Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/244255
Type: Artigo
Title: VapD in xylella fastidiosa Is a thermostable protein with ribonuclease activity
Author: Mendes, Juliano S.
Santiago, André da S.
Toledo, Marcelo A. S.
Rosselli-Murai
Luciana K.
Favaro, Marianna T. P.
Santos, Clelton A.
Horta, Maria Augusta C.
Crucello, Aline
Beloti, Lilian L.
Romero, Fabian
Tasic, Ljubica
Souza, Alessandra A. de|
Abstract: Xylella fastidiosa strain 9a5c is a gram-negative phytopathogen that is the causal agent of citrus variegated chlorosis (CVC), a disease that is responsible for economic losses in Brazilian agriculture. The most well-known mechanism of pathogenicity for this bacterial pathogen is xylem vessel occlusion, which results from bacterial movement and the formation of biofilms. The molecular mechanisms underlying the virulence caused by biofilm formation are unknown. Here, we provide evidence showing that virulence-associated protein D in X. fastidiosa (Xf-VapD) is a thermostable protein with ribonuclease activity. Moreover, protein expression analyses in two X. fastidiosa strains, including virulent (Xf9a5c) and nonpathogenic (XfJ1a12) strains, showed that Xf-VapD was expressed during all phases of development in both strains and that increased expression was observed in Xf9a5c during biofilm growth. This study is an important step toward characterizing and improving our understanding of the biological significance of Xf-VapD and its potential functions in the CVC pathosystem.
Xylella fastidiosa strain 9a5c is a gram-negative phytopathogen that is the causal agent of citrus variegated chlorosis (CVC), a disease that is responsible for economic losses in Brazilian agriculture. The most well-known mechanism of pathogenicity for t
Subject: Xylella fastidiosa
Proteínas
Country: Estados Unidos
Editor: Public Library of Science
Citation: Vapd In Xylella Fastidiosa Is A Thermostable Protein With Ribonuclease Activity. Public Library Science, v. 10, p. DEC-2015.
Rights: aberto
Identifier DOI: 10.1371/journal.pone.0145765
Address: https://journals.plos.org/plosone/article?id=10.1371/journal.pone.0145765
Date Issue: 2015
Appears in Collections:IQ - Artigos e Outros Documentos
IB - Artigos e Outros Documentos

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