CDR(s), it is intended to indicate the hypervariable regions of the heavy and light chains of the immunoglobulins as defined by IMGT. 5 The IMGT unique numbering has been defined to compare the variable domains whatever the antigen receptor, the chain type, or the species [Lefranc M.-P., Immunology Today 18, 509 (1997) / Lefranc M.-P., The Immunologist, 7, 132-136 (1999) / Lefranc, M.-P., Pommik, C., Ruiz, M., Giudicelli, V., Foulquier, E., Truong, L., Thouvenin-Contct, V. and Lefranc, Dev. Comp. Immunol., 27, 55-77 (2003)l. In the 10 IMGT unique numbering, the conserved amino acids always have the same position, for instance cysteine 23 (1st-CYS), tryptophan 41 (CONSERVED-TRP), hydrophobic amino acid 89, cysteine 104 (2nd-CYS), phenylalanine or tryptophan 118 (J-PHE or JTRP). The IMGT unique numbering provides a standardized delimitation of the framework regions (FR1-IMGT: positions 1 to 26, FR2-IMGT: 39 to 55, FR3-IMGT: 15 66 to 104 and FR4-IMGT: 118 to 128) and of the complementarity determining regions: CDR1-IMGT: 27 to 38, CDR2-IMGT: 56 to 65 and CDR3-IMGT: 105 to 117. As gaps represent unoccupied positions, the CDR-IMGT lengths (shown between brackets and separated by dots, e.g. [8.8.13]) become crucial information. The IMGT unique numbering is uscd in 2D graphical representations, designated as IMGT Colliers de 20 Perles [Ruiz, M. and Lefranc, M.-P., Immunogenetics, 53, 857-883 (2002) 1 Kaas, Q. and Lefranc, M.-P., Current Bioinformatics, 2, 21-30 (2007)], and in 3D structures in IMGT/3Dstructure-DB [Kaas, Q., Ruiz, M. and Lefranc, M.-P., T cell receptor and MHC structural data. Nucl. Acids. Res., 32, D208-D210 (2004)l. Three heavy chain CDRs and 3 light chain CDRs exist. The term CDR or CDRs 2 5 is used here in order to indicate, according to the case, one of these regions or several, or even the whole, of these regions which contain the majority of the amino acid residues responsible for the binding by afkity of the antibody for the antigen or the epitope which it recognizes. By "percentage of identity" between two nucleic acid or amino acid sequences 30 in the sense of the present invention, it is intendcd to indicate a pcrceniage of nucleotides or of identical amino acid residucs between the two sequences to be compared, obtaincd artcr the best alignment (optimum alignment), this percentagc bcing purcly statistical and the differences between the two sequences being distributed randomly and over their entire length. The comparisons of sequences between two nucleic acid or amino acid sequences are traditionally carried out by comparing these sequences after having aligned them in an optimum manner, said comparison being able 5 to be carried out by segment or by "comparison window". The optimum alignment of the sequences for the comparison can be carried out, in addition to manually, by means of the local homology algorithm of Smith and Waterman (1981) [Ad. App. Math. 2:482], by means of the local homology algorithm ofNeddleman and Wunsch (1970) [J. Mol Bin1 4 8 4431, by means of the similarity search method of Pearson and Lipman 10 (1988) [Proc. Natl. Acad. SCI. USA 85:2444), by means of computer software using these algorithms (GAP, BESTFIT, FASTA and TFASTA in the Wisconsin Genetics Software Package, Genetics Computer Group, 575 Science Dr., Madison, WI, or else by BLAST N or BLAST P comparison software). The percentage of identity between hvo nucleic acid or amino acid sequences is 15 determined by comparing these two sequences aligned in an optimum manner and in which the nucleic acid or amino acid sequence to be compared can comprise additions or deletions with respect to the reference sequence for an optimum alignment between these two sequences. The percentage of identity is calculated by determining the number of identical positions for which the nuclcotide or the amino acid rcsidue is 2 0 identical between the two sequences, by dividing this number of identical positions by the total number of positions in the comparison window and by multiplying the result obtained by 100 in ordcr to obtain the percentage of identity between thcsc two sequences. For example, it is possible to use the BLAST program, "BLAST 2 sequences" 25 (Tatusova et al., "Blast 2 scqucnces - a new tool for comparing protein and tlucleotidc sequcnces", FEMS Microbiol Lett. 174:247-250) avallablc on the site http://www ncbi.nlm.n~hg