Dr Marina Ioannou
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Email
mioanna@essex.ac.uk -
Location
Colchester Campus
Profile
Biography
2014- 2018 Ph.D., in Molecular Medicine at University of Essex, UK 2012-2013 M.Sc., in Molecular Medicine at University of Essex, UK 2009-2012 B.Sc., in Biological Sciences at University of Essex, UK The interaction between a virus and its receptor is major determinant of cell tropism. Understanding this interaction is needed to understand virus disease as well as showing ways that viruses can be exploited for example in oncolytic therapy. In this study the main protagonist is Coxsackie virus A9, an enterovirus known to have an RGD (arginine-glycine-aspartic acid) motif within a 15- amino acid carboxy terminal extension of VP1 capsid protein.As the RGD motif is known to be a strongly conserved region and implicated in interactions with receptors the aim is to investigate the viral infectivity and cell tropism of viruses with different mutations substituted downstream of the RGD motif (RGDX). A quick overview of some of the aims include: The cell tropism of a panel of CAV9 RGDX mutants using different cell lines Identification of the specific integrin receptor used by the wild type and mutant viruses by antibody blocking, flow cytometry and siRNA Finding of the mechanism of binding and internalization pathway if altered in different RGDX mutants using drugs, siRNA, antibodies, EDTA resistance methods etc.
Research and professional activities
Thesis
Cell Surface interactions of Coxsackie A9 virus
An understanding of how viruses interact with their receptors is vital as this step is a major determinant of host susceptibility and disease. CAV9, an enterovirus, harbors an integrin- recognition motif, RGD (Arg-Gly-Asp), in the capsid protein VP1 and although modes of transmission and pathogenesis are still largely unkown, this motif is believed to be primarily responsible for integrins avß6 and avß3 binding. The conservation of the RGD +1 position in CAV9 and other picornaviruses showed evid
Supervisor: Prof Glyn Stanway