Special Issue "Viral Glycoprotein Structure"
A special issue of Viruses (ISSN 1999-4915).
Deadline for manuscript submissions: closed (30 September 2015) | Viewed by 27166
Interests: viral glycoproteins, viral receptors, HIV-1, influenza, Ebola, electron microscopy, vaccines, antibody therapeutics, structural biology, biophysics, electron microscopy
Viral glycoproteins reside on the surface of virions and are often the sole component of the virus that interacts with the external environment. As such they must recognize appropriate host cells and initiate infection, either through membrane fusion or endocytosis, all while escaping detection by the immune system of animals. These multi-functional machines represent some of the most exciting but difficult protein complexes to structurally characterize. A number of technological breakthroughs have enabled increasingly detailed studies of these proteins, and with them a greater understanding of the viral fusion machinery and its interplay with antibodies, which have played a critical role in facilitating these studies. The glycans on the surface of viral glycoproteins are host derived and utilized by the virus to mimic the host and evade detection of the immune system. In many cases antibodies can still be generated either by avoiding the glycans (e.g. flu) or by incorporating them into epitopes (e.g. HIV). The rapid mutability of viruses coupled to immune pressure typically results in highly variable surfaces, resulting in a complex co-evolution between virus and host. The challenge then for structural biologists is to hit these moving targets. By combining a wide array of technologies and data types well-determined models of viral glycoprotein structure, function, and dynamics are attainable. The goal of this issue is to highlight the state of the art in viral glycoprotein structure and function that have been enabled by recent technological and methodological advances.
Dr. Andrew Ward
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- glycoprotein structure
- viral entry
- host recognition