Murid Herpesvirus 68 - MHV-68 Surface Proteins

MHV-68 Surface Proteins

Alpha-, beta-, and gammaherpesviruses display a heterodimer composed of glycoprotein H (gH) and glycoprotein L (gL) on their envelopes. This receptor is involved in the cell-to-cell transmission of the virus. Glycoprotein H has two conformations. Glycoprotein L is a chaperone protein which assures that gH takes on the correct conformation. When herpesviruses lack gL, gH misfolds. When alpha- or betaherpesviruses lack gL, they are noninfectious. When Murine Gammaherpesvirus 68 lacks gL, it remains infectious but is less able to bind to fibroblasts and epithelial cells.

The open reading frame M7 of the MHV-68 genome encodes for the surface receptor glycoprotein 150 (gp150). It is homologous to the Epstein-Barr virus membrane antigen gp350/220. MHV-68 is more closely related to the Kaposi's Sarcoma-associated herpesvirus (KSHV) than it is to the Epstein-Barr virus. Glycoprotein K8.1 is the KSHV homolog of MHV-68 gp150. MHV-68 is a very close relative of MHV-72. The MHV-68 M7 gene differs from the corresponding MHV-72 gene by five point mutations which alter four codons. Glycoprotein 150 allows MHV-68 to bind to B-cells.

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