Oligomeric structure of gp41, the transmembrane protein of human immunodeficiency virus type 1

A Pinter, W J Honnen, S A Tilley, C Bona, H Zaghouani, M K Gorny, S Zolla-Pazner
1989 Journal of Virology  
We characterized the structural forms of the human immunodeficiency virus env-encoded proteins with a panel of monoclonal and polyclonal antibodies. Western blot (immunoblot) assays with antibodies specific for gp4l invariably recognized a major component of 160 kilodaltons and a less intense component of 120 kilodaltons in viral lysates. We demonstrated that these species are noncovalently associated tetramers and trimers of gp4l which represent the native form of this protein in virions.
more » ... complexes were stable when boiled in the presence of low concentrations of sodium dodecyl sulfate but were dissociated to gp4l monomers at high sodium dodecyl sulfate concentrations. Moreover, two human monoclonal antibodies preferentially recognized the oligomeric complexes over monomeric gp4l in Western blots, indicating the presence of epitopes recognized by the human immune system on the gp4l multimers which are not efficiently expressed by the dissociated monomers. The demonstration of the existence of multimeric env complexes and the enhanced and altered antigenicity of such multimers may be relevant to the design of subunit and recombinant human immunodeficiency virus env vaccines. Structure of the influenza virus glycoprotein antigen neuramin-J. VIROL. on May 10, 2020 by guest
doi:10.1128/jvi.63.6.2674-2679.1989 fatcat:3xyprhnldrhvvlbdr7pkk756im