Human cytomegalovirus envelope glycoprotein L (gL) (gL)

Human cytomegalovirus (HCMV) envelope glycoprotein L (gL) is a critical viral protein encoded by the UL115 gene that serves as an essential component of the virus's entry machinery [1, 2]. It functions primarily as a chaperone for glycoprotein H (gH), forming a stable gH/gL heterodimer that is required for the correct folding and transport of gH to the viral envelope [1, 3]. This heterodimer acts as a scaffold for the assembly of the trimeric (gH/gL/gO) and pentameric (gH/gL/UL128/UL130/UL131A) complexes, which dictate the virus's ability to infect a wide range of cell types, including fibroblasts, epithelial, and endothelial cells [2, 5]. By interacting with host receptors such as PDGFR-alpha and NRP2, these complexes mediate the fusion of the viral envelope with the host cell membrane [1, 5]. Consequently, gL is a primary target for neutralizing antibodies and is a key antigen in several vaccine candidates, such as the mRNA-1647 vaccine [3, 4]. Therapeutic strategies targeting gL aim to block viral entry and spread, providing a vital approach for preventing congenital CMV and managing infections in transplant recipients and other immunocompromised populations [3, 5].

Other names

UL115gpUL115Glycoprotein LHCMV gL

Neutralization of viral entry and inhibition of membrane fusion by targeting gH/gL-containing complexes (trimer and pentamer), thereby preventing viral attachment and penetration into host cells [1, 3].