The export pathway of the pseudorabies virus gB homolog gII involves oligomer formation in the endoplasmic reticulum and protease processing in the Golgi apparatus.
AUTOR(ES)
Whealy, M E
RESUMO
The pseudorabies virus gII gene shares significant homology with the gB gene of herpes simplex virus type 1. Unlike gB, however, gII 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 gII 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 gIII glycoprotein and the gII glycoprotein genes of pseudorabies virus, we have mapped a functional cleavage domain of gII to an 11-amino-acid segment.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=249348Documentos Relacionados
- The pseudorabies virus gII gene is closely related to the gB glycoprotein gene of herpes simplex virus.
- Glycoprotein gB (gII) of pseudorabies virus can functionally substitute for glycoprotein gB in herpes simplex virus type 1.
- Processing of pseudorabies virus glycoprotein gII.
- Cytoplasmic Domain Signal Sequences That Mediate Transport of Varicella-Zoster Virus gB from the Endoplasmic Reticulum to the Golgi
- Oligomer formation of the gB glycoprotein of herpes simplex virus type 1.