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.

Abstract:

: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_name

FEBS Lett

journal_title

FEBS letters

authors

Lay CS,Wilson KA,Kobe B,Kemp BE,Drummer HE,Poumbourios P

doi

10.1016/j.febslet.2004.04.054

keywords:

subject

Has Abstract

pub_date

2004-06-04 00:00:00

pages

183-8

issue

2-3

eissn

0014-5793

issn

1873-3468

pii

S0014579304005332

journal_volume

567

pub_type

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