Dr Sarah Smith

Postdoctoral Fellow

 

Alumni

This person is a member of Sanger Institute Alumni.

Sarah is a Post-doctoral fellow in the Virus Genomics group. She investigates host genetic variation in order to understand the biology of virus spread, host species adaption, and zoonosis. Sarah has particular interest in one family of virus restriction factors (VRFs), the Interferon Inducible Transmembrane (IFITM) proteins.

I graduated from the University of York with a BSc in molecular biology, during which I completed a year of research in the Gene Medicine group at the Nuffield Department of Clinical Laboratory Sciences (University of Oxford). I have subsequently completed my PhD on The Function and Genetics of the Host IFITM Locus in the Virus Genomics group at the Wellcome Trust Sanger Institute. I am continuing my work on human IFITM3 as a Post-doctoral fellow with the aim of understanding the genetic variation that results in differences in virus restriction.

We primarily use cell culture assays to determine the effect of restriction factors on virus cell entry, using a range of techniques including fluorescence microscopy, flow cytometry and plaque assays. We culture both replication-competent viruses and pseudoviruses to interrogate our cell-based systems.

 

My publications

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IFITM proteins inhibit virus entry at different stages of cell trafficking. Viruses enter cells by fusing with or penetrating a limiting cellular membrane. For most enveloped viruses fusion occurs either at the cell surface or, following uptake by endocytosis, from within endosomes. Acid-dependent viruses require acidification of the endosomal lumen by the membrane-associate vacuolar proton ATPase for fusion (shown in red). Trafficking through the endocytic system, from early to late endosomes, exposes virions to increasingly acidic environments. IFITM proteins (green) can inhibit entry and infection by a number of viruses that fuse/penetrate at the cell surface or from within endosomes. IFITM1 is expressed primarily at the cell surface, while IFITM2 and 3 are primarily intracellular. IFITM3 has been localised to endosomal compartments, but the distribution of IFITM2 still needs to be clearly established.

IFITM proteins inhibit virus entry at different stages of cell trafficking. Viruses enter cells by fusing with or penetrating a limiting cellular membrane. For most enveloped viruses fusion occurs either at the cell surface or, following uptake by endocytosis, from within endosomes. Acid-dependent viruses require acidification of the endosomal lumen by the membrane-associate vacuolar proton ATPase for fusion (shown in red). Trafficking through the endocytic system, from early to late endosomes, exposes virions to increasingly acidic environments. IFITM proteins (green) can inhibit entry and infection by a number of viruses that fuse/penetrate at the cell surface or from within endosomes. IFITM1 is expressed primarily at the cell surface, while IFITM2 and 3 are primarily intracellular. IFITM3 has been localised to endosomal compartments, but the distribution of IFITM2 still needs to be clearly established.