IDENTIFICATION OF A 5TH NEUTRALIZABLE SITE ON TYPE-O FOOT-AND-MOUTH-DISEASE VIRUS FOLLOWING CHARACTERIZATION OF SINGLE AND QUINTUPLE MONOCLONAL-ANTIBODY ESCAPE MUTANTS

被引:158
作者
CROWTHER, JR [1 ]
FARIAS, S [1 ]
CARPENTER, WC [1 ]
SAMUEL, AR [1 ]
机构
[1] FED UNIV PORTO ALEGRE,DEPT PHYSIOL,CTR BIOTECHNOL,PORTO ALEGRE,BRAZIL
关键词
D O I
10.1099/0022-1317-74-8-1547
中图分类号
Q81 [生物工程学(生物技术)]; Q93 [微生物学];
学科分类号
071005 ; 0836 ; 090102 ; 100705 ;
摘要
A monoclonal antibody (C3) produced against foot-and-mouth disease virus type O1Caseros was found to neutralize quadrivalent monoclonal antibody escape mutant (G67) of foot-and-mouth disease virus type O1Kaufbeuren. This mutant had been characterized at the sequence level as having distinct changes affecting four non-overlapping neutralizable sites. The C3 monoclonal antibody was used to prepare a quintuple escape mutant from the G67 and a single escape mutant from the parental O1Kaufbeuren viruses. Polyclonal postvaccinated and infected cattle sera as well as polyclonal mouse and guinea-pig sera, which neutralized the quadrivalent mutant, no longer neutralized the quintuple mutant, indicating that a fifth site had been identified and that changing the fifth site eliminated all neutralization. The site was characterized using serological techniques and found to be conformationally dependent, trypsin-sensitive and independent of sites previously characterized by monoclonal antibodies. Amino acid sequencing comparing parental, single C3 and quintuple mutants showed that a single change from a glutamine to a histidine, at amino acid 149 in the structural protein VP1. (1D) characterized the C3 mutation. The fifth site probably represents a conformational epitope which is formed due to the interaction of the VP1 loop region with other surface amino acids.
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页码:1547 / 1553
页数:7
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