Viruses have developed remarkable mechanisms to inhibit the adaptive and innate immune systems of their hosts. Clearly, viral entry glycoproteins play critical roles in these activities. However, many of these roles and biological pathways are poorly defined. With new infectious diseases emerging and classical viral diseases reemerging, closer examination of viral entry glycoproteins as targets for preventative or therapeutic strategies is warranted.
Survival of infection with Ebola virus (EBOV) depends on the ability of the host to mount early and strong immune responses. However, given that EBOV cases are associated with 40%–90% human mortality, EBOV has developed intricate solutions to human immunological defenses. Enveloped viruses, like EBOV, must deposit their genetic material within a cell to ensure their propagation. The roles of viral envelope glycoproteins in mediating virus attachment to host cells and catalyzing the subsequent fusion of the viral and host plasma membranes have been well described. Given the limited number of genes in EBOV and other viruses, it stands to reason that these conformationally labile glycoproteins are also involved in more than just the initial steps of a productive infection. There is strong evidence that viral entry glycoproteins (GP) are modulators of host antiviral defenses. This article discusses current structural understanding of the functions of envelope entry glycoproteins in immune evasion using EBOV as an example.
- How Does Glycosylation of Ebola Virus Envelope Proteins Facilitate Immune Evasion?
- What Roles Do Shed Viral Glycoproteins Play in Immune Evasion?
- How Do Viral Glycoproteins Actively Suppress Host Immunity?
- What Are the Innate Restriction Strategies Targeted toward Viral Glycoproteins?