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Functional analysis of binding proteins of molybdate (ModA) and oligopeptide (OppA) from citri pv. citri

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Author(s):
Elisa Emiko Oshiro
Total Authors: 1
Document type: Doctoral Thesis
Press: São Paulo.
Institution: Universidade de São Paulo (USP). Instituto de Ciências Biomédicas (ICB/SDI)
Defense date:
Examining board members:
Rita de Cassia Cafe Ferreira; Celso Eduardo Benedetti; Vânia Santos Braz; Gabriel Padilla Maldonado; Julio Cezar Franco de Oliveira
Advisor: Rita de Cassia Cafe Ferreira
Abstract

Molybdenum is a trace element involved in nitrogen fixation, sulfur and carbon. Oligopeptides are involved in bacterial nutrition and several other intercellular signaling processes. The aim of this study was to investigate the functional role of binding proteins of molybdate (ModA) and oligopeptide (OppA) uptake systems of Xanthomonas campestris pv. citri in in vitro and in vivo conditions. ModA mutant showed a decreased production of xanthan gum, altered biofilm and adhesion impaired in vitro conditions. In vivo ModA mutant interaction showed changes in injuries on leaves of grapefruit possibly due to low expression of the gumB gene. The OppA mutant showed more cells co-aggregated by changing the structure of the biofilm and consequently reducing their capacity to adhere. In vivo, the mutant strain did not modify the phenotype of pathogenicity, but its ability for growth was affected at the early stationary phase suggesting that the Opp system plays a nutritional role. (AU)