Cloning of anti-MMP-2 human antibodies from semisynthetic phage antibody library
- VernacularTitle:从半合成噬菌体抗体库筛选基质金属蛋白酶-2人抗体
- Author:
Xiuyun DING
;
Yan WANG
;
Bing HUA
;
Al ET
- Publication Type:Journal Article
- Keywords:
Semisynthetic antibody library Matrix metalloproteinase 2 Human antibody
- From:
Chinese Journal of Immunology
2000;0(08):-
- CountryChina
- Language:Chinese
-
Abstract:
Objective:To clone human anti MMP 2 antibodies from semisynthetic phage antibody library.Methods:Panning of semisynthetic phage antibody library against recombinant human MMP 2 was conducted to select specific antibodies.The antigen binding characterastics were analyzed by ELISAs.Results:MMP 2 binding phage antibody clones were obtanied after four rounds of panning,but they all showed binding activity to unrelated ags tested.One clone,AD20,was chosen for further analysis by competitive ELISA.It was found that the binding of AD20 to MMP 2 could be inhibited only by free MMP 2 but not unrelated Ags,while the binding to other Ags could not be inhibited by Ags tested,including MMP 2.Neutralization test demonstrated that AD20 could neutralize the enzymatic activity of MMP 2.Conclusion:A neutralizing human antibody against MMP 2 was obtained from a semisynthetic phage antibody library,which shows bindings with unrelated Ags nonspecifically that may be caused by different binding modes,a phenomenon termed polyreactivity.
