Mammalian reoviruses contain a myristoylated structural protein

Max L. Nibert, Leslie A. Schiff, Bernard N. Fields

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Abstract

The structural protein μ1 of mammalian reoviruses was noted to have a potential N-myristoylation sequence at the amino terminus of its deduced amino acid sequence. Virions labeled with [3H]myristic acid were used to demonstrate that μ1 is modified by an amide-linked myristoyl group. A myristoylated peptide having a relative molecular weight (Mr) of ∼4,000 was also shown to be a structural component of virions and was concluded to represent the 4.2-kDa amino-terminal fragment of μ1 which is generated by the same proteolytic cleavage that yields the carboxy-terminal fragment and major outer capsid protein μ1C. The myristoylated 4,000-Mr peptide was found to be present in reovirus intermediate subviral particles but to be absent from cores, indicating that it is a component of the outer capsid. A distinct large myristoylated fragment of the intact μ1 protein was also identified in intermediate subviral particles, but no myristoylated μ-region proteins were identified in cores, consistent with the location of μ1 in the outer capsid. Similarities between amino-terminal regions of the reovirus μ1 protein and the poliovirus capsid polyprotein were noted. By analogy with other viruses that contain N-myristoylated structural proteins (particularly picornaviruses), we suggest that the myristoyl group attached to μ1 and its amino-terminal fragments has an essential role in the assembly and structure of the reovirus outer capsid and in the process of reovirus entry into cells.

Original languageEnglish (US)
Pages (from-to)1960-1967
Number of pages8
JournalJournal of virology
Volume65
Issue number4
StatePublished - 1991

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