Document Detail

Analysis of mutations within the cytoplasmic domain of the Moloney murine leukemia virus transmembrane protein.
MedLine Citation:
PMID:  9018129     Owner:  NLM     Status:  MEDLINE    
The role of the cytoplasmic tail of the Moloney murine leukemia virus transmembrane protein in the regulation of syncytia was examined. Three mutations within the cytoplasmic tail were studied. Linker-insertion in7705-12a is within the viral-associated cytoplasmic tail, linker-insertion in7748-12a is within the R peptide, and a third mutation expresses TM lacking the R peptide (Env R-). The Env R- construct was nonviable in Rat1 cells, however, rapidly reverted to a form containing the R peptide when passaged in NIH/3T3 cells. in7705-12a was temperature-sensitive in Rat1 cells, as previously characterized, but was viable at either temperature in NIH/3T3 cells. in7748-12a was comparable with wild-type M-MuLV. The ability of the env constructs to form large multinucleated syncytia with NIH/3T3 and XC cells were examined using transient expression assays, eliminating reversion events due to viral passage and reverse transcription. The Env R- constructs formed syncytia with NIH/3T3 cells. in7705-12a displays enhanced proteolytic cleavage of the R peptide. Neither linker-insertion mutation in7705-12a or in7748-12a activated fusion with NIH/3T3, despite the abundance of processed TM with in7705-12a. All three mutants were fusion competent with Rat XC cells, even in the absence of any cleavage of the R peptide. These results provide insights regarding steric and the temporal affects of cleavage of the R peptide and the assembly of a fusion competent oligomer.
A Thomas; K D Gray; M J Roth
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Publication Detail:
Type:  Journal Article; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  Virology     Volume:  227     ISSN:  0042-6822     ISO Abbreviation:  Virology     Publication Date:  1997 Jan 
Date Detail:
Created Date:  1997-03-04     Completed Date:  1997-03-04     Revised Date:  2007-11-14    
Medline Journal Info:
Nlm Unique ID:  0110674     Medline TA:  Virology     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  305-13     Citation Subset:  IM; X    
Department of Biochemistry, University of Medicine and Dentistry of New Jersey, Robert Wood Johnson Medical School, Piscataway 08854, USA.
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MeSH Terms
3T3 Cells
Cell Line
DNA Primers
Gene Deletion*
Genes, env*
Giant Cells
Moloney murine leukemia virus / genetics*,  physiology
Mutagenesis, Insertional*
Polymerase Chain Reaction
Proviruses / genetics,  physiology
Recombinant Proteins / biosynthesis
Retroviridae Proteins, Oncogenic / biosynthesis,  genetics*
Viral Envelope Proteins / biosynthesis,  genetics*
Viral Proteins / biosynthesis,  isolation & purification
Virus Replication
Grant Support
Reg. No./Substance:
0/DNA Primers; 0/Recombinant Proteins; 0/Retroviridae Proteins, Oncogenic; 0/Viral Envelope Proteins; 0/Viral Proteins; 0/p15E protein, Murine leukemia virus

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