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. 1982 Jun;42(3):963–968. doi: 10.1128/jvi.42.3.963-968.1982

Evidence for an interaction between the membrane protein of a paramyxovirus and actin.

R M Giuffre, D R Tovell, C M Kay, D L Tyrrell
PMCID: PMC256929  PMID: 6285006

Abstract

Evidence for an interaction of the membrane (M) protein of Newcastle disease and Sendai viruses with cellular actin was obtained by three different techniques. M protein linked to Sepharose 4B was found to bind actin, but not myoglobin or bovine serum albumin, and to selectively remove actin from a mixture of these three proteins. Sedimentation of a mixture of M protein and F-actin through a sucrose gradient resulted in sedimentation of M protein with actin. Control proteins, bovine serum albumin and cytochrome c, did not sediment with actin. In circular dichroism studies, M protein added to actin in a 1:1 complex resulted in a significant increase in negative ellipticity at 220 nm, which corresponds to an increase in alpha-helix and a decrease in beta-structure and random coil. This is indicative of an interaction between M protein and actin. It is possible that the frequent identification of cellular actin in a number of enveloped viruses may be attributed to the interaction of actin and M protein or its equivalent.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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