Viral-host cell surface interaction site

The viral-host cell surface interaction site is the primary interface where viruses initiate the infection cycle by binding to specific host cell receptors (Marsh & Helenius, 2006, Cell). This interaction involves viral attachment proteins, such as the HIV-1 envelope glycoprotein (gp120) or the SARS-CoV-2 spike protein, which recognize and bind to host molecules like CD4 or ACE2, respectively (Wilen et al., 2012, CSH Perspect Med; Hoffmann et al., 2020, Cell). This binding often triggers conformational changes that facilitate viral entry via direct membrane fusion or receptor-mediated endocytosis (Marsh & Helenius, 2006, Cell). As a therapeutic target, this interface is exploited by entry inhibitors and neutralizing antibodies that block these initial steps, thereby preventing the viral genome from entering the host cell (Cihlar & Fordyce, 2016, Antiviral Res). Drugs like Maraviroc target host co-receptors, while others like Enfuvirtide or Palivizumab target viral fusion machinery or attachment proteins (Cihlar & Fordyce, 2016, Antiviral Res). However, targeting host-side components of this interface requires careful consideration of potential interference with the receptor's endogenous physiological functions (Kang et al., 2020, Nat Rev Immunol). Additionally, the high mutation rate of viral surface proteins often leads to the emergence of resistance, necessitating the development of broadly neutralizing agents (Kang et al., 2020, Nat Rev Immunol).

Other names

Viral entry interfaceViral attachment siteHost-pathogen interfaceViral-host membrane interface

Inhibition of viral attachment to host receptors, blocking of co-receptor binding, and prevention of viral-host membrane fusion (Cihlar & Fordyce, 2016, Antiviral Res; Hoffmann et al., 2020, Cell).