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).
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).
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
et al., 2018, Cryo-EM structure of the bacteria-killing type IV secretion system core complex from Xanthomonas citri, Nature Microbiology, Vol:3, ISSN:2058-5276, Pages:1429-1440
Sgro GG, Costa TRD, 2018, Cryo-EM Grid Preparation of Membrane Protein Samples for Single Particle Analysis, Frontiers in Molecular Biosciences, Vol:5
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
et al., 2017, The Cryoelectron Microscopy Structure of the Type 1 Chaperone-Usher Pilus Rod, Structure, Vol:25, ISSN:0969-2126, Pages:1829-+
et al., 2017, Use of chimeric type IV secretion systems to define contributions of outer membrane subassemblies for contact-dependent translocation, Molecular Microbiology, Vol:105, ISSN:0950-382X, Pages:273-293