Evidence for virus-encoded glycosylation specificity

I. N. Wang, Y. Li, Q. Que, M. Bhattacharya, L. C. Lane, W. G. Chaney, J. L. Van Etten

Research output: Contribution to journalArticle

65 Scopus citations

Abstract

Four spontaneously derived serologically distinct classes of mutants of the Paramecium bursaria chlorella virus (PBCV-1) were isolated using polyclonal antiserum prepared against either intact PBCV-1 or PBCV-1-derived serotypes. The oligosaccharide(s) of the viral major capsid protein and two minor glycoproteins determined virus serological specificity. Normally, viral glycoproteins arise from host-specific glycosylation of viral proteins; the glycan portion can be altered only by growing the virus on another host or by mutations in glycosylation sites of the viral protein. Neither mechanism explains the changes in the glycan(s) of the PBCV-1 major capsid protein because all of the viruses were grown in the same host alga and the predicted amino acid sequence of the major capsid protein was identical in the PBCV-1 serotypes. PBCV-1 antiserum resistance is best explained by viral mutations that block specific steps in glycosylation, possibly by inactivating glycosyltransferases.

Original languageEnglish (US)
Pages (from-to)3840-3844
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume90
Issue number9
DOIs
StatePublished - 1993

Keywords

  • algal virus
  • chlorella
  • serotypes

ASJC Scopus subject areas

  • General

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