A mechanistic basis for potent, glycoprotein B-directed gammaherpesvirus neutralization
| Autor: | Philip G. Stevenson, Anne-Sophie Kratz, Daniel L. Glauser, Laurent Gillet |
|---|---|
| Rok vydání: | 2011 |
| Předmět: |
Rhadinovirus
Endosome Antibodies Viral Neutralization Epitope Cell Line 03 medical and health sciences Epitopes Mice Neutralization Tests Virology Animals 030304 developmental biology Glycoproteins chemistry.chemical_classification Viral Structural Proteins 0303 health sciences Mice Inbred BALB C biology Animal Murid herpesvirus 4 030302 biochemistry & molecular biology Lipid bilayer fusion Antibodies Monoclonal biology.organism_classification Antibodies Neutralizing Standard chemistry biology.protein Antibody Glycoprotein DNA viruses |
| Zdroj: | The Journal of general virology The Journal of General Virology |
| Popis: | Glycoprotein B (gB) is a conserved, essential component of gammaherpes virions and so potentially vulnerable to neutralization. However, few good gB-specific neutralizing antibodies have been identified. Here, we show that murid herpesvirus 4 is strongly neutralized by mAbs that recognize an epitope close to one of the gB fusion loops. Antibody binding did not stop gB interacting with its cellular ligands or initiating its fusion-associated conformation change, but did stop gB resolving stably to its post-fusion form, and so blocked membrane fusion to leave virions stranded in late endosomes. The conservation of gB makes this mechanism a possible general route to gammaherpesvirus neutralization. |
| Databáze: | OpenAIRE |
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