Role of Glycoproteins in Virus–Human Cell Interactions

  • Thomas A. Bowden
  • Elizabeth E. FryEmail author


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.


Structural virology Viral glycoprotein Protein–protein interactions Membrane fusion Immune evasion 



core protein


cluster of differentiation 46


canine feline parvovirus


Dendritic Cell-Specific Intercellular adhesion molecule-3-Grabbing Non-integrin


Dengue virus




envelope glycoprotein


Ebola virus


endoplasmic reticulum


attachment glycoprotein


viral glycoprotein precursor


Guanarito virus




human immune deficiency virus-1


Human macrophage C-type lectin specific for galactose and N-acetylgalactosamine




human parainfluenza virus


heptad repeat motif


Japanese encephalitis virus


Junin virus


Lassa virus


Lymphocytic Choriomeningitis Virus


Machupo virus


Marburg virus


mouse mammary tumour virus


measles virus H




Newcastle disease virus


protein data bank


parainfluenza virus


precursor membrane protein


Sabia virus


signalling lymphocyte activation molecule


stable sequence peptide


simian parainfluenza type-5


tick-borne encephalitis virus


human transferrin receptor 1


West Nile virus



We gratefully acknowledge D.I. Stuart, E.Y. Jones, J. Grimes, A.R. Aricescu, and M. Crispin at the Division of Structural Biology, Oxford, for their support and many helpful discussions. T.A.B. is funded as a Sir Henry Wellcome Postdoctoral Fellow by the Wellcome Trust. E.E.F. is funded by the Medical Research Council, UK.


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Copyright information

© Springer Science+Business Media B.V. 2010

Authors and Affiliations

  1. 1.The Division of Structural BiologyThe Wellcome Trust Centre for Human Genetics, University of Oxford, Roosevelt DriveOxfordUK

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