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(2002) Smit, Jolanda Mariske
Mutational analysis of the viral spike proteins has greatly contributed to our current understanding of the molecular mechanisms involved in the membrane fusion process of alphaviruses. The studies described in this thesis attempt to further unravel the molecular basis of the membrane fusion activity of SIN, by site-specific mutagenesis of amino acids in the E2 and E1 glycoprotein sequences.
These mutations are generated in full-length clones of SIN. The receptor interaction and the membrane fusion characteristics of the mutants are analyzed by cell binding assays, on-line lipid mixing assays, content mixing assays, and analysis of the viral spike conformational changes. The first chapters deal with the general characteristics of the membrane fusion process of SIN with liposomes.
Subsequently, the influence of post-translational modifications, including glycosylation, palmitoylation, PE2 cleavage, of the viral glycoproteins on the membrane fusion process of SIN is investigated.
Gebruik a.u.b. deze link om te verwijzen naar dit
document:
http://irs.ub.rug.nl/ppn/239352920 |
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