Synthesis, stability, and cleavage of Newcastle disease virus glycoproteins in the absence of glycosylation.

Abstract:

:Polypeptides synthesized in Newcastle disease virus (NDV)-infected CHO cells in the absence of glycosylation were characterized. Incorporation of either [3H]mannose of [3H]glucosamine into NDV polypeptides was inhibited to greater than 99% by the antibiotic tunicamycin. Under these conditions, infected cells synthesized proteins which comigrated on polyacrylamide gels with the viral L protein, nucleocapsid protein, membrane protein, and a polypeptide with a molecular weight of 55,000 (P55). These cells did not synthesize polypeptides with the size of the hemagglutinin-neuraminidase (HN) protein or the fusion (F0) protein. They did, however, synthesize new polypeptides with molecular weights of 75,000 (P75), 67,000 (P67), and 52,000 (P52). Peptide analysis revealed that P75 was a host cell protein whose synthesis is enhanced by tunicamycin. P67 corresponded to the unglycosylated forms of the glycoproteins were found to be relatively stable in infected cells. P55, previously thought to correspond to the cleaved form of F0, was found to be a unique viral protein which is associated with intracellular nucleocapsid structures.

journal_name

J Virol

journal_title

Journal of virology

authors

Morrison TG,Simpson D

doi

10.1128/JVI.36.1.171-180.1980

subject

Has Abstract

pub_date

1980-10-01 00:00:00

pages

171-80

issue

1

eissn

0022-538X

issn

1098-5514

journal_volume

36

pub_type

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