Host: Marta Carroni

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Abstract -
Protein macromolecules that create gaps or holes in biological membranes are ubiquitous in nature and present in all organisms and some viruses. Each family of these proteins has evolved to create a pore or lesion that will accommodate its purpose ranging from a few Angstroms to over a micrometer in size. We have studied the structures of several aerolysin family members from annelids to bacteria and found that they produce pores very similar in structure despite little to no sequence homology. In bacteriophages other macromolecules and processes have evolved to allow the escape of newly assemble virions. We are now revisiting some of these structures at high-resolution to elucidate the molecular mechanism of phage host lysis. Cryo-EM has proven a very valuable method for studying the diversity of complexity of such proteins.

"Christos obtained his PhD from Texas A&M university under the guidance of Andreas Holzenburg and Ryland young studying bacteriophage lysis proteins by EM. He then worked as a research scientist at the university’s EM facility before moving to Birkbeck college to study clostridial pore forming toxins by Cryo-EM and x-ray crystallography in the lab of Ajit Basak and David Moss. From there he joined the MRC LMB EM facility just as the resolution-revolution was beginning before moving to the university of Leicester in 2018 to manage the Midlands Regional Cryo-EM facility."