Abstract
Changes to the overall glycosylation profile of viral glycoproteins have been shown to be advantageous to virus survival and virulence. Many human viral pathogens rely on specific oligosaccharides to evade detection by the host immune system. Viruses such as HIV, Hendra, SARS-CoV, influenza, respiratory syncytial virus, hepatitis and West Nile virus rely on N-linked and O-Linked glycosylation for critical functions such as entry into host cells, proteolytic processing and protein trafficking. Recent findings demonstrate the importance of glycosylation to viral virulence, infectivity and immune evasion in several virus families impacting on human health. This review considers the role of glycosylation in viral infection and will detail several potential therapies for these important human pathogens and emerging infections.
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Acknowledgements
Thanks to Emily Clark PhD, Natalie Thornburg PhD and Brooke Vigerust for critical reading of the manuscript.
Financial disclosure
The author is supported in part by Burroughs Welcome and the National Institute of Allergy & Infectious Diseases. The author has no other relevant affiliations or financial involvement with any organization or entity with a financial interest in or financial conflict with the subject matter or materials discussed in the manuscript apart from those disclosed.