Processing of the herpes simplex virus type 2 glycoprotein gG-2 results in secretion of a 34,000-Mr cleavage product.
AUTOR(ES)
Su, H K
RESUMO
Herpes simplex virus type 2 glycoprotein gG-2 undergoes a cleavage event during its synthesis and processing. The focus of this report is on the detection and fate of the small-molecular-weight component of gG-2, designated the 34K component. In cultures containing the inhibitor monensin, a 31K component accumulated within infected cells. In contrast, the intracellular accumulation of this 31K precursor was not detected in cultures grown in the absence of the inhibitor. However, the 34K component of gG-2 was found in the extracellular culture fluid. The data suggest that the 31K high-mannose cleavage product of gG-2 is further glycosylated and rapidly secreted from herpes simplex virus type 2-infected cells; however, if glycosylation is perturbed, the 31K high-mannose form remains cell associated.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=254167Documentos Relacionados
- Synthesis and processing of glycoprotein gG of herpes simplex virus type 2.
- Inducible expression of herpes simplex virus type 2 glycoprotein gene gG-2 in a mammalian cell line.
- In vitro synthesis and processing of herpes simplex virus type 2 gG-2, using cell-free transcription and translation systems.
- Orientation of the cleavage site of the herpes simplex virus glycoprotein G-2.
- Characterization of a herpes simplex virus type 2 75,000-molecular-weight glycoprotein antigenically related to herpes simplex virus type 1 glycoprotein C.