ov/ gorf/bl2.html, thc parameters used being those given by default (in particular for the parameters "open gap penalty": 5, and "exte~~siogna p penalty": 2; the matrix choscn bcing, for example, the matrix "BLOSUM 62" proposed 3 0 by the program), the percentage of idcntity between the two sequcnccs to be compared being calculated directly by thc program. By amino acid sequence having at least 80 %, preferably 85 %, 90 %, 95 % and 98 % identity with a reference amino acid sequence, those having, with respect to the reference sequence, certain modifications, in particular a deletion, addition or substitution of at least one amino acid, a truncation or ail elongation are preferred. In the 5 case of a substitution of one or more consecutive or nonconsecutive amino acid(s), the substitutions are preferred in which the substituted amino acids are replaced by "equivalent" amino acids. The expression "equivalent amino acids" is aimed here at indicating any amino acid capable of being substituted with one of the amino acids of the base structure without, however, essentially modifying the biological activities of 10 the corresponding antibodies and such as will be defined later, especially in the examples. These equivalent amino acids can be determined either by relying on their structural homology with the amino acids which they replace, or on results of comparative trials of biological activity between the different antibodies capable of being carried out. 15 By way of example, mention is made of the possibilities of substitution capable of being carried out without resulting in a profound modification of the biological activity of the corresponding modified antibody. As non limitative example, the following table I is giving substitution possibilities conceivable with a conservation of the biological activity of the modified 2 0 antibody. Thc reverse substitutions are also, of course, possible in the same conditions. Table 1 It must bc understood here that the invention does not relate to the antibodies in 5 natural form, that is to say they are not in their natural environment but that they have been able to be isolated or obtained hy purification from natural sources, or elsc obtained by genetic recombination, or by chemical synthesis, and that they can then contain unnatural amino acids as will be described further on. According a first approach, the antibody will be defined by its heavy chain 10 scqucnce. More particularly, the antibody of the invention, or one of its functional fragments or derivatives, is characterized in that it comprises a heavy chain comprising at ledst one CDR chosen from CDRs comprising the amino acid sequences SEQ ID Nos. 1 to 9 and 56 to 58. Thc mentioned sequences are the following ones: SEQ ID No. 1: GYIFTAYT SEQ ID No. 2: TKPNNGLA SEQ ID No. 3: AKSEITTEFDY Original residu Ala (A) Arg (R) Asn (N) ASP @) Cys (C) Gin (Q) Glu (G) G~(YG I His (H) Ile (I) Leu (L) Lys Met OLI) Phe (F) Pro (P) Ser (S) Thr (T) Trp (W) T Y(Y~) Val (v) Substitution(s) Val, Gly, Pro Lys, His Gln G lu Ser Asn Asp Ala Arg Leu Ile, Val, Met Arg Leu TF Ala Thr, Cys S er T yr Phe, Trp Leu, Ala SEQ ID No. 4: SEQ ID No. 5: SEQ ID No. 6: SEQ ID No. 7: 5 SEQ ID No. 8: SEQ ID No. 9: SEQ ID No. 56: SEQ ID No. 57: SEQ ID No. 58: GYSFTDYT INPYNGGT AREEITKDFDF GYTFTDYN INPNNGGT ARGRWGYYYAMDY GYTFTSYW INPTTGST AIGGYGSWFAY The CDRs of the heavy chain could be chosen randomly in the previous sequences, i.e. SEQ ID Nos. 1 to 9 and 56 to 58. According to a preferred aspect, the antibody of the invention, or one of its functional fragments or derivatives, comprises a heavy chain comprising at least one 15 CDR chosen from CDR-HI, CDR-H2 and CDR-H3, wherein: - CDR-HI comprises the amino acid sequence SEQ ID No. 1,4, 7 or 56, - CDR-H2 comprises the amino acid sequence SEQ ID No. 2,5,8 or 57, and - CDR-H3 comprises the amino acid sequence SEQ ID No. 3,6,9 or 58. According to a first embodiment of said aspect, thc antibody of the invention, or 2 0 one of its functional fragments or derivatives, comprises a heavy chain comprising CDR-HI, CDR-H2 and CDR-H3, wherein CDR-HI comprises the amino acid sequence SEQ ID No. 1, CDR-H2 compriscs the amino acid sequence SEQ ID No. 2 and CDRH3 comprises the amino acid seqncnce SEQ ID No. 3. More particularly, said antibody, or one of its functional fragments or 25 derivatives, according to this first embodiment