Characterization of soluble glycoprotein D-mediated herpes simplex virus type 1 infection
| Autor: | Justus B. Cohen, Steven K. Wendell, Arthur R. Frampton, Marianna Tsvitov, Ali Ozuer, Zoher Kapacee, Joseph C. Glorioso, William F. Goins, Waris A. Shah |
|---|---|
| Rok vydání: | 2006 |
| Předmět: |
Virus genetics
viruses Virus Attachment CHO Cells Herpesvirus 1 Human Biology HVEM medicine.disease_cause Virus Article Cell Line 03 medical and health sciences Virus entry Cricetulus Viral envelope Soluble glycoprotein Viral Envelope Proteins Viral entry Virology Cricetinae Chlorocebus aethiops medicine Animals Humans Vero Cells 030304 developmental biology Glycosaminoglycans chemistry.chemical_classification 0303 health sciences 030306 microbiology Glycoprotein D (gD) Virus Internalization Herpesvirus glycoprotein B HSV-1 3. Good health Cell biology Herpes simplex virus chemistry Ectodomain Receptors Virus Glycoprotein Gene Deletion Nectin-1 |
| Zdroj: | Virology. 360(2) |
| ISSN: | 0042-6822 |
| Popis: | Herpes simplex virus type 1 (HSV-1) entry into permissive cells involves attachment to cell-surface glycosaminoglycans (GAGs) and fusion of the virus envelope with the cell membrane triggered by the binding of glycoprotein D (gD) to cognate receptors. In this study, we characterized the observation that soluble forms of the gD ectodomain (sgD) can mediate entry of gD-deficient HSV-1. We examined the efficiency and receptor specificity of this activity and used sequential incubation protocols to determine the order and stability of the initial interactions required for entry. Surprisingly, virus binding to GAGs did not increase the efficiency of sgD-mediated entry and gD-deficient virus was capable of attaching to GAG-deficient cells in the absence of sgD. These observations suggested a novel binding interaction that may play a role in normal HSV infection. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|
Full Text from ScienceDirect