Imperial College London

Dr Tiago Costa

Faculty of Natural SciencesDepartment of Life Sciences

Lecturer in Bacterial Pathogenesis
 
 
 
//

Contact

 

+44 (0)20 7594 3696t.costa Website

 
 
//

Location

 

G.22Flowers buildingSouth Kensington Campus

//

Summary

 

Summary

Tiago Costa obtained his PhD in Molecular Biology from University of Umeå, Sweden in 2012 where he studied, the molecular and biochemical details of Yersinia Type III Secretion System (T3SS) translocators in the lab of Prof. Matthew Francis.

As a postdoctoral researcher in the laboratory of Prof. Gabriel Waksman (ISMB, London, UK) he studied the structural and molecular details of the E.coli conjugative Type IV Secretion System (T4SS) by cryo-electron microscopy (Cryo-EM) (Costa et al, Nat Rev Micro, 2015). He solved the structure of the iconic bacterial F-pilus at near-atomic resolution by cryo-EM, which provides the first atomic view of a bacterial extracellular appendage made of a protein-lipid complex. This study set the stage for understanding how DNA is transported from one bacterial cell (donor) to another (recipient), a process that leads to the spread of antibiotics resistance genes (Costa et al, Cell, 2016).

Recently, he solved the 3.3 Å-resolution cryo-EM structure of the T4SS core complex from Xanthomonas citri, a phytopathogen that utilizes this system to kill bacterial competitors (Sgro & Costa et al. Nat Micro, 2018).

Cryo-EM structure of a bacterial killing T4SS

Cryo-EM structure of a bacterial killing T4SS


Tiago Costa joined the Department of Life Sciences at Imperial College, London, UK in 2017 as a Lecturer in Bacterial Pathogenesis and Group Leader at the MRC Center for Molecular Bacteriology and Infection to study by Cryo-EM, the role of Bacterial Secretion Systems in pathogenicity. To fully understand how these macromolecular machines work, he uses a multi-disciplinary approach that includes: bacterial genetics (gene disruption and site-specific mutagenesis), membrane proteins biochemistry, cutting-edge single particle Cryo-EM, X-ray crystallography and protein cross-linking coupled with mass spectrometry (XL-MS).

Selected Publications

Sgro G.S.#, Costa, T.R.D.#, Cenens, W., Souza, D.P., Cassago, A., Oliveira, L.C., Salinas, R.K., Portugal, R.V., Farah, C.S., Waksman, G. (2018) Cryo-EM structure of the bacteria killing type IV secretion system core complex from Xanthomonas citri. Nature Microbiology doi: 10.1038/s41564-018-0262-z PMID: 30349081

Sgro G.S., Costa, T.R.D.* (2018) Cryo-EM grid preparation of membrane protein samples for single particle analysis. Frontiers in Molecular Biosciences 5,74, doi:10.3389/fmolb.2018.00074 PMID:30131964

Costa, T.R.D., Ilangovan, A., Ukleja, M., Redzej, A., Santini, J.M., Smith, T.K., Egelman, E.H., and Waksman, G. (2016). Structure of the Bacterial Sex F Pilus Reveals an Assembly of a Stoichiometric Protein-Phospholipid Complex. Cell 166, 1436-1444 e1410.PMID:27610568

Costa, T.R.D., Felisberto-Rodrigues, C., Meir, A., Prevost, M.S., Redzej, A., Trokter, M., and Waksman, G. (2015). Secretion systems in Gram-negative bacteria: structural and mechanistic insights. Nature Reviews Microbiology 13, 343-359. PMID:25978706


Publications

Journals

S. Sgro G, Costa TRD, 2018, Cryo-EM grid preparation of membrane protein samples for single particle analysis, Frontiers in Molecular Biosciences, Vol:5, ISSN:2296-889X

Gurung JM, Amer AAA, Francis MK, et al., 2018, Heterologous Complementation Studies With the YscX and YscY Protein Families Reveals a Specificity for Yersinia pseudotuberculosis Type III Secretion, Frontiers in Cellular and Infection Microbiology, Vol:8, ISSN:2235-2988

Sgro GG, Costa TRD, Cenens W, et al., 2018, Cryo-EM structure of the bacteria-killing type IV secretion system core complex from Xanthomonas citri., Nat Microbiol

Costa TRD, Ignatiou A, Orlova EV, 2017, Structural Analysis of Protein Complexes by Cryo Electron Microscopy., Methods Mol Biol, Vol:1615, Pages:377-413

Francis MS, Amer AAA, Milton DL, et al., 2017, Site-Directed Mutagenesis and Its Application in Studying the Interactions of T3S Components., Methods Mol Biol, Vol:1531, Pages:11-31

More Publications