Mechanism of neutralization of herpes simplex virus by antibodies directed at the fusion domain of glycoprotein B.

ABSTRACT:

Unlabelled

Glycoprotein B (gB), the fusogen of herpes simplex virus (HSV), is a class III fusion protein with a trimeric ectodomain of known structure for the postfusion state. Seen by negative-staining electron microscopy, it presents as a rod with three lobes (base, middle, and crown). gB has four functional regions (FR), defined by the physical location of epitopes recognized by anti-gB neutralizing monoclonal antibodies (MAbs). Located in the base, FR1 contains two internal fusion loops (FLs) and is the site of gB-lipid interaction (the fusion domain). Many of the MAbs to FR1 are neutralizing, block cell-cell fusion, and prevent the association of gB with lipid, suggesting that these MAbs affect FL function. Here we characterize FR1 epitopes by using electron microscopy to visu

SUBMITTER: Cairns TM 

PROVIDER: S-EPMC3958082 | biostudies-literature | 2014 Mar

REPOSITORIES: biostudies-literature