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 functi...

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Veröffentlicht in:Biochemical and biophysical research communications 2007-03, Vol.354 (1), p.115-121
Hauptverfasser: Kim, Kisu, Hur, Youngmi, Ryu, En-Kyung, Rhim, Jung-Hyo, Choi, Cha Yong, Baek, Cheol-Min, Lee, Jae-Ho, Chung, Junho
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Sprache:eng
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Zusammenfassung: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.
ISSN:0006-291X
1090-2104
DOI:10.1016/j.bbrc.2006.12.164