comprises a heavy chain of sequence comprising the amino acid sequence SEQ ID No. 18. SEQ ID No. 18: EVQLQQSGPELVKPGASVKISCKTSGYIFTAYTMHWRSLG ESLDWIGGTKPNNGLANYNQKFKGKATLTVDKSSSTAYMDLRSLTSEDSAVYY CARSESTTEFDYWGQGTALTVSS 3 0 According to a second embodiment of said aspect, the antibody of the invention, or one of its functional fragments or derivatives, compriscs a heavy chain comprising CDR-HI, CDR-H2 and CDR-H3, wherein CDR-H I comprises the amino acid sequence SEQ ID No. 4, CDR-H2 comprises the amino acid sequence SEQ ID No. 5 and CDRH3 comprises the amino acid sequence SEQ ID No. 6. The antibody, or one of its functional fragments or derivatives, according to said 5 second embodiment will preferably comprise a heavy chain of sequence comprising the amino acid sequence SEQ ID No. 19. I SEQ ID No. 19: EVQLQQSGPELVKPGASMKISCKASGYSFTDYTLNWVKQSH GI 100 nucleotides) followed by 2 washes of 20 minutes at 20°C in 2 x SSC + 2% of SDS, 1 wash of 20 minutes at 20°C in 0.1 x SSC + 0.1 ?4 of SDS. The last wash is carried out in 0.1 x SSC + 0.1 % of SDS for 30 minutes at 60°C for a probe size > 100 nucleotides. 10 The hybridization conditions of high stringency described above for a polynucleotide of defined size can be adapted by the person slcilled in the art for oligonucleotides of greater or smaller size, according to the teaching of Sambrook et al. (1989, Molecular cloning: a laboratory manual. 2nd Ed. Cold Spring Harbor). The invention likewise relates to a vector comprising a nucleic acid according to 15 the present invention. The invention aims especially at cloning and/or expression vectors which contain a nucleotide sequence according to the invention. The vectors according to the invention preferably contain elements which allow^ the expression and/or the secretion of the nucleotide sequences in a determined host 2 0 cell. The vector must therefore contain a promoter, signals of initiation and termination of translation, as well as appropriate regions of regulation of trdn~cription. It must be able to be maintained in a stable manner in the host cell and can optionally have particular signals which specify the secretion of the translated protein. These different elements are chosen and optimized by the person slcilled in the art as a function of the 25 host cell used. To this effect, the nucleotide sequences according to the invention can be inserted into autonomous replication vectors in the chosen host, or be integrative vectors of the chosen host. Such vectors are prepared by methods currently used by the person skilled in the art, and the resulting clones can be introduced into an appropriate host by standard 30 mcthods, such as lipofection, electroporation, thermal shock, or chemical mcthods. The vectors according to thc invention are, for example, vectors of plasmidic or viral origin. They are useful for transforming host cells in order to clone or to express the nucleotide sequences according to the invention. The invention likewise comprises the host cells transformed by or comprising a 5 vector according to the invention. The host cell can be chosen from prolcaryotic or eulcaryotic systems, for example bacterial cells but likewise yeast cells or animal cells, in particular mammalian cells. It is lilcewise possible to use insect cells or plant cells. The invention lilcewise conccrns animals, except man, which comprise at least 10 one cell transformed according to the invention. According to another aspect, a subject of the invention is a process for production of an antibody, or one of its functional fragments accord~ngto the invention, characterized in that it comprises the following stages: a) culture in a medium and appropriate culture conditions of a host cell 15 according to the invention; and b) the recovery of said antibodies, or one of their functional fragments, thus produced starting from the culture medium or said cultured cells. The cells transformed according to the invention can be used in processes for preparation of recombinant polypeptidcs according to thc invention. The processcs for 20 preparation of a polypeptide accord~ng to the invention ~n recombinant form, characterized in that they employ a vector andlor a cell transformed by a vector according to the invention, are themselves comprised in the present invention. Preferably, a cell transformed by a vector according to the invention is