E. E. Heldwein

In-vitro reconstitution of Herpes Simplex Virus 1 fusion identifies low pH as a fusion co-trigger

This study reconstitutes HSV-1 membrane fusion in vitro and identifies low pH as a co-trigger, along with a host receptor, for efficient fusion.

Herpes simplex virus 1 entry glycoproteins form stable complexes prior to and during membrane fusion

This study shows HSV-1 glycoproteins form stable complexes before and during membrane fusion, independent of receptor binding, and proposes a revised conformational cascade model for viral entry.

A surface pocket in the cytoplasmic domain of the herpes simplex virus fusogen gB controls membrane fusion

This paper identifies a surface pocket in the cytoplasmic domain of herpes simplex virus gB and a residue in gH that interact to release the inhibitory clamp on gB, activating membrane fusion.

Highly basic clusters in the HSV-1 nuclear egress complex drive membrane budding by inducing lipid ordering

This study identifies how basic regions in the HSV-1 nuclear egress complex induce lipid ordering and negative curvature to drive membrane budding, with phosphorylation inhibiting this process.

Virus-derived peptide inhibitors of the herpes simplex virus type 1 nuclear egress complex

The paper identifies virus-derived peptides that inhibit the herpes simplex virus type 1 nuclear egress complex in vitro, suggesting a new therapeutic approach for herpesvirus infections.