Biosynthesis of measles virus hemagglutinin in persistently infected cells.

Abstract:

:The synthesis of the hemagglutinin (HA) glycoprotein of measles virus was investigated in a persistently infected cell line using a monoclonal anti-HA. The synthesis of the HA protein was shown to be associated with the rough endoplasmic reticulum. The unglycosylated (HA0) apoprotein is synthesized as a 65,000 dalton peptide and is inserted into the rough endoplasmic reticulum as a transmembrane protein with approximately 2 to 3000 daltons of the peptide exposed to the cytoplasmic membrane surface. Primary glycosylation of the HA protein was found to occur through the lipid-linked carrier, dolichol-phosphate, as determined by inhibition of glycosylation by tunicamycin. Glycosylation, however, was not a prerequisite for membrane insertion. Endo-beta-N-acetylglucosaminidase H digestion of the fully glycosylated HA protein indicated that both simple and complex oligosaccharides are present on the surface glycoprotein.

journal_name

Arch Virol

journal_title

Archives of virology

authors

Bellini WJ,Silver GD,McFarlin DE

doi

10.1007/BF01314129

subject

Has Abstract

pub_date

1983-01-01 00:00:00

pages

87-101

issue

1-2

eissn

0304-8608

issn

1432-8798

journal_volume

75

pub_type

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