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Article

Myristoylation of the poliovirus polyprotein is required for proteolytic processing of the capsid and for viral infectivity.

Journal of virology - 1 May 1990

Kräusslich H G, Hölscher C, Reuer Q, Harber J, Wimmer E

Abstract excerpt

The poliovirus polyprotein is cotranslationally linked to myristic acid at its amino-terminal glycine residue. We investigated the role of myristoylation in the viral replication cycle by site-directed mutagenesis of this glycine codon. Synthetic full-length RNA transcripts carrying a Gly-to-Ala...

Topics

Alanine
Capsid
Codon
Glycine
HeLa Cells
Humans
Mutation
Myristic Acid
Myristic Acids
Poliovirus
Protein Biosynthesis
Protein Processing, Post-Translational

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Transcription, Genetic

Virulence

Virus Replication

Source

Open in PubMed Open full text

Identifiers

PMID: 2157900
DOI: 10.1128/JVI.64.5.2433-2436.1990
PMCID: PMC249411

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026. Prepared record publication-2157900-2026-08-30.1. Manifest publication-graph-cohort-2026-08-30.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 30 Aug 2026.

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Myristoylation of the poliovirus polyprotein is required for proteolytic processing of the capsid and for viral infectivity.PMID 2157900Read ↗

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