Our publications
- Pereira, I. S., Pais. S. V., Borges, V., Borrego, M. J., Gomes, J. P., Mota, L. J. (2022). The type III secretion effector CteG mediates host cell lysis of Chlamydia trachomatis. Front Cell Infect Microbiol.
- Monteiro, I. P., Sousa, S., Borges, V., Gonçalves, P., Gomes, J. P., Mota, L. J., Franco, I. (2022). A search for novel Legionella pneumophila effector proteins reveals a strain specific nucleotropic effector. Front Cell Infect Microbiol. doi.org/10.3389/fcimb.2022.864626.
- Bugalhão, J. N., Luís, M. P., Pereira, I. S., da Cunha, M., Mota, L. J. (2022). The Chlamydia trachomatis inclusion membrane protein CT006 associates with lipid droplets in eukaryotic cells. PLoS One. 17:e0264292. doi: 10.1371/journal.pone.0264292.
- Bugalhão, J. N., Mota, L. J. (2019). The multiple functions of the numerous Chlamydia trachomatis secreted proteins: the tip of ghe iceberg. Microb Cell. 6: 414-449. doi: 10.15698/mic2019.09.691.
- Pais., S. V., Key, C. E., Borges, V., Pereira, I. S., Gomes, J. P., Fisher, D. J., Mota, L. J. (2019). CteG is a Chlamydia trachomatis effector protein that associates with the Golgi complex of infected host cells. Sci Rep. 9:6133. doi: 10.1038/s41598-019-42647-3
- Almeida, F., Luís, M. P., Pereira, I. S., Pais, S. V., Mota, L. J. (2018). The human centrosomal protein CCDC146 binds Chlamydia trachomatis inclusion membrane protein CT288 and is recruited to the periphery of the Chlamydia-containing vacuole. Front Cell Infect Microbiol. 8:254. doi:10.3389/fcimb.2018.00254.
- Franco, I. S., Pais, S. V., Charro, N., and Mota, L. J. (2017). Effector translocation assay: differential solubilization. In Methods in Molecular Biology: Bacterial Protein Secretion Systems, Methods and Protocols. In press - June 2017. Journet, L., Cascales, E. (Eds.). Humana Press, Springer Science+Business Media LLC. doi: 10.1007/978-1-4939-7033-9_35.
- da Cunha, M., Pais, S. V., Bugalhão, J. N., Mota, L. J. (2017). The Chlamydia trachomatis type III secretion substrates CT142, CT143, and CT144 are secreted into the lumen of the inclusion. PLoS One. 12:e0178856. doi: 10.1371/journal.pone.0178856.
- Inácio, Â. S, Nunes, A., Milho, C., Mota, L. J., Borrego, M. J., Gomes, J. P., Vaz, W. L., Vieira, O. V. (2016). In Vitro Activity of Quaternary Ammonium Surfactants against Streptococcal, Chlamydial, and Gonococcal Infective Agents. Antimicrob Agents Chemother. 60:3323-32. doi: 10.1128/AAC.00166-16.
- Domingues, L., Ismail, A., Charro, N., Rodríguez-Escudero, I., Holden, D. W., Molina, M., Cid, V. J., Mota, L. J. (2016) The Salmonella effector SteA binds phosphatidylinositol 4-phosphate for subcellular targeting within host cells. Cell Microbiol. 18:949-69. doi: 10.1111/cmi.12558.
- Bugalhão, J. N., Mota, L. J., Franco, I.S. (2016) Identification of regions within the Legionella pneumophila VipA effector protein involved in actin binding and polymerization and in interference with eukaryotic organelle trafficking. Microbiologyopen. 5:118-33. doi: 10.1002/mbo3.316.
- Bugalhão, J. N., Mota, L. J., and Franco, I. S. (2015). Bacterial nucleators: actin' on actin. Pathog Dis. 73. pii: ftv078. doi: 10.1093/femspd/ftv078.
- Borges, V., Pinheiro, M., Antelo, M., Sampaio, D. A., Vieira, L., Ferreira, R., Nunes, A., Almeida, F., Mota, L. J., Borrego, M. J., and Gomes, J. P. (2015). Chlamydia trachomatis In Vivo to In Vitro Transition Reveals Mechanisms of Phase Variation and Down-Regulation of Virulence Factors. PLoS One. 10:e0133420. doi: 10.1371/journal.pone.0133420.
- Charro, N., and Mota, L. J. (2015). Approaches targeting the type III secretion system to prevent or treat bacterial infections. Expert Opinion On Drug Discovery. 10:373-87. doi: 10.1517/17460441.2015.1019860.
- Domingues, L., Holden, D. W., and Mota, L. J. (2014). The Salmonella effector SteA contributes to the control of membrane dynamics of Salmonella-containing vacuoles. Infect. Immun. 82:2923-34. doi: 10.1128/IAI.01385-13.
- da Cunha, M., Milho, C., Almeida, F., Pais, S. V., Borges, V., Maurício, R., Borrego, M. J., Gomes, J. P., and Mota, L. J. (2014). Identification of type III secretion substrates of Chlamydia trachomatis using Yersinia enterocolitica as a heterologous system. BMC Microbiol. 14(1):40. doi: 10.1186/1471-2180-14-40.
- Pais, S. V., Milho, C., Almeida, F., Mota, L. J. (2013). Identification of novel type III secretion chaperone-substrate complexes of Chlamydia trachomatis. PLoS ONE. 8: e56292. doi: 10.1371/journal.pone.0056292.
- Almeida, F., Borges, V, Ferreira, R., Borrego, M. J., Gomes, J. P, and Mota, L. J. (2012). Polymorphisms in Inc proteins and differential expression of inc genes among Chlamydia trachomatis strains correlate with invasiveness and tropism of lymphogranuloma venereum isolates. J Bacteriol. 194: 6574-6785. doi: 10.1128/JB.01428-12.
- McGourty, K. Thurston, T. L., Matthews, S.A., Pinaud, L., Mota, L. J., and Holden, D.W. (2012). Salmonella inhibits retrograde trafficking of mannose-6-phosphate receptors and lysosome function. Science. 338:963-967. doi: 10.1126/science.1227037.
- Bacteria and protozoa differentially modulate the expression of Rab proteins (2012). Seixas, E., Ramalho, J. S., Mota, L. J., Barral, D. C, Seabra, M. C. (2012), PLoS ONE. 7:e39858. doi: 10.1371/journal.pone.0039858.
- Schroeder N., Mota L. J., Méresse S. (2011). Salmonella-induced tubular networks. Trends Microbiol.19:268-277. doi: 10.1016/j.tim.2011.01.006.