Delineation of the essential function of bovine herpesvirus 1 gD: an indication for the modulatory
Glycoprotein gIV is an envelope component of bovine herpesvirus type 1 and appears to be involved in attachment, penetration, and cell fusion. The BHV-2-specific 130-kDa glycoprotein is able to induce cross-reacting antibodies, some of which even cross-neutralize HSV-1. 2011 Nov 4;17(45):12659-68 glycoprotein B, human herpesvirus 1 0 *Viral Envelope Proteins Herpesvirus 1, Human. This region of VP22 (residues 165–225) overlaps the glycoprotein E (gE) binding domain of VP22 (residues 165–270), which is sufficient to mediate VP22 packaging into assembling virus particles. Final envelopment, including the acquisition of more than 15 tegument and more than 10 envelope (glyco) proteins occurs by budding into Golgi-derived vesicles. The diverse interactions between the involved proteins exhibit a striking redundancy which is still insufficiently understood. In addition, we found that a gD-null virus (a virus containing no gD on its virion) could infect gD-expressing cells, but not normal MDBK cells.
The ability of the gD-null virus to infect gD-expressing cells was dependent on the gD present on the cell surface, since either treating cells with phosphatidylinositol-specific phospholipase C to remove the GPI-anchored gD or incubating cells with gD monoclonal antibodies could block gD-null virus infection. This demonstrates that gD present on the cell surface can act in trans to facilitate the entry of virion lacking gD. This indicates that essential gD function can take place in the absence of gD-mediated virus attachment and membrane fusion. Copyright: © 2014 Liu et al. Typically, during fusion on the cell surface, receptor binding induces conformational changes in viral glycoproteins that expose a hydrophobic fusion peptide.