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Study of the function of different Hcp proteins encoded by Salmonella spp

Grant number: 21/09162-0
Support Opportunities:Scholarships in Brazil - Doctorate (Direct)
Effective date (Start): February 01, 2022
Effective date (End): December 31, 2023
Field of knowledge:Biological Sciences - Microbiology - Biology and Physiology of Microorganisms
Principal Investigator:Ethel Bayer Santos
Grantee:Stephanie Sibinelli de Sousa
Host Institution: Instituto de Ciências Biomédicas (ICB). Universidade de São Paulo (USP). São Paulo , SP, Brazil
Associated research grant:17/02178-2 - Function of type VI secretion systems of pathogenic bacteria in the interaction with eukaryotic cells, AP.JP


Salmonella spp. encode five type VI secretion systems (T6SS) in different pathogenicity islands. These systems translocate effector proteins into target cells, which can be either eukaryotic or prokaryotic. Hcps (hemolysin-coregulated proteins) are components of T6SS and have several functions. The main one is structural, in which hexamers of Hcps form the tube that is ejected towards the target cell. Hcps also have chaperone functions and bind to secreted proteins facilitating their translocation. Some Hcps contain a C-terminal domain that functions as a toxic effector. Furthermore, certain Hcps play a role in gene expression regulation by interacting with transcription factors. Salmonella Typhimurium encodes Hcps inside and outside (orphan Hcps) of the T6SS structural cluster, and these appear to play different roles. Preliminary phylogenetic analyzes revealed that Hcps from different species form several groups, with representatives of Salmonella spp. present in all groups. The present project aims to continue and expand the characterization of the function of Hcps in Salmonella spp. First, we will perform a functional classification of different Hcps proteins based on phylogenetic analysis and identification of interaction partners. Later, we will choose an interaction partner to perform a functional characterization. We believe that this work will increase the knowledge about these multifunctional proteins encoded in the genome of several bacteria. (AU)

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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)
COBO, NEIL LORENTE; SIBINELLI-SOUSA, STEPHANIE; BIBOY, JACOB; VOLLMER, WALDEMAR; BAYER-SANTOS, ETHEL; PREHNA, GERD. Molecular characterization of the type VI secretion system effector Tlde1a reveals a structurally altered fold. Journal of Biological Chemistry, v. 298, n. 11, p. 17-pg., . (17/02178-2, 21/09162-0)

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