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Journal of Virology, September 2008, p. 9288-9292, Vol. 82, No. 18
0022-538X/08/$08.00+0 doi:10.1128/JVI.00704-08
Copyright © 2008, American Society for Microbiology. All Rights Reserved.

A. N. Belozersky Institute of Physico-Chemical Biology, Moscow State University, Moscow 119991, Russia,1 Institute of Physico-Chemical Medicine, Federal Agency for Health Care and Social Development, Moscow 119992, Russia,2 Immunology and Molecular Biology, Faculty of Veterinary Medicine, Free University Berlin, Berlin, Germany3
Received 28 March 2008/ Accepted 27 June 2008
S acylation of cysteines located in the transmembrane and/or cytoplasmic region of influenza virus hemagglutinins (HA) contributes to the membrane fusion and assembly of virions. Our results from using mass spectrometry (MS) show that influenza B virus HA possessing two cytoplasmic cysteines contains palmitate, whereas HA-esterase-fusion glycoprotein of influenza C virus having one transmembrane cysteine is stearoylated. HAs of influenza A virus having one transmembrane and two cytoplasmic cysteines contain both palmitate and stearate. MS analysis of recombinant viruses with deletions of individual cysteines, as well as tandem-MS sequencing, revealed the surprising result that stearate is exclusively attached to the cysteine positioned in the transmembrane region of HA.
Published ahead of print on 2 July 2008.
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