Journal of Virology, October 2006, p. 9921-9925, Vol. 80, No. 19
0022-538X/06/$08.00+0 doi:10.1128/JVI.00380-06
Copyright © 2006, American Society for Microbiology. All Rights Reserved.
Department of Biosciences at Novum, Karolinska Institute, S-141 57 Huddinge, Sweden
Received 23 February 2006/ Accepted 14 July 2006
A central feature of the prevailing model for retrovirus fusion is conversion of the transmembrane (TM) subunit from a prehairpin to a hairpin-like structure. The fusion inhibition of many retroviruses, except murine leukemia virus (MLV), with peptides corresponding to interacting regions in the hairpin supports the model. MLV fusion is controlled by isomerization of the intersubunit disulfide in Env. We show here that TM peptides bind to MLV Env that has been arrested at an intermediate stage of activation by alkylation of the isomerization-active thiol in the surface subunit. This inhibits fusion rescue by dithiothreitol-mediated reduction of the surface protein-TM disulfide.
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