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Mass spectrometry analysis of influenza virus reassortant clones does not reveal an influence of other viral proteins on S-acylation of hemagglutinin

tetano

Editor, Senior Moderator
Arch Virol. 2012 Oct 12. [Epub ahead of print]
Mass spectrometry analysis of influenza virus reassortant clones does not reveal an influence of other viral proteins on S-acylation of hemagglutinin.
Serebryakova MV, Kordyukova LV, Rudneva IA, Kropotkina EA, Veit M, Baratova LA.
Source

Belozersky Institute of Physico-Chemical Biology, Lomonosov Moscow State University, Leninskie Gory 1, Bldg. 40, 119991, Moscow, Russia.
Abstract

Hemagglutinin (HA) of influenza virus is S-acylated with stearate at a transmembrane cysteine and with palmitate at two cytoplasmic cysteines. The amount of stearate varies from 35 (in avian strains) to 12% (in human strains), although the acylation region exhibits only minor or even no amino acid differences between HAs. To address whether matrix proteins and neuraminidase affect stearoylation of HA, we used mass spectrometry to analyze laboratory reassortants containing avian virus HA and the internal proteins from a human virus. Only minor fluctuations in the amount of stearate were observed, implying that other viral proteins do not affect acylation of HA.

PMID:
23065113
[PubMed - as supplied by publisher]

http://www.ncbi.nlm.nih.gov/pubmed/23065113
 
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