Scholarship 24/12387-1 - Bacteriófagos, Fitopatologia - BV FAPESP
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Development of a system for the identification and characterization of peptides associated with the adsorption of Xanthomonas citri bacteriophages

Grant number: 24/12387-1
Support Opportunities:Scholarships in Brazil - Doctorate
Start date until: December 01, 2024
End date until: April 30, 2028
Field of knowledge:Agronomical Sciences - Agronomy - Plant Health
Principal Investigator:Henrique Ferreira
Grantee:Mario Nicolas Caccalano
Host Institution: Instituto de Biociências (IB). Universidade Estadual Paulista (UNESP). Campus de Rio Claro. Rio Claro , SP, Brazil
Associated research grant:21/10577-0 - Biology of Bacteria and Bacteriophages Research Center, AP.CEPID

Abstract

Bacteriophages are viruses that specifically infect bacteria. With the increase in antimicrobial resistance and a reduced availability of drugs capable of controlling multidrug-resistant infections, bacteriophages are being reconsidered as alternatives for combating bacterial infections. During bacteriophage infection of the host/target cell, proteins located on the tail of the virus (Receptor Binding Proteins, RBP) recognize specific receptors on the bacterial surface. The binding of the virus to the bacterium is called adsorption, in which the recognition between the tail proteins (RBPs) and the receptors located on the bacterial surface is highly specific. Consequently, RBPs have a high potential to be used for identifying bacterial strains (phagetyping) as well as a possible agent for the specific delivery of antibacterial agents. This project aims to identify RBPs from a lytic phage of X. citri, its receptor in the bacterium, and explore the use of these RBPs as possible agents for the delivery of antimicrobials. We intend to characterize RBPs from a phage of Xanthomonas citri (X. citri) and use them as potential carriers of anti-X. citri compounds, while simultaneously identifying the bacterial receptors used by the phage, which is crucial for optimizing phage therapy. To this end, we will construct a genomic library of a lytic bacteriophage of X. citri using a vector that allows the expression of proteins/peptides associated with the outer membrane of E. coli (protein display technique). Subsequently, we will interact this library of E. coli expressing various phage proteins, possibly RBPs, with X. citri strains sensitive to infection. Protein complexes retrieved using cross-linking techniques will be identified by mass spectrometry. Identified phage peptides could be explored as carrier agents for antibacterial agents.

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