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PMID:1851815

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Citation

Marc, D, Girard, M and van der Werf, S (1991) A Gly1 to Ala substitution in poliovirus capsid protein VP0 blocks its myristoylation and prevents viral assembly. J. Gen. Virol. 72 ( Pt 5):1151-7

Abstract

Capsid protein VP4 of poliovirus is acylated with myristic acid via an amide linkage to its N-terminal glycine residue. Our previous studies suggested that myristic acid plays a role in poliovirus assembly and in the early events of infection. In order to understand better its role in the assembly process, we introduced a Gly1 to Ala amino acid substitution in the myristoylation signal sequence of VP4. This substitution prevented VP0 myristoylation in vivo and abolished the infectivity of genomic transcripts harbouring the mutation. These mutated RNAs were still able to replicate in the transfected cells but the assembly processes were inefficient and no mature virions could be detected.

Links

PubMed Online version:10.1099/0022-1317-72-5-1151

Keywords

Alanine/genetics; Amino Acid Sequence; Base Sequence; Capsid/genetics; Capsid/metabolism; Capsid Proteins; Electrophoresis, Polyacrylamide Gel; Glycine/genetics; HeLa Cells; Humans; Molecular Sequence Data; Mutation; Myristates/metabolism; Poliovirus/pathogenicity; Poliovirus/physiology; Transcription, Genetic; Transfection; Virion/analysis; Virus Replication

Significance

Annotations

Gene product Qualifier GO Term Evidence Code with/from Aspect Extension Notes Status

POL1M:POLG

part_of

GO:0019028: viral capsid

ECO:0000314: direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

POL1M:POLG

involved_in

GO:0019068: virion assembly

ECO:0000314: direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

Notes

See also

References

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