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Functional and Structural study of LIC13137 and LIC11300 of Leptospira interrogans serovar copenhageni

Grant number: 13/06650-7
Support type:Scholarships in Brazil - Scientific Initiation
Effective date (Start): August 01, 2013
Effective date (End): July 31, 2014
Field of knowledge:Biological Sciences - Biochemistry - Chemistry of Macromolecules
Principal researcher:Cristiane Rodrigues Guzzo Carvalho
Grantee:Nikolas Koshiyama Maciel
Home Institution: Instituto de Ciências Biomédicas (ICB). Universidade de São Paulo (USP). São Paulo , SP, Brazil


Leptospirosis is a zoonosis that has been highlighted by the high incidence rate in Brazil, mainly in regions devoid of sanitation. Understanding the biochemical mechanisms involved with this bacteria metabolism is of great importance to advance the understanding of the disease. This project seeks to analyze the structure and function of the proteins LIC13137 and LIC13000, which have a GGDEF domain, responsable for the production of a bacterial second messenger, c-di-GMP. Currently, we have cloned LIC11300 and LIC13137 different fragments in order to increase chances of obtaining well reeled proteins to make crystallization assays.We have expressed and obtained GAF domain crystals of LIC13137 and we are focused also on obtaining clones of the entire LIC13137 protein to analyze GAF domain effect on the activity of the GGDEF domain.

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Scientific publications
(References retrieved automatically from Web of Science and SciELO through information on FAPESP grants and their corresponding numbers as mentioned in the publications by the authors)
DA COSTA VASCONCELOS, FERNANDA NOGALES; MACIEL, NIKOLAS KOSHIYAMA; FAVARO, DENIZE CRISTINA; DE OLIVEIRA, LUCIANA COUTINHO; BARBOSA, ANGELA SILVA; SALINAS, ROBERTO KOPKE; DE SOUZA, ROBSON FRANCISCO; FARAH, CHUCK SHAKER; GUZZO, CRISTIANE RODRIGUES. Structural and Enzymatic Characterization of a cAMP-Dependent Diguanylate Cyclase from Pathogenic Leptospira Species. Journal of Molecular Biology, v. 429, n. 15, p. 2337-2352, JUL 21 2017. Web of Science Citations: 6.

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