Christos Savva

profilephoto

Principal Electron Microscopist for the electron Bio-Imaging Centre (eBIC)

Christos joined eBIC in November 2024.

Email: [email protected]
Tel: +44 (0) 1235 77 8976

Dr. Christos Savva joined eBIC in 2024 as a Principal EM Scientist. His research focuses on understanding how double-stranded DNA bacteriophages achieve host-cell lysis by disrupting the inner and outer membranes of bacterial cells using specific protein complexes. In collaboration with Prof. Ryland Young at Texas A&M University the aim is to use high-resolution single-particle Cryo-EM and in situ Cryo-Tomography to determine the structures of the proteins involved in this process. This research seeks to uncover the mechanisms behind one of biology's largest pore-forming systems, providing insights that could support the development of phage-based therapeutics to combat antibiotic resistance.

Christos obtained his B.Sc. from the University of Leeds in 2000 and completed his Ph.D. at Texas A&M University in 2007. During this time, he developed an interest in how proteins form pores in biological membranes, focusing on the structural mechanisms through which bacteriophages disrupt bacterial membranes. Later, during his postdoctoral research at Birkbeck College and as a staff scientist at the MRC-LMB, he solved the structures of several pore-forming toxins in the hemolysin and aerolysin families using Cryo-EM and X-ray crystallography.

Over the past 20 years, Christos has been involved in managing and maintaining high-end EM facilities at Texas A&M University, the MRC-LMB, and the University of Leicester. In his current role at eBIC, he will contribute to the maintenance and development of this world-class facility, as well as support the dissemination of knowledge and training of new structural biologists in the use of Cryo-EM.

Selected publications

Savva CG, Sobhy MA, De Biasio A, Hamdan SM. Structure of Aquifex aeolicus lumazine synthase by cryo-electron microscopy to 1.42 Å resolution. IUCrJ. 2024 Sep 1;11(Pt 5):723-729. doi:10.1107/S2052252524005530. PMID: 38965901; PMCID: PMC11364023.

Bate N, Savva CG, Moody PCE, Brown EA, Evans SE, Ball JK, Schwabe JWR, Sale JE, Brindle NPJ. In vitro evolution predicts emerging SARS-CoV-2 mutations with high affinity for ACE2 and cross-species binding. PLoS Pathog. 2022 Jul 18;18(7):e1010733. doi: 10.1371/journal.ppat.1010733. PMID: 35849637; PMCID: PMC9333441.

Savva CG, Clark AR, Naylor CE, Popoff MR, Moss DS, Basak AK, Titball RW, Bokori-Brown M. The pore structure of Clostridium perfringens epsilon toxin. Nat Commun. 2019 Jun 14;10(1):2641. doi:10.1038/s41467-019-10645-8. PMID: 31201325; PMCID: PMC6572795.

Bokori-Brown M, Martin TG, Naylor CE, Basak AK, Titball RW, Savva CG. Cryo-EM structure of lysenin pore elucidates membrane insertion by an aerolysin family protein. Nat Commun. 2016 Apr 6;7:11293. doi:10.1038/ncomms11293. PMID: 27048994; PMCID: PMC4823867.

Savva CG, Dewey JS, Moussa SH, To KH, Holzenburg A, Young R. Stable micron-scale holes are a general feature of canonical holins. Mol Microbiol. 2014 Jan;91(1):57-65. doi:10.1111/mmi.12439. Epub 2013 Nov 21. PMID: 24164554; PMCID: PMC4009996.

Bokori-Brown M, Kokkinidou MC, Savva CG, Fernandes da Costa S, Naylor CE, Cole AR, Moss DS, Basak AK, Titball RW. Clostridium perfringens epsilon toxin H149A mutant as a platform for receptor binding studies. Protein Sci. 2013 May;22(5):650-9. doi:10.1002/pro.2250. Epub 2013 Apr 8. PMID: 23504825; PMCID: PMC3649266.

Savva CG, Fernandes da Costa SP, Bokori-Brown M, Naylor CE, Cole AR, Moss DS, Titball RW, Basak AK. Molecular architecture and functional analysis of NetB, a pore-forming toxin from Clostridium perfringens. J Biol Chem. 2013 Feb 1;288(5):3512-22. doi:10.1074/jbc.M112.430223. Epub 2012 Dec 13. PMID: 23239883; PMCID: PMC3561570.

Dewey JS, Savva CG, White RL, Vitha S, Holzenburg A, Young R. Micron-scale holes terminate the phage infection cycle. Proc Natl Acad Sci U S A. 2010 Feb 2;107(5):2219-23. doi:10.1073/pnas.0914030107. Epub 2010 Jan 11. PMID: 20080651; PMCID: PMC2836697.

Pang T, Savva CG, Fleming KG, Struck DK, Young R. Structure of the lethal phage pinhole. Proc Natl Acad Sci U S A. 2009 Nov 10;106(45):18966-71. doi:10.1073/pnas.0907941106. Epub 2009 Oct 27. PMID: 19861547; PMCID: PMC2776468.

Savva CG, Dewey JS, Deaton J, White RL, Struck DK, Holzenburg A, Young R. The holin of bacteriophage lambda forms rings with large diameter. Mol Microbiol. 2008 Aug;69(4):784-793. doi:10.1111/j.1365-2958.2008.06298.x. PMID: 18788120; PMCID: PMC6005192.

Diamond Light Source

Diamond Light Source is the UK's national synchrotron science facility, located at the Harwell Science and Innovation Campus in Oxfordshire.

Copyright © 2022 Diamond Light Source

 

Diamond Light Source Ltd
Diamond House
Harwell Science & Innovation Campus
Didcot
Oxfordshire
OX11 0DE

See on Google Maps

Diamond Light Source® and the Diamond logo are registered trademarks of Diamond Light Source Ltd

Registered in England and Wales at Diamond House, Harwell Science and Innovation Campus, Didcot, Oxfordshire, OX11 0DE, United Kingdom. Company number: 4375679. VAT number: 287 461 957. Economic Operators Registration and Identification (EORI) number: GB287461957003.

feedback