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. 1993 May 1;90(9):3840–3844. doi: 10.1073/pnas.90.9.3840

Evidence for virus-encoded glycosylation specificity.

I N Wang 1, Y Li 1, Q Que 1, M Bhattacharya 1, L C Lane 1, W G Chaney 1, J L Van Etten 1
PMCID: PMC46401  PMID: 7683409

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.

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Selected References

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