Cookies on this website

We use cookies to ensure that we give you the best experience on our website. If you click 'Accept all cookies' we'll assume that you are happy to receive all cookies and you won't see this message again. If you click 'Reject all non-essential cookies' only necessary cookies providing core functionality such as security, network management, and accessibility will be enabled. Click 'Find out more' for information on how to change your cookie settings.

© Springer Science+Business Media B.V. 2011. All rights reserved. Glycosylation of viral proteins is clearly advantageous to virus survival, having roles in cell entry, proteolytic processing, trafficking and immune evasion. For enveloped RNA viruses, including many important human pathogens, entry into host cells tends to be mediated by viral glycoproteins. Structural studies of glycoproteins from different viral families have gradually elucidated the mechanisms by which this occurs. We illustrate this by providing examples from recent studies and show that clear differences exist between viruses which use individual glycoproteins for attachment and fusion, and those that use a single glycoprotein for both functions. However, in all cases a similar end-point is reached. Understanding the biology of infection and host responses should lead to the development of enhanced therapeutics.

Original publication

DOI

10.1007/978-90-481-9355-4-7

Type

Chapter

Book title

Functional and Structural Proteomics of Glycoproteins

Publication Date

01/01/2011

Pages

159 - 180