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Insertional Mutations in Herpes Simplex Virus Type 1 gL Identify Functional Domains for Association with gH and for Membrane Fusion
- Source :
- Journal of Virology. 83:11607-11615
- Publication Year :
- 2009
- Publisher :
- American Society for Microbiology, 2009.
-
Abstract
- Glycoprotein L (gL) is one of four glycoproteins required for the entry of herpes simplex virus (HSV) into cells and for virus-induced cell fusion. This glycoprotein oligomerizes with gH to form a membrane-bound heterodimer but can be secreted when expressed without gH. Twelve unique gL linker-insertion mutants were generated to identify regions critical for gH binding and gH/gL processing and regions essential for cell fusion and viral entry. All gL mutants were detected on the cell surface in the absence of gH, suggesting incomplete cleavage of the signal peptide or the presence of a cell surface receptor for secreted gL. Coexpression with gH enhanced the levels of cell surface gL detected by antibodies for all gL mutants except those that were defective in their interactions with gH. Two insertions into a conserved region of gL abrogated the binding of gL to gH and prevented gH expression on the cell surface. Three other insertions reduced the cell surface expression of gH and/or altered the properties of gH/gL heterodimers. Altered or absent interaction of gL with gH was correlated with reduced or absent cell fusion activity and impaired complementation of virion infectivity. These results identify a conserved domain of gL that is critical for its binding to gH and two noncontiguous regions of gL, one of which contains the conserved domain, that are critical for the gH/gL complex to perform its role in membrane fusion.
- Subjects :
- Signal peptide
Virus Integration
Immunology
Mutant
CHO Cells
Herpesvirus 1, Human
Biology
Microbiology
Cricetulus
Viral Envelope Proteins
Viral entry
Cell surface receptor
Cricetinae
Virology
Animals
chemistry.chemical_classification
Cell fusion
Lipid bilayer fusion
Virus Internalization
Molecular biology
Herpesvirus glycoprotein B
Protein Structure, Tertiary
Virus-Cell Interactions
Mutagenesis, Insertional
chemistry
Insect Science
Glycoprotein
Dimerization
Subjects
Details
- ISSN :
- 10985514 and 0022538X
- Volume :
- 83
- Database :
- OpenAIRE
- Journal :
- Journal of Virology
- Accession number :
- edsair.doi.dedup.....563ab3b621eb8c4866928fc750a6e2df
- Full Text :
- https://doi.org/10.1128/jvi.01369-09