Virion basic phosphoprotein from human cytomegalovirus contains O-linked N-acetylglucosamine.

D. M. Benko, R. S. Haltiwanger, G. W. Hart, W. Gibson

Research output: Contribution to journalArticle

Abstract

A 149-kDa virion protein of human strains of cytomegalovirus is the principal acceptor for galactose added in vitro by bovine milk galactosyltransferase. Peptide comparisons with other biochemical characteristics of the galactosylated protein identified it as the virus-encoded basic phosphoprotein. This protein is an abundant constituent of the virion and is located in the tegument region, between the capsid and the envelope, rather than in the envelope layer with the recognized virion glycoproteins. The galactosylated carbohydrate was resistant to a commercial preparation of endoglycosidase F but was sensitive to removal by alkali-induced beta-elimination, indicating an O-linkage to the protein. Chromatographic and electrophoretic determinations identified the beta-eliminated material as the alditol of Gal beta 1-4GlcNAc, establishing that the human cytomegalovirus virion basic phosphoprotein contains single O-linked residues of N-acetylglucosamine.

Original languageEnglish (US)
Pages (from-to)2573-2577
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume85
Issue number8
DOIs
StatePublished - Apr 1988

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