Cytoplasmic tail of Moloney murine leukemia virus envelope protein influences the conformation of the extracellular domain: implications for mechanism of action of the R Peptide

Hector C Aguilar; W French Anderson; Paula M Cannon

doi:10.1128/JVI.77.2.1281-1291.2003

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Cytoplasmic tail of Moloney murine leukemia virus envelope protein influences the conformation of the extracellular domain: implications for mechanism of action of the R Peptide

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Cytoplasmic tail of Moloney murine leukemia virus envelope protein influences the conformation of the extracellular domain: implications for mechanism of action of the R Peptide

Hector C Aguilar, W French Anderson and Paula M Cannon

Journal of virology, Vol.77(2), pp.1281-1291

01/2003

DOI: https://doi.org/10.1128/JVI.77.2.1281-1291.2003

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https://hdl.handle.net/2376/115483

PMCID: PMC140788

PMID: 12502845

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https://doi.org/10.1128/JVI.77.2.1281-1291.2003View

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Abstract

Amino Acid Sequence

Cell Line

Animals

Humans

Viral Envelope Proteins - chemistry

Viral Envelope Proteins - metabolism

Molecular Sequence Data

Cytoplasm - metabolism

Protein Conformation

Mice

Moloney murine leukemia virus - metabolism

The envelope (Env) protein of Moloney murine leukemia virus (MoMuLV) is a homotrimeric complex whose monomers consist of linked surface (SU) and transmembrane (TM) proteins cleaved from a precursor protein by a cellular protease. In addition, a significant fraction of virion-associated TM is further processed by the viral protease to remove the C-terminal 16 amino acids of the cytoplasmic domain, the R peptide. This cleavage greatly enhances the fusogenicity of the protein and is necessary for the formation of a fully functional Env protein complex. We have previously proposed that R peptide cleavage enhances fusogenicity by altering the conformation of the ectodomain of the protein (Y. Zhao et al., J. Virol. 72:5392-5398, 1998). Using a series of truncation and point mutants of MoMuLV Env, we now provide direct biochemical and immunological evidence that the cytoplasmic tail and the membrane-spanning region of Env can influence the overall structure of the ectodomain of the protein and alter the strength of the SU-TM interaction. The R-peptide-truncated form of the protein, in particular, exhibits a markedly different conformation than the full-length protein.

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Title: Cytoplasmic tail of Moloney murine leukemia virus envelope protein influences the conformation of the extracellular domain: implications for mechanism of action of the R Peptide
Creators: Hector C Aguilar - Gene Therapy Laboratories, Keck School of Medicine, University of Southern California, Los Angeles 90033, USA
W French Anderson
Paula M Cannon
Publication Details: Journal of virology, Vol.77(2), pp.1281-1291
Academic Unit: Paul G. Allen School for Global Animal Health
Publisher: United States
Grant note: P01 CA059318 / NCI NIH HHS CA59318-08 / NCI NIH HHS
Identifiers: 99900547536001842
Language: English
Resource Type: Journal article