Study on the relevance in pathogenesis of the perception of amino acids and derivates in the phytopathogenic bacteria pseudomonas syrangae pv. tomato

Díaz Bárcena, Alba (2019). Study on the relevance in pathogenesis of the perception of amino acids and derivates in the phytopathogenic bacteria pseudomonas syrangae pv. tomato. Proyecto Fin de Carrera / Trabajo Fin de Grado, E.T.S. de Ingeniería Agronómica, Alimentaria y de Biosistemas (UPM), Madrid.

Description

Title: Study on the relevance in pathogenesis of the perception of amino acids and derivates in the phytopathogenic bacteria pseudomonas syrangae pv. tomato
Author/s:
  • Díaz Bárcena, Alba
Contributor/s:
  • López Solanilla, Emilia A.
  • Santamaría Hernando, Saray
Item Type: Final Project
Degree: Grado en Biotecnología
Date: June 2019
Subjects:
Faculty: E.T.S. de Ingeniería Agronómica, Alimentaria y de Biosistemas (UPM)
Department: Biotecnología - Biología Vegetal
Creative Commons Licenses: Recognition - No derivative works - Non commercial

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Abstract

Pseudomonas syringae pv. tomato DC3000 (PsPto) is the causal agent of bacterial speck of tomato, an important agricultural disease. PsPto displays a short initial epiphytic phase followed by an aggressive pathogenic phase in plant apoplast. As other plant-pathogens, PsPto senses different plant signals in order to activate motility mechanisms and to colonize plant tissues through natural openings or via mechanical wounds. One of the signal perception mechanisms in bacteria is mediated by the function of Methyl-accepting Chemotaxis Proteins (MCPs) specialized in the binding to the putative chemical signal. Amino acids levels in plant change during bacterial infection. Moreover, these compounds have been shown to play an important role in plant defense. Therefore, the recognition of these changes seems to be decisive for PsPto success. In this work the functional characterization of PsPto_1061 and PsPto_3379 chemoreceptors has been approached. In vivo assays using a mutant strain in PsPto_1061 MCP have allowed us to determine the relevance of this chemoreceptor not only in the perception of amino acids, but also in virulence process. PsPto_1061 mutant strain was impaired on the perception of L-Homoserine, L-Tryptophan, L-Asparagine, L-Methionine and L-Phenylalanine and showed less virulence than the wild type strain. These results suggest that bacteria exploit amino acid perception to optimize virulence. After several attempts it was not possible to obtain the mutant strain in PsPto_3379 chemoreceptor. Therefore, the in vivo functional characterization of this MCP could not be carried out. Recombinant expression and purification of PsPto_3379 LBD has been optimized which would allow in vitro assays to determine its ligand binding profile. Preliminary thermal shift assays performed with the purified recombinant LBD revealed that it does not bind GABA, L-Homoserine and L-Phenylalanine.

More information

Item ID: 56924
DC Identifier: http://oa.upm.es/56924/
OAI Identifier: oai:oa.upm.es:56924
Deposited by: Biblioteca ETSI Agrónomos
Deposited on: 17 Oct 2019 11:54
Last Modified: 17 Oct 2019 11:55
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