cultured under conditions which allow the expression of said polypeptide and said recombinant peptide 2 5 is recovered. As has been said, thc host cell can be chosen from proka~otico r e~~lcaryotic systems. In particular, it is possible to identify nucleotide sequences according to the invention, facilitating secretion in such a prolraryotic or eukaryotic system. A vector according to the invention carrying such a sequence can therefore advantageously be 3 0 used for the production of recombinant proteins, intended to be secreted. In effect, the purification of these recombinant proteins of interest will be facilitatcd by the fact that they are present in the supernatant of the cell culture rather than in the interior of the host cells. It is likewise possible to prepare the polypeptides according to the invention by chemical synthesis. Such a preparation process is lilcewise a subject of the invention. 5 The person skilled in the art lmows the processes of chemical synthesis, for example the techniques employing solid phases [Steward et al., 1984, Solid phase peptide synthesis, Pierce Chem. Company, Rockford, 11 1, 2nd ed., (1984)l or techniques using partial solid phases, by condensation of fragments or by a classical synthesis in solution. The polypeptides obtained by chemical synthesis and being able to contain corresponding 10 unnatural amino acids are likewise comprised in the invention. The antibodies, or one of their functional fragments or derivatives, capable of being obtained by a process according to the invention are likewise comprised in the present invention. The invention also concerns the antibody ofthe invention as a medicament. 15 The invention likewise concerns a pharmaceutical composition comprising by way of active principle a compound consisting of an antibody, or one of its functional fragments according to the invention, preferably mixed with an excipient and/or a pharmaceutically acceptable vehicle. Another complementary embodiment of the invention consists in a composition 20 such as described above which comprises, moreover, as a combination product for simultaneous, separate or sequential use, an anti-tumoral antibody. Most preferably, said second anti-tumoral antibody could be chosen through anti-IGF-IR, anti-EGFR, anti-HER2/neu, anti-VEGFR, anti-VEGF, etc., antibodies or any other anti-tumoral antibodies known by the man skilled in the art. It is evident that 25 the use, as second antibody, of functional frapcnts or derivatives of above mentioned antibodies is part of the invention. As a most preferred antibody, anti-EGFR antibodies are sclected such as for example the antibody C225 (Erbitux). "Simultaneous use" is understood as mcaning the administration of thc two 30 compounds of the composition according to thc invcntion in a single and identical pharmaceutical form. "Separate use" is undcrstood as meaning the administration, at thc same time, of the two compounds of the composition according to the invention in distinct pharmaceutical forms. "Sequential use" is understood as meaning the successive administration of the two compounds of the composition according to the invention, each in a distinct 5 pharmaceutical form. In a general fashion, the composition according to the invention considerably increases the efficacy of the treatment of cancer. In other words, the therapeutic effect of the anti-c-Met antibodies according to the invention is potentiated in an unexpected manner by the administration of a cytotoxic agent. Another major subsequent advantage 10 produced by a composition according to the invention concerns the possibility of using lower efficacious doses of active principle, which allows the risks of appearance of secondav effects to be avoided or to be reduced, in particular the effects of the cytotoxic agent. In addition, this composition according to the invention would allow the 15 expected therapeutic effect to be attained more rapidly. The composition of the invention can also be characterized in that it comprises, moreover, as a combination product for simultaneous, separate or sequential use, a cytotoxiclcytostatic agent. By "anti-canccr therapeutic agents" or "cytotoxiclcytostatic agents", it is 20 intended a substance which, when administered to a subject, treats or prevents the development of cancer in the subject's body. As non limitative example of such agents, it can bc mentioned alkylating agents, anti-metabolites, anti-tumor antibiotics, mitotic inhibitors, chromatin function inhibitors, anti-angiogencsis agents, anti-est~ogens, antiandrogens or imnlunomodulators. 