Abstract
The ionophore monensin inhibited the formation of mature, fully glycosylated glycoproteins gB, gC, and gD during herpes simplex virus type 1 infection of human embryonic lung cells. Underglycosylated forms, including the apparent high-mannose precursor forms of the major glycoproteins, appeared. Monensin inhibited virus-induced cell fusion. Infectious virions produced in the presence of monensin appeared to contain predominantly underglycosylated glycoproteins.
Original language | English (US) |
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Pages (from-to) | 56-60 |
Number of pages | 5 |
Journal | Intervirology |
Volume | 20 |
Issue number | 1 |
DOIs | |
State | Published - 1983 |
Keywords
- Cell fusion
- Glycoprotein synthesis
- Herpes simplex virus type 1
- Infectious virus
- Monensin
ASJC Scopus subject areas
- Virology
- Infectious Diseases