Disease relevance of UL10

• Analysis of the requirement for glycoprotein m in herpes simplex virus type 1 morphogenesis [1].
• Bovine herpesvirus 1 UL49.5 protein inhibits the transporter associated with antigen processing despite complex formation with glycoprotein M [2].
• In BHV-1-infected cells and virions, the UL49.5 protein forms a complex with glycoprotein M (gM) [2].
• The ability of gM to cause the relocalization of plasma membrane proteins was not restricted to HSV-1 glycoproteins, as other viral and non-viral proteins were also affected [3].
• Glycoprotein M of bovine herpesvirus 1 (BHV-1) is nonessential for replication in cell culture and is involved in inhibition of bovine respiratory syncytial virus F protein induced syncytium formation in recombinant BHV-1 infected cells [4].

High impact information on UL10

• However, in BHV-1-infected cells, differences in UL49.5 and gM expression kinetics were seen to create a window of opportunity at the early stages of infection, during which time the UL49.5 protein can act on TAP without gM interference [2].
• In cell lines constitutively expressing both UL49.5 and gM, UL49.5 appears to be required for functional processing of gM [2].
• Alphaherpesvirus glycoprotein M causes the relocalization of plasma membrane proteins [3].
• Here, the effect of pseudorabies virus (PRV) gM and the herpes simplex virus type 1 (HSV-1) gM/UL49A complex on the fusion events caused by the HSV-1 glycoproteins gB, gD, gH and gL was investigated [3].
• Infection of cell cultures with the resulting gM(-) mutant of BHV-1/F(syn) led to formation of syncytia, whereas the CPE in gM(-)BHV-1 infected cells was comparable to the CPE in wtBHV-1 infected cultures [4].

Biological context of UL10

• Our results demonstrate that gM is not essential for BHV-1 replication in cell culture and that gM is involved in inhibition of the cell fusion activity of the BHV-1 expressed BRSV F protein [4].

References