Evidence for virus-encoded glycosylation specificity

Ing Nang Wang, Yu Li, Quideng Que, Meenakshi Bhattacharya, Leslie C. Lane, William G. Chaney, James L. Van Etten

Research output: Contribution to journalArticlepeer-review

68 Scopus citations


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 glycosyl-transferases.

Original languageEnglish (US)
Pages (from-to)3840-3844
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Issue number9
StatePublished - May 1 1993


  • Algal virus
  • Chlorella
  • Serotypes

ASJC Scopus subject areas

  • General


Dive into the research topics of 'Evidence for virus-encoded glycosylation specificity'. Together they form a unique fingerprint.

Cite this