Publications & Reports

Expression and biochemical analysis of the entire HIV-2 gp41 ectodomain: determinants of stability map to N- and C-terminal sequences outside the 6-helix bundle core.

Chan-Sien Lay, Kirilee A Wilson, Bostjan Kobe, Bruce E Kemp, Heidi E Drummer, Pantelis Poumbourios
St. Vincent's Institute of Medical Research, and Department of Microbiology and Immunology, University of Melbourne, Victoria, Australia.


The folding of HIV gp41 into a 6-helix bundle drives virus-cell membrane fusion. To examine the structural relationship between the 6-helix bundle core domain and other regions of gp41, we expressed in Escherichia coli, the entire ectodomain of HIV-2(ST) gp41 as a soluble, trimeric maltose-binding protein (MBP)/gp41 chimera. Limiting proteolysis indicated that the Cys-591-Cys-597 disulfide-bonded region is outside a core domain comprising two peptides, Thr-529-Trp-589 and Val-604-Ser-666. A biochemical examination of MBP/gp41 chimeras encompassing these core peptides indicated that the N-terminal polar segment, 521-528, and C-terminal membrane-proximal segment, 658-666, cooperate in stabilizing the ectodomain. A functional interaction between sequences outside the gp41 core may contribute energy to membrane fusion.


  • Journal: FEBS letters
  • Published: 04/06/2004
  • Volume: 567
  • Issue: 2-3
  • Pagination: 183-188