Fusion-deficient insertion mutants of herpes simplex virus type 1 glycoprotein B adopt the trimeric postfusion conformation.

Journal of Virology
Jessica L SilvermanEkaterina E Heldwein

Abstract

Glycoprotein B (gB) enables the fusion of viral and cell membranes during entry of herpesviruses. However, gB alone is insufficient for membrane fusion; the gH/gL heterodimer is also required. The crystal structure of the herpes simplex virus type 1 (HSV-1) gB ectodomain, gB730, has demonstrated similarities between gB and other viral fusion proteins, leading to the hypothesis that gB is a fusogen, presumably directly involved in bringing the membranes together by refolding from its initial or prefusion form to its final or postfusion form. The only available crystal structure likely represents the postfusion form of gB; the prefusion form has not yet been determined. Previously, a panel of HSV-1 gB mutants was generated by using random 5-amino-acid-linker insertion mutagenesis. Several mutants were unable to mediate cell-cell fusion despite being expressed on the cell surface. Mapping of the insertion sites onto the crystal structure of gB730 suggested that several insertions might not be accommodated in the postfusion form. Thus, we hypothesized that some insertion mutants were nonfunctional due to being "trapped" in a prefusion form. Here, we generated five insertion mutants as soluble ectodomains and characterized them bioc...Continue Reading

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Citations

Aug 19, 2015·Current Opinion in Structural Biology·Eduard BaqueroYves Gaudin
Sep 13, 2016·ACS Infectious Diseases·Richard W Clarke
Mar 19, 2013·Journal of Molecular Biology·Elvira VituEkaterina E Heldwein
Oct 23, 2020·Nature Reviews. Microbiology·Sarah A ConnollyRichard Longnecker

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