The pseudorabies virus gll gene shares significant homology with the gB gene of herpes simplex virus type 1. Unlike gB, however, gll is processed by specific protease cleavage events after the synthesis of its precursor. The processed forms are maintained in an oligomeric complex that includes disulfide linkages. In this report, we demonstrate the kinetics of modification, complex formation, and subsequent protease processing. In particular, we suggest that gll oligomer formation in the endoplasmic reticulum is an integral part of the export pathway and that protease cleavage occurs only after oligomers have formed. Furthermore, through the use of glycoprotein gene fusions between the gill glycoprotein and the gll glycoprotein genes of pseudorabies virus, we have mapped a functional cleavage domain of gll to an 11-amino-acid segment.
|Original language||English (US)|
|Number of pages||10|
|Journal||Journal of virology|
|State||Published - 1990|
All Science Journal Classification (ASJC) codes
- Insect Science