Herpesvirus glycoprotein B

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Herpesvirus Glycoprotein B (PH-like 2)
Crystallographic structure of glycoprotein B from herpes simplex virus type 1.[1]
Identifiers
SymbolGlycoprot_B_PH2
PfamPF17417
InterProIPR038631
OPM superfamily109
OPM protein3nw8
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary
Herpesvirus Glycoprotein B (PH-like 1)
Identifiers
SymbolGlycoprot_B_PH1
PfamPF17416
InterProIPR035377
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary
Herpesvirus glycoprotein B ectodomain
Identifiers
SymbolGlycoprotein_B
PfamPF00606
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary

Herpesvirus glycoprotein B is a

cellular membrane or via endocytosis. Other viral glycoproteins involved in the process of viral cell entry include gC, gB, gD, gH, and gL, but only gC, gB, gD, and gH are required for the fusion of the HSV's envelope with the cellular membrane. It can be noted that all herpesviruses have glycoproteins gB, gH, and gL.[2]

Structure

The herpesvirus glycoprotein B is a

monoclonal antibodies map to structural domains I, II, IV and V.[7] Due to its unique structure, herpesvirus glycoprotein B (along with vesicular stomatitis virus glycoprotein G and baculovirus gp64) belongs to a new class of viral membrane fusion glycoproteins, class III.[3]

Function

The herpesvirus glycoprotein B is the most highly conserved of all surface glycoproteins and acts primarily as a fusion protein. The precise functions of gB and gH/gL are unknown but they are required for viral entry into the cell and constitute the core fusion machinery. The claim that gB is involved in fusion comes from the notable syncytial phenotype caused by certain mutations within the cytoplasmic domain of glycoprotein B,[8] as well as its structural homology to other viral fusion proteins.[3]

References

Further reading

This article incorporates text from the public domain Pfam and InterPro: IPR000234