Mass spectrometry analysis of influenza virus reassortant clones does not reveal an influence of other viral proteins on S-acylation of hemagglutinin.
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.
Belozersky Institute of Physico-Chemical Biology, Lomonosov Moscow State University, Leninskie Gory 1, Bldg. 40, 119991, Moscow, Russia.
Marina V
MV
Serebryakova
Larisa V
LV
Kordyukova
Irina A
IA
Rudneva
Ekaterina A
EA
Kropotkina
Michael
M
Veit
Lyudmila A
LA
Baratova
D000215:Acylation; D019267:Hemagglutinin Glycoproteins, Influenza Virus / Q000737:chemistry* / Q000378:metabolism; D006801:Humans; D013058:Mass Spectrometry; D009975:Orthomyxoviridae / Q000737:chemistry*; D010168:Palmitates / Q000032:analysis*; D011499:Protein Processing, Post-Translational; D016865:Reassortant Viruses / Q000737:chemistry*; D013228:Stearates / Q000032:analysis*
D019267:Hemagglutinin Glycoproteins, Influenza Virus; D010168:Palmitates; D013228:Stearates