       Document 0115
 DOCN  M9630115
 TI    Analysis of the cell fusion activities of chimeric simian
       immunodeficiency virus-murine leukemia virus envelope proteins:
       inhibitory effects of the R peptide.
 DT    9603
 AU    Yang C; Compans RW; Department of Microbiology and Immunology, Emory
       University; School of Medicine, Atlanta, Georgia 30322, USA.
 SO    J Virol. 1996 Jan;70(1):248-54. Unique Identifier : AIDSLINE
       MED/96099437
 AB    It was previously reported that truncation or proteolytic removal of the
       C-terminal 16 amino acids (the R peptide) from the cytoplasmic tail of
       the murine leukemia virus (MuLV) envelope protein greatly increases its
       fusion activity. In this study, to investigate the specificity of the
       effect of the R peptide on the fusion activity of viral envelope
       proteins, we expressed simian immunodeficiency virus (SIV)-MuLV chimeric
       proteins in which the entire cytoplasmic tail of the SIV envelope
       protein was replaced by either the full-length MuLV cytoplasmic tail or
       a truncated MuLV cytoplasmic tail with the R peptide deleted. Extensive
       fusion of CD4-positive cells with the chimeric protein containing a
       truncated MuLV cytoplasmic tail was observed. In contrast, no cell
       fusion activity was found for the chimeric protein with a full-length
       MuLV cytoplasmic tail. We constructed another SIV-MuLV chimeric protein
       in which the MuLV R peptide was added to an SIV envelope protein
       cytoplasmic tail 17 amino acids from its membrane-spanning domain. No
       fusion activity was observed within this construct, while the
       corresponding truncated SIV envelope protein lacking the R peptide
       showed extensive fusion activity. No significant difference in the
       transport or surface expression was observed among the various SIV-MuLV
       chimeric proteins and the truncated SIV envelope protein. Our results
       thus demonstrate that the MuLV R peptide has profound inhibitory effects
       on virus-induced cell fusion, not only with MuLV but also in a distantly
       related retroviral envelope protein which utilizes a different receptor
       and fuses different cell types.
 DE    Amino Acid Sequence  Base Sequence  Cell Membrane/METABOLISM  Chimeric
       Proteins/METABOLISM  DNA, Recombinant  DNA, Viral  Friend
       Virus/GENETICS/*METABOLISM  Hela Cells  Human  Membrane
       Fusion/*PHYSIOLOGY  Molecular Sequence Data  Peptide
       Fragments/GENETICS/METABOLISM  Retroviridae Proteins,
       Oncogenic/GENETICS/METABOLISM  Support, U.S. Gov't, P.H.S.
       SIV/GENETICS/*METABOLISM  Viral Envelope Proteins/GENETICS/*METABOLISM
       JOURNAL ARTICLE

       SOURCE: National Library of Medicine.  NOTICE: This material may be
       protected by Copyright Law (Title 17, U.S.Code).

