ANTIBODY RAISED AGAINST SOLUBLE CD4-RGP120 COMPLEX RECOGNIZES THE CD4 MOIETY AND BLOCKS MEMBRANE-FUSION WITHOUT INHIBITING CD4-GP120 BINDING

被引：83

作者：

CELADA, F

CAMBIAGGI, C

MACCARI, J

BURASTERO, S

GREGORY, T

PATZER, E

PORTER, J

MCDANAL, C

MATTHEWS, T

机构：

[1] GENENTECH INC,DEPT RECOVERY PROC,S SAN FRANCISCO,CA 94080

[2] UNIV GENOA,DEPT IMMUNOL,I-16132 GENOA,ITALY

[3] NYU,DEPT PATHOL,NEW YORK,NY 10003

[4] GENENTECH INC,DEPT RES & DEV,S SAN FRANCISCO,CA 94080

[5] DUKE UNIV,MED CTR,DEPT SURG,DURHAM,NC 27710

[6] GENENTECH INC,DEPT MED & ANALYT CHEM,S SAN FRANCISCO,CA 94080

来源：

JOURNAL OF EXPERIMENTAL MEDICINE | 1990年 / 172卷 / 04期

关键词：

D O I：

10.1084/jem.172.4.1143

中图分类号：

R392 [医学免疫学]; Q939.91 [免疫学];

学科分类号：

100102 ;

摘要：

We studied the humoral response of mice immunized with soluble CD4-rgpl20 complex, testing polyclonal and monoclonal antibodies (mAbs) with the aim of identifying molecular changes that take place after the first interaction between human immunodeficiency virus and the cell surface. The antisera had a paradoxically high syncytia-blocking titer associated with anti-CD4 specificity, while their capacity to inhibit CD4-gpl20 binding was relatively modest. One of the mAbs produced from these responders blocks syncytia formation but does not inhibit CD4 interaction with gpl20. Apparently, this mAb interacts with the CD4 moiety of CD4-gpl20 complex and prevents a post-binding event necessary for membrane fusion and viral infection. © 1990, Rockefeller University Press., All rights reserved.

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页码：1143 / 1150

页数：8

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