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    
Abstract/OtherAbstract:
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.
Authors:
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    
Affiliation:
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
Descriptor/Qualifier:
3T3 Cells
Animals
Cell Line
DNA Primers
Gene Deletion*
Genes, env*
Giant Cells
Humans
Mice
Moloney murine leukemia virus / genetics*,  physiology
Mutagenesis, Insertional*
Polymerase Chain Reaction
Proviruses / genetics,  physiology
Rats
Recombinant Proteins / biosynthesis
Retroviridae Proteins, Oncogenic / biosynthesis,  genetics*
Viral Envelope Proteins / biosynthesis,  genetics*
Viral Proteins / biosynthesis,  isolation & purification
Virus Replication
Grant Support
ID/Acronym/Agency:
R01-CA49932/CA/NCI NIH HHS
Chemical
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

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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