Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/195560
Type: Artigo de periódico
Title: Proteome Analysis Of The Plant Pathogen Xylella Fastidiosa Reveals Major Cellular And Extracellular Proteins And A Peculiar Codon Bias Distribution.
Author: Smolka, Marcus Bustamante
Martins-de-Souza, Daniel
Martins, Daniel
Winck, Flavia Vischi
Santoro, Carlos Eduardo
Castellari, Rafael Ramos
Ferrari, Fernanda
Brum, Itaraju Junior
Galembeck, Eduardo
Della Coletta Filho, Helvécio
Machado, Marcos Antonio
Marangoni, Sergio
Novello, Jose Camillo
Abstract: The bacteria Xylella fastidiosa is the causative agent of a number of economically important crop diseases, including citrus variegated chlorosis. Although its complete genome is already sequenced, X. fastidiosa is very poorly characterized by biochemical approaches at the protein level. In an initial effort to characterize protein expression in X. fastidiosa we used one- and two-dimensional gel electrophoresis and mass spectrometry to identify the products of 142 genes present in a whole cell extract and in an extracellular fraction of the citrus isolated strain 9a5c. Of particular interest for the study of pathogenesis are adhesion and secreted proteins. Homologs to proteins from three different adhesion systems (type IV fimbriae, mrk pili and hsf surface fibrils) were found to be coexpressed, the last two being detected only as multimeric complexes in the high molecular weight region of one-dimensional electrophoresis gels. Using a procedure to extract secreted proteins as well as proteins weakly attached to the cell surface we identified 30 different proteins including toxins, adhesion related proteins, antioxidant enzymes, different types of proteases and 16 hypothetical proteins. These data suggest that the intercellular space of X. fastidiosa colonies is a multifunctional microenvironment containing proteins related to in vivo bacterial survival and pathogenesis. A codon usage analysis of the most expressed proteins from the whole cell extract revealed a low biased distribution, which we propose is related to the slow growing nature of X. fastidiosa. A database of the X. fastidiosa proteome was developed and can be accessed via the internet (URL: www.proteome.ibi.unicamp.br).
Subject: Antioxidants
Bacterial Adhesion
Bacterial Proteins
Codon
Databases As Topic
Electrophoresis, Gel, Two-dimensional
Electrophoresis, Polyacrylamide Gel
Gammaproteobacteria
Genome, Bacterial
Image Processing, Computer-assisted
Iron
Mass Spectrometry
Open Reading Frames
Peptides
Plant Diseases
Porins
Proteome
Rights: fechado
Identifier DOI: 10.1002/pmic.200390031
Address: http://www.ncbi.nlm.nih.gov/pubmed/12601815
Date Issue: 2003
Appears in Collections:Artigos e Materiais de Revistas Científicas - Unicamp

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