25 Such agents are, for example, cited in the 2001 cdition of VIDAL, on the page devoted to the compounds attached to the cancerology and henlatology column "Cytotoxics", thcse cytotoxic compounds cited with reference to this document are cited here as prefcrred cytotoxic agents. More particularly, the following agents are preferred according to the invention. 3 0 "Allylating agent" refers to any substance which can cross-link or alkylate any molecule, preferably nuclcic acid (e.g., DNA), within a cell. Examples of akylating agents include nitrogen mustard such as mechlorcthamine, chlorambucol, melpl~alen, chlorydrate, pipobromen, prednimustin, disodic-phosphate or estramustine; oxazophorins such as cyclophosphamide, altretamine, trofosfamide, sulfofosfamide or ifosfamide; aziridines or imine-ethylenes such as thiotepa, triethylenamine or altetramine; nitrosourea such as camustine, streptozocin, fotemustin or lomustine; 5 allcyle-sulfonates such as busulfan, treosulfan or improsulfan; triazenes such as dacarbazine; or platinum complexes such as cis-platinum, oxaliplatin and carboplatin. "Anti-metabolites" refer to substances that blocli cell growth andlor metabolism by interfering with certain activities, usually DNA synthesis. Examples of antimetabolites include methotrexate, 5-fluoruracil, floxuridine, 5-fluorodeoxyuridine, 10 capecitabine, cytarabine, fludarabine, cytosine arabinoside, 6-mercaptopurine (6-MP), 6-thioguanine (6-TG), chlorodesoxyadenosine, Sazacytidine, gemcitabine, cladribine, deoxycoformycin and pentostatin. "Anti-tumor antibiotics" refer to compounds which may prevent or inhibit DNA, RNA andlor protein synthesis. Examples of anti-tumor antibiotics include doxorubicin, 15 daunorubicin, idarubicin, valnibicin, mitoxantrone, dactinomycin, mithramycin, plicamycin, mitomycin C, bleomycin, and procarbazine. "Mitotic inhibitors" prevent normal progression of the cell cycle and mitosis. In general, microtubule inhibitors or taxoides such as paclitaxel and docetaxel are capable of inhibiting mitosis. Vinca aUialoid such as vinblastine, vincristine, vindcsine and 2 0 vinorelbine are also capable of inhibiting mitosis. "Chromatin function inhibitors" or "topoisomerase inhibitors" refer to substances which inhibit the normal function of chromatin modeling proteins such as topoisomerase I or topoisomerasc TI. Examples of chromatin function inhibitors include, for topoisomerase I, camptothecine and its derivatives such as topotecan or irinotecan, 2 5 and, for topoisomerase TI, etoposidc, etoposide phosphate and teniposide. "Anti-angiogenesis agent" refers to any drug, compound, substance or agent which inhibits growth of blood vessels. Exemplary anti-angiogenesis agents include, but are by no means limited to, razoxin, marimastat, batimastat, prinomastat, tanomastat, ilomastat, CGS-27023A, halofuginon, COL-3, neovastat, BMS-275291, thalidomide, 30 CDC 501, DMXAA, L-651582, squalamine, endostatin, SU5416, SU6668, interferonalpha, EMD121974, interleuliin-12, TM862, angiostatin and vitaxin. "Anti-estrogen" or "anti-estrogenic agent" rcfcr to any substance which reduces, antagonizes or inhibits the action of estrogen. Examples of anti-estrogen agents are tamoxifen, toremifene, raloxifene, droloxifene, iodoxyfene, anastrozole, letrozole, and exemestane. "Anti-androgens" or "anti-androgen agents" refer to any substance which 5 reduces, antagonizes or inhibits the action of an androgen. Examples of anti-androgens are flutamide, nilutamide, bicalutamide, sprironolactone, cyproterone acetate, finasteride and cimitidine. "Immunomodulators" are substances which stimulate the immune system. Examples ofimmunomodulators include interferon, interleukin such as 10 aldesleukine, OCT-43, denileukin diflitox and interleukin-2, tumoral necrose fators such as tasonermine or others immunomodulators such as lentinan, sizofiran, roquinimex, pidotimod, pegademase, thymopentine, poly I:C or levamisole in conjunction with 5- fluorouracil. For more detail, the man sltill in the art could refer to the manual edited by the 15 "Association Fran~aise des Enseignants de Chimie ThQapeutiquen and entitled "trait6 de chimie thbrapeutique, vol. 6, M6dicaments antitumoraux et perspectives dans le traitement des cancers, edition TEC & DOC, 2003". Can also be mentioned as chemical agents or cytotoxic agents, all liinase inhibitors such as, for examplc, gefitinib or erlotinib. 