Recombinant HSV1 gD protein

Supplementary info

This supplementary information is collated from multiple sources and compiled automatically.

Activity summary

The HSV1 gD protein also known as glycoprotein D plays a mechanical role in herpes simplex virus 1 (HSV-1) entry. It binds to cellular receptors initiating viral fusion with host cells. Glycoprotein D (gD) has a molecular mass of about 39-41 kDa and is expressed on the surface of the viral envelope. The interaction with host cell receptors such as nectin-1 is essential for the virus to penetrate the cell membrane and establish infection within epithelial and neuronal tissues. This process causes HSV-1 to localize in areas where it can reactivate later.

Biological function summary

Glycoprotein D facilitates virus entry into the host by interacting with entry mediators. Although gD itself is not part of a larger protein complex its interaction with host cell receptors is essential to trigger downstream events necessary for viral replication. The binding of gD to cellular receptors initiates conformational changes that lead to the fusion of the viral envelope with the cell membrane. This fusion is a critical step in the viral life cycle allowing the viral capsid to enter the host cell cytoplasm and ultimately reach the nucleus for replication.

Pathways

Glycoprotein D is involved in the viral entry pathway coordinating with proteins such as glycoprotein B and glycoprotein H to successfully mediate the fusion process. The role of gD in HSV-1 entry links to pathways that manage cellular response to viral infections particularly engaging immune response mechanisms and signaling pathways involved in membrane fusion and receptor-mediated endocytosis. During its replication cycle HSV1 gD participates in the broader context of herpesvirus entry and spread within host tissues.

Associated diseases and disorders

Glycoprotein D plays a significant role in herpes-related conditions specifically herpes labialis (cold sores) and genital herpes. Its function in facilitating viral fusion makes it a target of the host immune response which seeks to neutralize the virus by blocking gD binding sites on the virus. The protein's interaction with host receptors connects it to other viral proteins involved in immune evasion tactics such as glycoprotein E which helps shield HSV-1 from antibody detection. Understanding these interactions can inform vaccine development and therapeutic strategies targeting HSV-1 infections.