PMID: 9445056Jan 28, 1998Paper

Mutation-directed chemical cross-linking of human immunodeficiency virus type 1 gp41 oligomers

Journal of Virology
T L McInerneyP Poumbourios

Abstract

The human immunodeficiency virus type 1 transmembrane protein gp41 oligomer anchors the attachment protein, gp120, to the viral envelope and mediates viral envelope-cell membrane fusion following gp120-CD4 receptor-chemokine coreceptor binding. We have used mutation-directed chemical cross-linking with bis(sulfosuccinimidyl)suberate (BS3) to investigate the architecture of the gp41 oligomer. Treatment of gp41 with BS3 generates a ladder of four bands on sodium dodecyl sulfate-polyacrylamide gels, corresponding to monomers, dimers, trimers, and tetramers. By systematically replacing gp41 lysines with arginine and determining the mutant gp41 cross-linking pattern, we observed that gp41 N termini are cross-linked. Lysine 678, which is close to the transmembrane sequence, was readily cross-linked to Lys-678 on other monomers within the oligomeric structure. This arrangement appears to be facilitated by the close packing of membrane-anchoring sequences, since the efficiency of assembly of heterooligomers between wild-type and mutant Env proteins is improved more than twofold if the mutant contains the membrane-anchoring sequence. We also detected close contacts between Lys-596 and Lys-612 in the disulfide-bonded loop/glycan cluster ...Continue Reading

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Citations

Nov 4, 2000·Expert Opinion on Investigational Drugs·C PintérA Clivio
Dec 3, 2003·The Journal of Biological Chemistry·Yui-Ping WengJung-Yaw Lin
Jun 14, 2000·Journal of Virology·J M MatthewsJ P Mackay
Jul 18, 2001·The Journal of General Virology·P KaukinenA Plyusnin
Aug 24, 1999·European Journal of Immunology·G W LynchA L Cunningham

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