Show simple item record

dc.rights.licenseCC-BY-NC-ND
dc.contributor.advisorDortmans, Dr. J.C.F.M
dc.contributor.authorBoeijen, M.
dc.date.accessioned2013-09-03T17:01:10Z
dc.date.available2013-09-03
dc.date.available2013-09-03T17:01:10Z
dc.date.issued2013
dc.identifier.urihttps://studenttheses.uu.nl/handle/20.500.12932/14431
dc.description.abstractInfluenza is a dangerous virus which has been the cause of many epidemics in the past and may create many more health issues in the future. Each year, high risk groups of the population are vaccinated against the influenza virus, however the antibodies generated against the vaccine might not fit the viral strain that is circling at that moment. This can be due to the form of hemagglutinin. The glycoprotein hemagglutinin is located on the envelope of influenza virus particles and can have different glycosylation forms. For antibody recognition the length of the glycans and the location of the glycosylation site are important. In this review an overview is provided of the glycosylation of the hemagglutinin protein and how it affects the functional properties of hemagglutinin. Lastly, it will be discussed how this knowledge may contribute to the development of influenza virus vaccines.
dc.description.sponsorshipUtrecht University
dc.format.extent581323 bytes
dc.format.mimetypeapplication/pdf
dc.language.isoen
dc.titleGlycosylation of the influenza A virus hemagglutinin protein
dc.type.contentMaster Thesis
dc.rights.accessrightsOpen Access
dc.subject.keywordsinfluenza A, hemagglutinin, glycosylation, glycan, oligosaccharide, vaccine
dc.subject.courseuuMolecular and Cellular Life Sciences


Files in this item

Thumbnail

This item appears in the following Collection(s)

Show simple item record