J Gen Virol
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J Gen Virol 75 (1994), 839-847; DOI 10.1099/0022-1317-75-4-839
© 1994 Society for General Microbiology
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Analysis of the human immunodeficiency virus type 1 envelope protein interaction with the CD4 host cell receptor

Etienne Malvoisin and Fabian Wild

Immunologie et Stratégie Vaccinale, Institut Pasteur de Lyon, Avenue Tony Garnier, 69365 Lyon Cedex 07, France

A secreted form of human immunodeficiency virus type 1 (HIV-1) envelope glycoprotein (gp160s), expressed in HeLa cells from a vaccinia virus recombinant was analysed by velocity-gradient centrifugation and chemical cross-linking. We showed that gp160s existed predominantly as a dimer, but higher forms corresponding to trimers and tetramers were also found. Soluble CD4 (sCD4) and native CD4 expressed by recombinant vaccinia viruses were analysed by sucrosegradient sedimentation alone or after complexing with gp160s. The sCD4 sedimented in sucrose gradients as a monomer, whereas after solubilization the native CD4 was in a dimeric state. Both forms of CD4 were able to form complexes when incubated with gp160s. In the case of the sCD4, the Mr corresponded to a (sCD4)2-(gp160s)2 complex, whereas with CD4 the complexes were of a greater order of magnitude. HIV gp120 was secreted into the medium in a monomeric state. With sCD4 it gave a one-to-one complex, whereas with the native CD4 high Mr complexes were formed. The importance of the oligomeric state of the virus- and cell-receptor proteins are discussed regarding their avidities.

Received 3 September 1993; accepted 1 November 1993.


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