Antibody raised against soluble CD4-rgp120 complex recognizes the CD4 moiety and blocks membrane fusion without inhibiting CD4-gp120 binding

Franco Celada, Caterina Cambiaggi, Joan Maccari, Samuele Burastero, Timothy Gregory, Eric Patzer, James Porter, Charlene McDanal, Thomas Matthews

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Abstract

We studied the humoral response of mice immunized with soluble CD4-rgp120 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-gp120 binding was relatively modest. One of the mAbs produced from these responders blocks syncytia formation but does not inhibit CD4 interaction with gp120. Apparently, this mAb interacts with the CD4 moiety of CD4-gp120 complex and prevents a post-binding event necessary for membrane fusion and viral infection.

Original languageEnglish
Pages (from-to)1143-1150
Number of pages8
JournalJournal of Experimental Medicine
Volume172
Issue number4
Publication statusPublished - Oct 1 1990

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ASJC Scopus subject areas

  • Immunology

Cite this

Celada, F., Cambiaggi, C., Maccari, J., Burastero, S., Gregory, T., Patzer, E., Porter, J., McDanal, C., & Matthews, T. (1990). Antibody raised against soluble CD4-rgp120 complex recognizes the CD4 moiety and blocks membrane fusion without inhibiting CD4-gp120 binding. Journal of Experimental Medicine, 172(4), 1143-1150.