Viral fusion proteins refer to a group of specialized proteins found on the surface of certain viruses that play a pivotal role in the process of viral fusion with host cells. This fusion process is essential for the virus to enter and infect its target host cells.
Viral fusion proteins are typically composed of two subunits that work together to mediate the fusion of the viral envelope with the host cell membrane. These subunits undergo a series of conformational changes, triggered by various factors such as receptor binding or changes in pH, leading to the fusion of the two membranes.
One commonly studied type of viral fusion protein is the class I fusion protein, which includes proteins found in viruses such as influenza, HIV, and Ebola. Class I fusion proteins consist of a fusion peptide, a transmembrane domain, and a long ectodomain consisting of α-helical coiled coils. These proteins undergo dramatic structural changes upon receptor binding or exposure to low pH environments, allowing them to insert the fusion peptide into the host cell membrane and bring the viral and host membranes into close proximity, ultimately leading to fusion.
Understanding the structure and function of viral fusion proteins is crucial for the development of antiviral drugs and vaccines. Disrupting the fusion process by targeting these proteins or their interactions may prevent viral entry and inhibit infection. Therefore, viral fusion proteins are important targets for therapeutic interventions and strategies to combat viral diseases.