Mammalian reoviruses contain a myristoylated structural protein

M. L. Nibert, L. A. Schiff, B. N. Fields

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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 (M(r)) 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 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
Issue number4
StatePublished - 1991


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