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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

Author:
Serebryakova, Marina V., Kordyukova, Larisa V., Rudneva, Irina A., Kropotkina, Ekaterina A., Veit, Michael, Baratova, Lyudmila A.
Source:
Archives of virology 2013 v.158 no.2 pp. 467-472
ISSN:
0304-8608
Subject:
Influenza A virus, acylation, birds, clones, cysteine, mass spectrometry, sialidase, stearic acid, vertebrate viruses, viral proteins
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.
Agid:
454014