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Structural and functional studies of the reovirus attachment protein sigma1 and its interaction with the receptor JAM-A; Strukturelle und funktionelle Studien am Zelladsorptionsprotein sigma1 des Reovirus und seiner Interaktion mit dem Rezeptor JAM-A

Kirchner, Eva
Fonte: Universidade de Tubinga Publicador: Universidade de Tubinga
Tipo: Dissertação
Relevância na Pesquisa
The attachment of viruses to host cells and subsequent viral entry are key steps in viral infection. Receptor recognition also serves an essential function in target cell selection. Mammalian orthoreoviruses (reoviruses) are highly tractable experimental models for studies of virus-receptor interactions and viral pathogenesis. Furthermore, they show promise as vectors for oncolytics and vaccines. Similarly to many other viruses, reoviruses use cell-surface carbohydrates and a cell adhesion molecule as receptors. How the usage of multiple receptors contributes to viral attachment is still unclear, and general rules for receptor recognition at an atomic level have not yet been established. In this thesis, structural properties and receptor binding mechanisms of the reovirus attachment protein sigma1 were analyzed. sigma1 contains an unusal trimerization motif, the aspartic acid cluster, at its trimer interface. A sigma1 protein, in which one of the aspartic acids of the cluster was mutated to asparagine (D345N), was analyzed regarding binding to the reovirus receptor JAM-A, and its crystal structure was solved to high resolution. The analysis of the D345N mutant provides information about the protonation state of the aspartic acids and the forces holding the sigma1 trimer together. Moreover...