| Description | Herpesviruses are enveloped by a lipid bilayer that contains at least a dozen glycoproteins. The virion surface glycoproteins mediate recognition of susceptible cells and promote fusion of the viral envelope with the cell membrane, leading to virus entry. No single glycoprotein associated with the virion membrane has been identified as the fusogen [ ].Glycoprotein L (gL) forms a non-covalently linked heterodimer with glycoprotein H (gH). This heterodimer is essential for virus-cell and cell-cell fusion since the association of gH and gL is necessary for correct localisation of gH to the virion or cell surface. gH anchoring the heterodimer to the plasma membrane through its transmembrane domain. gL lacks a transmembrane domain and is secreted from cells when expressed in the absence of gH [ ].This entry represents Herpesvirus glycoprotein L (gL), which is a virion associated envelope glycoprotein [ ]. Heterodimer formation between gH and gL has been demonstrated in both virions and infected cells [ ]. Heterodimer formation between gL and gH is important for the proper folding of gH and its insertion into the membrane because the anti-gH conformation-dependent monoclonal antibodies (mAbs) 53S and LP11 bind gH only when gL is present [, ]. | Name | Herpesvirus glycoprotein L, N-terminal domain superfamily |
| Short Name | Herpes_gL_N_sf | Type | Homologous_superfamily |
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