Insertion of influenza M protein into the viral lipid bilayer and localization of site of insertion.
AUTOR(ES)
Gregoriades, A
RESUMO
Recent studies with isolated M protein from influenza virus have shown that the protein has a high affinity for lipid. The ability of M to partition into lipid vesicles merely by shaking vesicles and M together is suggestive evidence that the protein could be interacting with the lipid in the virus particle. A more direct analysis was carried our here to determine whether M is in contact with the viral lipid in situ, by using the photoactivatable hydrophobic probe, pyrenesulfonyl azide. Covalent linkage of this probe to M indicated that a segment of M residues with in the virus membrane in contact with the lipid bilayer. M inserted into lipid vesicles at two locations on the molecule. A major insertion into lipid occurred in the middle of the molecule where a large cluster of 20 hydrophobic and neutral amino acids occurs. A second insertion occurred approximately one fourth in from the amino terminus, where a smaller segment of 13 uncharged amino acids is found. Confirmation that M inserted into lipid at these locations came also from results with cyanogen bromide fragments of M. Of the 12 to 13 fragments produced, 3 specifically bound to lipid vesicles. These were the first, second, and third contiguous segments beginnings at the amino terminus and containing the two hydrophobic areas noted above.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=256625Documentos Relacionados
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