title: Genomics and X-ray microanalysis indicate that Ca2+ and thiols mediate the aggregation and adhesion of Xylella fastidiosa.
abstract: The availability of the genome sequence of the bacterial plant pathogen Xylella fastidiosa, the causal agent of citrus variegated chlorosis, is accelerating important investigations concerning its pathogenicity. Plant vessel occlusion is critical for symptom development. The objective of the present study was to search for information that would help to explain the adhesion of X. fastidiosa cells to the xylem. Scanning electron microscopy revealed that adhesion may occur without the fastidium gum, an exopolysaccharide produced by X. fastidiosa, and X-ray microanalysis demonstrated the presence of elemental sulfur both in cells grown in vitro and in cells found inside plant vessels, indicating that the sulfur signal is generated by the pathogen surface. Calcium and magnesium peaks were detected in association with sulfur in occluded vessels. We propose an explanation for the adhesion and aggregation process. Thiol groups, maintained by the enzyme peptide methionine sulfoxide reductase, could be active on the surface of the bacteria and appear to promote cell-cell aggregation by forming disulfide bonds with thiol groups on the surface of adjacent cells. The enzyme methionine sulfoxide reductase has been shown to be an auxiliary component in the adhesiveness of some human pathogens. The negative charge conferred by the ionized thiol group could of itself constitute a mechanism of adhesion by allowing the formation of divalent cation bridges between the negatively charged bacteria and predominantly negatively charged xylem walls.
authors.affiliation: Departamento de Entomologia, Fitopatologia e Zoologia Agrícola, Escola Superior de Agricultura Luiz de Queiroz, Universidade de São Paulo, Piracicaba, SP, Brasil. bleite@mail.ifas.ufl.edu
authors.forename: B
authors.initials: B
authors.lastname: Leite
authors.forename: M L
authors.initials: ML
authors.lastname: Ishida
authors.forename: E
authors.initials: E
authors.lastname: Alves
authors.forename: H
authors.initials: H
authors.lastname: Carrer
authors.forename: S F
authors.initials: SF
authors.lastname: Pascholati
authors.forename: E W
authors.initials: EW
authors.lastname: Kitajima
mesh_terms: D001422:Bacterial Adhesion / Q000502:physiology*; D002118:Calcium / Q000737:chemistry / Q000378:metabolism*; D002957:Citrus / Q000737:chemistry / Q000382:microbiology*; D004577:Electron Probe Microanalysis; D020563:Gammaproteobacteria / Q000235:genetics / Q000502:physiology* / Q000648:ultrastructure; D016680:Genome, Bacterial; D008274:Magnesium / Q000737:chemistry; D051150:Methionine Sulfoxide Reductases; D010088:Oxidoreductases / Q000737:chemistry / Q000378:metabolism; D010935:Plant Diseases / Q000382:microbiology*; D013438:Sulfhydryl Compounds / Q000737:chemistry / Q000378:metabolism*; D013455:Sulfur / Q000737:chemistry
chemical_list: D013438:Sulfhydryl Compounds; D013455:Sulfur; D010088:Oxidoreductases; D051150:Methionine Sulfoxide Reductases; C027219:methionine sulfoxide reductase; D008274:Magnesium; D002118:Calcium