Acidic pH Mediates Changes in Antigenic and Oligomeric Conformation of Herpes Simplex Virus gB and Is a Determinant of Cell-Specific Entry
Copyright policy )Acidic pH Mediates Changes in Antigenic and Oligomeric Conformation of Herpes Simplex Virus gB and Is a Determinant of Cell-Specific Entry
Herpes simplex virus (HSV) causes infection of the mouth, skin, eyes, and genitals and establishes lifelong latency in humans. gB is conserved among all herpesviruses. HSV gB undergoes reversible conformational changes following exposure to acidic pH which are thought to mediate fusion and entry into epithelial cells. Here, we identified cotranslational folding and oligomerization of newly synthesized gB. A panel of antibodies to gB blocked both low-pH and pH-neutral entry of HSV, suggesting conserved conformational changes in gB regardless of cell entry route. Changes in HSV gB conformation were not triggered by increased temperature alone, in contrast to results with EBV gB. Acid pH-induced changes in the oligomeric conformation of gB are related but distinct from pH-triggered changes in gB antigenic conformation. These results highlight critical aspects of the class III fusion protein, gB, and inform strategies to block HSV infection at the level of fusion and entry.
- Washington State University United States
- Washington State University United States
- Virginia Commonwealth University United States
570, Protein Folding, Herpesvirus 1, Protein Conformation, Protein Conformation - drug effects, Temperature, Viral Envelope Proteins - immunology, 610, Herpesvirus 1, Human, Viral Envelope Proteins - metabolism, Hydrogen-Ion Concentration, Virus Internalization, Human - drug effects, Human - radiation effects, Protein Multimerization - drug effects, Viral Envelope Proteins, Viral Envelope Proteins - chemistry, Humans, Human - physiology, Protein Multimerization, Protein Folding - drug effects
570, Protein Folding, Herpesvirus 1, Protein Conformation, Protein Conformation - drug effects, Temperature, Viral Envelope Proteins - immunology, 610, Herpesvirus 1, Human, Viral Envelope Proteins - metabolism, Hydrogen-Ion Concentration, Virus Internalization, Human - drug effects, Human - radiation effects, Protein Multimerization - drug effects, Viral Envelope Proteins, Viral Envelope Proteins - chemistry, Humans, Human - physiology, Protein Multimerization, Protein Folding - drug effects
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