title: R-Peptide cleavage potentiates fusion-controlling isomerization of the intersubunit disulfide in Moloney murine leukemia virus Env.
abstract: 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.
authors: Department of Biosciences and Nutrition, Karolinska Institute, S-141 57 Huddinge, Sweden.
authors: Robin
authors: R
authors: Löving
authors: Kejun
authors: K
authors: Li
authors: Michael
authors: M
authors: Wallin
authors: Mathilda
authors: M
authors: Sjöberg
authors: Henrik
authors: H
authors: Garoff
mesh_terms: D000818:Animals; D004220:Disulfides / Q000737:chemistry / Q000378:metabolism*; D015686:Gene Products, env / Q000737:chemistry / Q000378:metabolism*; D006868:Hydrolysis; D007536:Isomerism; D008561:Membrane Fusion; D008979:Moloney murine leukemia virus; D009154:Mutation; D009363:Neoplasm Proteins / Q000378:metabolism*; D010455:Peptides / Q000378:metabolism*
chemical_list: D004220:Disulfides; D015686:Gene Products, env; D009363:Neoplasm Proteins; D010455:Peptides