A Single Amino Acid Substitution in the Transmembrane Domain of Glycoprotein H Functionally Compensates for the Absence of gL in Pseudorabies Virus.

ABSTRACT: Herpesvirus entry requires the coordinated action of at least four viral glycoproteins. Virus-specific binding to a cellular receptor triggers a membrane fusion cascade involving the conserved gH/gL complex and gB. Although gB is the genuine herpesvirus fusogen, it requires gH/gL for fusion, but how activation occurs is still unclear. To study the underlying mechanism, we used a gL-deleted pseudorabies virus (PrV) mutant characterized by its limited capability to directly infect neighboring cells that was exploited for several independent serial passages in cell culture. Unlike previous revertants that acquired mutations in the gL-binding N-terminus of gH, we obtained a variant, PrV-ΔgLPassV99, that unexpectedly contained two amino acid substitutions in the gH transmembrane domain (TMD). O

SUBMITTER: Vallbracht M 

PROVIDER: S-EPMC10819001 | biostudies-literature | 2023 Dec

REPOSITORIES: biostudies-literature