2 0 In a particularly preferred embodiment, said composition as a combination product according to the invention is characterized in that said cytotoxic agent is coupled chemically to said antibody for simultaneous use. In order to facilitate the coupling bctwcen said cytotoxic agent and said antibody according to the invention, it is especially possible to introduce spacer molecules 25 between the two compounds to be coupled, such as poly(alky1ene) glycols like polyethylene glycol, or else amino acids, or, in another embodiment, to use active derivatives of said cytotoxic agents into which would have been introduced functions capable of reacting with said antibody according to the invention. These coupling techniques are well laown to the person skilled in the art and will not be expanded upon 3 0 in the present description. The invention relates, in another aspect, to a composition characterized in that one, at least, of said antibodies, or one of their functional fragments or derivatives, is conjugated with a cell toxin and/or a radioelement. Preferably, said toxin or said radioelement is capable of inhibiting at least one 5 cell activity of cells expressing the c-Met, in a more preferred manner capable of preventing the growth or the proliferation of said cell, especially of totally inactivating said cell. Preferably also, said toxin is an enterobacterial toxin, especially Pseudomonas exotoxin A. 10 The radioelements (or radioisotopes) preferably conjugated to the antibodies employed for the therapy are radioisotopes which emit gamma rays and preferably iodineI3', yttriumg0, gold'gg, palladium'00, copper6', bismuth2'' and antimon?". The radioisotopes which emit beta and alpha rays can likewise be used for the therapy. By toxin or radioelement conjugated to at least one antibody, or one of its 15 functional fragments, according to the invention, it is intended to indicate any means allowing said toxin or said radioelement to bind to said at least one antibody, especially by covalent coupling between the two compounds, with or without introduction of a linking molecule. Among the agents allowing binding in a chcmical (covalent), electrostatic or 20 noncovalent manner of all or part of the components of the conjugate, mention may particularly be made of benzoquinone, carbodiimide and more particularly EDC (1- ethyl-3-[3-dimethyl-aminopropyll-carbodiimide hydrochloride), dimaleimide, dithiobisnitrobenzoic acid (DTNB), N-succinimidyl S-acetyl thio-acetate (SATA), the bridging agents having one or more phenylazide groups reacting with the ultraviolets (U.V.) and 2 5 preferably N-[-4-(azidosalicylamino)butyl]-3'-(2'-pyridyldithio)-propionainide (APDP), N-succinimid-yl 3-(2-pyridy1dithio)propionate (SPDP), 6-hydrazino-nicotinamide (HYNIC). Another form of coupling, especially for the radioelements, can consist in the use of a bifunctional ion chelator. 30 Among these chelatcs, it is possible to mention the chelates derived from EDTA (ethylenediaminctetraacetic acid) or from DTPA (diethylenetriaminepentaacetic acid) which have been developed for binding metals, cspccially radioactive metals, and immunoglobulins. Thus, DTPA and its derivatives can be substituted by different groups on the carbon chain in order to increase the stability and the rigidity of the ligand-metal complex (Krejcarek et al. (1977); Brechbiel et al. (1991); Gansow (1991); US patent 4,831,175). 5 For example diethylenetriaminepentaacetic acid (DTPA) and its derivatives, which have been widely used in medicme and in biology for a long time either in their free form, or in the form of a complex with a metallic ion, have the remarlcable characteristic of forming stable chelates with metallic ions and of being coupled with proteins of therapeutic or diagnostic interest such as antibodies for the devclopment of 10 radioimrnunoconjugates in cancer therapy (Meases et al., (1984); Gansow et al. (1990)). Likewise preferably, said at least one antibody forming said conjugate according to the invention is chosen from its fimctional fragments, especially the fragments amputated of their Fc component such as the scFv fragments. As already mentioned, in a preferred embodiment of the invention, said 15 cytotoxiclcytostatic agent or said toxin andlor a radioelement is coupled chemically to at least one of the elements of said composition for simultaneous use. The present invention comprises the described composition as a medicament. The present invention moreover comprises the use of the composition according to the invention for the preparation of a medicament. 