Native HSV Type 1 Grade III Antigen

Herpes simplex virus 1 (HSV1) is an important pathogen with a worldwide epidemic trend that affects populations of various ages. It has a high morbidity, particularly in juveniles, but a successful HSV1 vaccine is not currently available. Thus, our study systematically observed the immune responses induced in mice immunized with the attenuated HSV1 M3 mutant strain, which has mutations in the genes encoding the UL7 and Vhs tegument proteins and the latency-associated transcript. The immunity induced by the M3 mutant strain can control acute viral infection during HSV1 wildtype strain infection. Moreover, this immunity exerts a potent effect on controlling viral entry into the trigeminal neurons. These data encourage further studies investigating the development of M3 as a potential vaccine candidate, and much work is necessary to evaluate the safety and improve the immunogenicity of this strain.

Herpesvirus entry into cells requires coordinated interactions among several viral transmembrane glycoproteins. Viral glycoproteins bind to receptors and interact with other glycoproteins to trigger virus-cell membrane fusion. Details of these glycoprotein interactions are not well understood because they are likely transient and/or low affinity. Proximity biotinylation is a promising protein-protein interaction assay that can capture transient interactions in live cells. One protein is linked to a biotin ligase and a second protein is linked to a short specific acceptor peptide (AP). If the two proteins interact, the ligase will biotinylate the AP, without requiring a sustained interaction. To examine herpesvirus glycoprotein interactions, the ligase and AP were linked to herpes simplex virus 1 (HSV1) gD and Epstein Barr virus (EBV) gB. Interactions between monomers of these oligomeric proteins (homotypic interactions) served as positive controls to demonstrate assay sensitivity. Heterotypic combinations served as negative controls to determine assay specificity, since HSV1 gD and EBV gB do not interact functionally. Positive controls showed strong biotinylation, indicating that viral glycoprotein proximity can be detected. Unexpectedly, the negative controls also showed biotinylation. These results demonstrate the special circumstances that must be considered when examining interactions among glycosylated proteins that are constrained within a membrane. (C) 2015 Elsevier B.V. All rights reserved.