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Journal of Virology, March 2008, p. 2594-2597, Vol. 82, No. 5
0022-538X/08/$08.00+0     doi:10.1128/JVI.02039-07
Copyright © 2008, American Society for Microbiology. All Rights Reserved.

R-Peptide Cleavage Potentiates Fusion-Controlling Isomerization of the Intersubunit Disulfide in Moloney Murine Leukemia Virus Env{triangledown}

Robin Löving, Kejun Li, Michael Wallin, Mathilda Sjöberg, and Henrik Garoff*

Department of Biosciences and Nutrition, Karolinska Institute, S-141 57 Huddinge, Sweden

Received 14 September 2007/ Accepted 12 December 2007

Fusion of the membrane of the Moloney murine leukemia virus (Mo-MLV) Env protein is facilitated by cleavage of the R peptide from the cytoplasmic tail of its TM subunit, but the mechanism for this effect has remained obscure. The fusion is also controlled by the isomerization of the intersubunit disulfide of the Env SU-TM complex. In the present study, we used several R-peptide-cleavage-inhibited virus mutants to show that the R peptide suppresses the isomerization reaction in both in vitro and in vivo assays. Thus, the R peptide affects early steps in the activation pathway of murine leukemia virus Env.

* Corresponding author. Mailing address: Department of Biosciences and Nutrition, Karolinska Institute, S-141 57 Huddinge, Sweden. Phone: 46-8-6089125. Fax: 46-8-7745538. E-mail: henrik.garoff{at}cbt.ki.se

{triangledown} Published ahead of print on 19 December 2007.

Journal of Virology, March 2008, p. 2594-2597, Vol. 82, No. 5
0022-538X/08/$08.00+0     doi:10.1128/JVI.02039-07
Copyright © 2008, American Society for Microbiology. All Rights Reserved.





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