2 0 In another aspect, the invention deals with the use of an antibody, or one of its functional fragments or derivatives, and/or of a composition as above described for the preparation of a medicament intended to inhibit the growth andor the proliferation of tumor cells. Another aspect of the invention consists in the use of an antibody, or one of its 2 5 functional fragments or derivatives andlor of a composition, as described above or the use above mentioned, for the preparation of a medicament intended for the prevention or for the treatment of cancer. Is also comprises in the present invention a method intended to inhibit the growth andlor the proliferation of tumor cells in a patient comprising the administration 30 to a paticnt in need thereof of an antibody, or one of its functional fragments or derivatives according to the invention, an antibody produced by an hybridoma according to the invention or a composition according to the invention. WE CLAIM: 1. An isolated antibody, or one of its functional divalent fragments capable of binding to the c-Met, characterized in that said isolated antibody or said functional divalent fragments is selected from: 5 a) an antibody comprising a heavy chain comprising CDR-HI, CDR-HZ and CDR-H3 comprising respectively the amino acid sequence SEQ ID Nos. 56, 57 and 58; and a light chain comprising CDR-L1, CDR-L2 and CDR-L3 comprising respectively the amino acid sequence SEQ ID Nos. 59, 60 and 61; b) an antibody comprising a heavy chain comprising CDR-HI, CDR-H2 and CDR-H3 10 comprising respectively the amino acid sequence SEQ ID Nos. 4, 5 and 6; and a light chain comprising CDR-L1, CDR-L2 and CDR-L3 comprising respectively the amino acid sequence SEQ ID Nos. 13, 11 and 14; and c) an antibody comprising a heavy chain comprising CDR-HI, CDR-H2 and CDR-H3 comprising respectively the amino acid sequence SEQ ID Nos. 7, 8 and 9; and a light chain comprising CDR-L1, CDR-L2 and CDR-L3 comprising respectively the amino acid sequence SEQID Nos. 15, 16 and 17. 2. The antibody of claim 1, or one of i t s functional divalent fragments, characterized in that said isolated antibody or said functional divalent fragments is selected from: 20 a) an antibody comprising a heavy chain comprising the amino acid sequence SEQ ID No. 63 and a light chain comprising the amino acid sequence SEQ ID No. 62; b) an antibody comprising a heavy chain comprising the amino acid sequence SEQ ID No. 19 and a light chain comprising the amino acid sequence SEQ ID No. 22; and c) an antibody comprising a heavy chain comprising the amino acid sequence SEQ ID No. 20 and a light chain comprising the amino acid sequence SEQ ID No. 23. 3. A murine hybridoma capable of secreting an antibody as claimed in claim 2, 30 characterized in that said murine hybridoma is selected from: a) the murine hybridoma deposited at the CNCM, lnstitut Pasteur, Paris, on March 14, 2007 under the number 1-3724; 93 b) the murine hybridoma deposited at the CNCM, lnstitut Pasteur, Paris, on March 14, 2007 under the number 1-3732; and c) the murine hybridoma deposited at the CNCM, lnstitut Pasteur, Paris, on July 6, 2007 under the number 1-3786. 5 4. The antibody of claim 1 or 2, or one of i t s functional divalent fragments, characterized in that it consists in a monoclonal antibody. 5. The antibody of claim 4, or one of i t s functional divalent fragments, characterized in that said antibody is a chimeric antibody and moreover comprises the light chain and heavy chain constant regions derived from an 10 antibody of a species heterologous to the mouse. 6. The chimeric antibody of claim 5, or one of i t s functional divalent fragments, characterized in that said heterologous species is man. 7. The humanized antibody of claim 6, or one of i t s functional divalent fragments or, characterized in that the light chain and heavy chain constant regions derived 15 from a human antibody are respectively for the light chain the kappa region and for the heavy chain the gamma-I, gamma-2 or gamma-4 region. 