Document Detail


Temperature-sensitive lesions in the capsid proteins of the rotavirus mutants tsF and tsG that affect virion assembly.
MedLine Citation:
PMID:  8091686     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
The SA11 rotavirus mutants tsF and tsG contain temperature sensitive (ts) lesions in the capsid proteins VP2 and VP6, respectively, that interfere with their ability to assemble. To understand the nature of their lesions, full-length cDNAs of tsF gene 2 and tsG gene 6 were prepared from viral mRNA by reverse transcription and polymerase chain reaction. Comparative sequence analysis indicated that the ts phenotype of tsF VP2 is due to an Ala-->Asp substitution at position 387. The mutation falls outside of those regions of VP2 previously suggested to be of functional significance and therefore points to a previously unidentified site in VP2 that is important for the assembly of viral cores. Comparative sequence analysis showed that tsG VP6 contains two mutant amino acids, i.e., Thr-10 and His-13, and therefore one or both of these mutations are responsible for the ts phenotype of the mutant VP6. In the case of other group A and group C VP6 sequences, these residues are Ser and Asp, respectively. Characterization of tsG-infected cells by indirect immunofluorescence staining showed that while viroplasmic inclusions are formed at the nonpermissive temperature, the mutant VP6 accumulates in these structures only at the permissive temperature. While influencing intracellular accumulation, the Thr-10-->Ser and His-13-->Asp mutations in tsG VP6 are probably not directly involved in the interaction of VP6 with VP2, as VP6 deletion mutants lacking residues 10 and 13 retain the ability to bind VP2 in vitro. Analysis of VP6 failed to confirm previous reports that the protein was myristylated and thus excludes the possibility that this cotranslational modification is temperature-dependent for tsG VP6. Together, these data suggest that the amino terminus of VP6 plays an essential role in virus assembly in vivo, perhaps by being necessary for the movement of the protein to viroplasmic inclusions, the site of core and single-shelled particle formation.
Authors:
E A Mansell; R F Ramig; J T Patton
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Publication Detail:
Type:  Journal Article; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  Virology     Volume:  204     ISSN:  0042-6822     ISO Abbreviation:  Virology     Publication Date:  1994 Oct 
Date Detail:
Created Date:  1994-10-20     Completed Date:  1994-10-20     Revised Date:  2007-11-14    
Medline Journal Info:
Nlm Unique ID:  0110674     Medline TA:  Virology     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  69-81     Citation Subset:  IM    
Affiliation:
Department of Microbiology and Immunology, University of Miami School of Medicine, Florida 33101.
Data Bank Information
Bank Name/Acc. No.:
GENBANK/D00326;  L15384;  L33365
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MeSH Terms
Descriptor/Qualifier:
Amino Acid Sequence
Antigens, Viral*
Base Sequence
Capsid / chemistry,  genetics*,  metabolism
Capsid Proteins
Cell Line
DNA, Complementary / analysis
Inclusion Bodies, Viral / metabolism
Molecular Sequence Data
Mutation / genetics*
Myristic Acid
Myristic Acids / metabolism
Protein Processing, Post-Translational
Protein Structure, Secondary
RNA, Messenger / analysis
RNA, Viral / analysis
Rotavirus / genetics*,  growth & development
Temperature
Virion / growth & development*
Grant Support
ID/Acronym/Agency:
A100990//PHS HHS; A121478//PHS HHS; AI16687/AI/NIAID NIH HHS
Chemical
Reg. No./Substance:
0/Antigens, Viral; 0/Capsid Proteins; 0/DNA, Complementary; 0/Myristic Acids; 0/RNA, Messenger; 0/RNA, Viral; 0/VP2 protein, Rotavirus; 0/VP6 protein, Rotavirus; 544-63-8/Myristic Acid

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


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