Evidence for Virus-Encoded Glycosylation Specificity

Authors

Ing-Nang Wang, University of Nebraska-Lincoln
Yu Li, University of Nebraska-Lincoln
Quideng Que, University of Nebraska-Lincoln
Meenakshi Bhattacharya, University of Nebraska-Lincoln
Leslie C. Lane, University of Nebraska-LincolnFollow
William G. Chaney, University of Nebraska Medical Center, Omaha, NE
James L. Van Etten, University of Nebraska-LincolnFollow

Date of this Version

5-1-1993

Comments

Published in Proceedings of the National Academy of Sciences USA 90:9 (May 1, 1993), pp. 3840-3844. Copyright © 1993 National Academy of Sciences USA. Used by permission. http://www.pnas.org/content/90/9/3840.full.pdf+html

Abstract

Four spontaneously derived serologically distinct classes of mutants of the Paramecium bursaria chlorella virus (PBCV-1) were isolated using polydonal 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.