Document Detail


Molecular basis of viral persistence: a single amino acid change in the glycoprotein of lymphocytic choriomeningitis virus is associated with suppression of the antiviral cytotoxic T-lymphocyte response and establishment of persistence.
MedLine Citation:
PMID:  1840619     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Isolates of lymphocytic choriomeningitis virus (LCMV) that elicit a cytotoxic T-lymphocyte response (CTL+) have been compared with isolates that suppress the CTL response (CTL-) in an effort to map this phenotype. A single amino acid change in the glycoprotein of the LCMV Armstrong (ARM) strain is consistently associated with the CTL- trait and the ability of the virus to persist (P+). The CTL+ P- parental strain spontaneously gives rise to CTL- P+ variants within lymphoid tissues of mice persistently infected from birth. To map the structural basis of the phenotype, the complete RNA sequence of LCMV ARM 53b (CTL+) was compared with that of its variant ARM clone 13 (CTL-). Differences in 5 of 10,600 nucleotides were found. Three changes are noted in the large L RNA segment, and two are noted in the small S RNA segment. Only two of the changes distinguishing CTL+ from CTL- isolates affect amino acid coding: lysine to glutamine at amino acid 1079 of the polymerase protein, and phenylalanine to leucine at amino acid 260 of the envelope glycoprotein (GP). We also analyzed two additional CTL- variants and four spontaneous CTL+ revertants. All three CTL- variants differ from the original CTL+ parental strain at GP amino acid 260, indicating that this amino acid change is consistently associated with the CTL- phenotype. By contrast the other four mutations in LCMV are not associated with the CTL- phenotype. Sequence analysis of the coding regions of four CTL+ revertants of ARM clone 13 did not reveal back mutations at the GP 260 locus. This finding indicates that the GP 260 mutation is necessary but not sufficient for a CTL- P+ phenotype and that the reversion to CTL+ P- is likely either due to secondary mutations in other regions of the viral genome or to quasispecies within the revertant population that make significant contributions to the phenotype.
Authors:
M Salvato; P Borrow; E Shimomaye; M B Oldstone
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  Journal of virology     Volume:  65     ISSN:  0022-538X     ISO Abbreviation:  J. Virol.     Publication Date:  1991 Apr 
Date Detail:
Created Date:  1991-04-17     Completed Date:  1991-04-17     Revised Date:  2009-11-18    
Medline Journal Info:
Nlm Unique ID:  0113724     Medline TA:  J Virol     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  1863-9     Citation Subset:  IM    
Affiliation:
Department of Neuropharmacology, Scripps Clinic and Research Foundation, La Jolla, California 92037.
Data Bank Information
Bank Name/Acc. No.:
GENBANK/J04331;  M20869;  M27693;  M61066;  M61067;  M61068;  M61069;  M61070;  M61071;  M64449;  M64450;  M64451;  M64452
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MeSH Terms
Descriptor/Qualifier:
Amino Acid Sequence
Animals
Base Sequence
Clone Cells / microbiology
Cricetinae
Glycoproteins / chemistry,  genetics*
Lymphocytic Choriomeningitis / genetics
Lymphocytic choriomeningitis virus / genetics*
Mice
Mice, Inbred BALB C
Molecular Sequence Data
Mutation
Phenotype
RNA, Viral / chemistry*
Recurrence
T-Lymphocytes, Cytotoxic / immunology*,  microbiology
Viral Envelope Proteins / chemistry,  genetics*
Grant Support
ID/Acronym/Agency:
AG-04342/AG/NIA NIH HHS; AI-09484/AI/NIAID NIH HHS; AI-25522/AI/NIAID NIH HHS
Chemical
Reg. No./Substance:
0/Glycoproteins; 0/RNA, Viral; 0/Viral Envelope Proteins
Comments/Corrections

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