A neutralizable epitope is induced on HGF upon its interaction with its receptor cMet.
A new conformational neutralizable epitope is created on heptocyte growth factor (HGF), when it interacts with its receptor, cMet. By immunizing rabbits with HGF-cMet complex, we successfully generated a monoclonal antibody (SFN68) that inhibits HGF-cMet interaction, and blocks the biological function mediated by HGF. To define the epitope, we screened out an epitope-mimicking peptide, KSLSRHDHIHHH, from a phage display of combinatorial peptide library. In molecular mimicry this peptide bound to cMet and inhibited HGF-cMet interaction. No humoral response was induced to this epitope-mimicking peptide when immunization was done with HGF alone.
Kim
Kisu
K
Cancer Research Institute, Seoul National University College of Medicine, 28 Yongon-Dong, Chongno-gu, Seoul, Republic of Korea.
Hur
Youngmi
Y
Ryu
En-Kyung
EK
Rhim
Jung-Hyo
JH
Choi
Cha Yong
CY
Baek
Cheol-Min
CM
Lee
Jae-Ho
JH
Chung
Junho
J
D000818:Animals; D000911:Antibodies, Monoclonal / Q000737:chemistry* / Q000276:immunology*; D018604:Epitope Mapping; D000939:Epitopes / Q000276:immunology*; D017228:Hepatocyte Growth Factor / Q000276:immunology*; D009500:Neutralization Tests; D019151:Peptide Library; D025941:Protein Interaction Mapping; D019859:Proto-Oncogene Proteins c-met / Q000276:immunology*; D011817:Rabbits
D000911:Antibodies, Monoclonal; D000939:Epitopes; D019151:Peptide Library; D017228:Hepatocyte Growth Factor; D019859:Proto-Oncogene Proteins c-met