The structural proteins of infectious pancreatic virus are not glycosylated.
The major capsid protein, VP2, of infectious pancreatic necrosis virus, a nonenveloped icosahedral virus, contains six N-glycosylation consensus sequences (Asn-X-[Thr/Ser]). Since VP2 contains the major virus-neutralizing epitopes, the possible role for glycosylation in capsid formation and antigenicity was examined. The carbohydrate content of the virion proteins was determined by chemical detection, pulse-chase experiments,[3H]mannose labeling, and alteration of protein migration on sodium dodecyl sulfate-polyacrylamide gels after tunicamycin treatment. No glycosylation of any virion protein was observed when the carbohydrate nature of the glycoprotein of infectious hematopoietic necrosis virus was detected.
Perez
L
L
Department of Microbiology, Oregon State University, Corvallis, USA.
Chiou
P P
PP
Leong
J C
JC
D000818:Animals; D006031:Glycosylation; D018061:Infectious pancreatic necrosis virus / Q000378:metabolism*; D015678:Viral Structural Proteins / Q000378:metabolism*
D015678:Viral Structural Proteins