8. The antibody of one of claims 1 to 7, or one of i t s functional divalent fragments, characterized in that it is capable to bind specifically to c-Met. 9. The antibody of claim 8, or one of i t s functional divalent fragments, 20 characterized in that it is capable to inhibit ligand-dependent and ligandindependent activation of c-Met. 10.The antibody of claim 9, or one of i t s functional divalent fragments, characterized in that it inhibits the c-Met dimerization. 11. The antibody of claim 10, or one of i t s functional divalent fragments, 25 characterized in that it inhibits at least 50 % of tumoral cell proliferation for at least one tumor type. 12. An isolated nucleic acid, characterized in that it is chosen from the following nucleic acids: a) a nucleic acid, DNA or RNA, coding for an antibody, or one of its functional divalent fragments, as claimed in claim 1 or 2; b) a nucleic acid comprising a DNA sequence comprising the sequences SEQ ID No. 64, SEQ ID No. 65, SEQ ID No. 66 and the sequences SEQ ID No. 67, SEQ ID No. 5 68 and SEQ ID No. 69, or a DNA sequence comprising the sequences of SEQ ID No. 27, SEQ ID No. 28, SEQ ID No. 29 and the sequences SEQ ID No. 36, SEQ ID No. 34 and SEQ ID No. 37, or a DNA sequence comprising the sequences of SEQ ID No. 30, SEQ ID No. 31, SEQ ID No. 32 and the sequences SEQ ID No. 38, SEQ ID No. 39 and SEQ ID No. 40; 10 c) a nucleic acid comprising a DNA sequence comprising the sequences SEQ ID No. 70 and SEQ ID No. 71, or a DNA sequence comprising the sequences of SEQ ID No. 42 and SEQ ID No. 45, or a DNA sequence comprising the sequences of SEQ ID No. 43 and SEQ ID No. 46; d) the corresponding RNA nucleic acids of the nucleic acids as defined in b) or c); 15 and e) the complementary nucleic acids of the nucleic acids as defined in a), b) and c). 13. A vector comprising a nucleic acid as claimed in claim 12. 14. A host cell with the exception of a transformed host cell within a human, 20 comprising a vector as claimed in claim 13. 15. A transgenic animal with the exception of human comprising at least one cell transformed by a vector as claimed in claim 14. 16. A process for production of an antibody, or one of i t s functional divalent fragments, as claimed in one of claims 1, 2 and 4-11, characterized in that it 25 comprises the following stages: a) culture in a medium and appropriate culture conditions of a cell as claimed in claim 14; and b) the recovery of said antibodies, or one of their functional divalent fragments, thus produced starting from the culture medium or said cultured cells. 17. The antibody of claims 1, 2 and 4-11, or obtained by the process of claim 16, as a medicament. 18. A pharmaceutical conlposition comprising by way of active principle a compound consisting of an antibody, or one of i t s functional divalent fragments, as claimed 5 in one of claims 1, 2 and 4-1 1, or obtained by the process of claim 16. 19. The composition of claim 18, characterized in that it comprises, moreover, as a combination product for simultaneous, separate or sequential use, a cytotoxic/cytostatic agent. 20. The composition of claim 19, characterized in that said cytotoxic or cytostatic 10 agent i s coupled chemically to said antibody. 21. The composition of claim 19 or 20, wherein said cytotoxic agent is selected in the group consisting of alkylating agents, anti-metabolites, anti-tumor antibiotics, mitotic inhibitors, chromatin function inhibitors, anti-angiogenesis agents, antiestrogenic agents, anti-androgen agents or immunomodulators. 15 22. The composition of claim 21, wherein said cytotoxic agent is a mitotic inhibitor. 23. A method of in vitro diagnosis of illnesses induced by an overexpression or an underexpression of the c-Met receptor starting from a biological sample in which the abnormal presence of c-Met receptor is suspected, characterized in that said method comprises: 20 a) a step wherein said biological sample i s contacted with an antibody of claims 1, 2 and 4-11, or obtained by the process of claim 16, or of an antibody produced by hybridoma of claim 3, it being possible for said antibody to be, i f necessary, Labeled; and b) a step wherein the overexpression or an underexpression of the c-Met receptor 25 i s determined by the demonstration of the c-Metlantibody complex formed in step a).