Please use this identifier to cite or link to this item: https://www.arca.fiocruz.br/handle/icict/30843
Title: Molecular analysis of VCA1008: a putative phosphoporin of Vibrio cholerae
Authors: Goulart, Carolina L.
Lery, Letícia M. S.
Diniz, Michelle M. P.
Vianez Junior, João L.
Ferreira, Ana Gisele C. Neves
Perales, Jonas
Bisch, Paulo M.
von Krüger, Wanda M. A.
Affilliation: Universidade Federal do Rio de Janeiro. Instituto de Biofísica Carlos Chagas Filho. Unidade Multidisciplinar de Genômica. Rio de Janeiro, RJ, Brasil.
Universidade Federal do Rio de Janeiro. Instituto de Biofísica Carlos Chagas Filho. Unidade Multidisciplinar de Genômica. Rio de Janeiro, RJ, Brasil.
Universidade Federal do Rio de Janeiro. Instituto de Biofísica Carlos Chagas Filho. Unidade Multidisciplinar de Genômica. Rio de Janeiro, RJ, Brasil.
Universidade Federal do Rio de Janeiro. Instituto de Biofísica Carlos Chagas Filho. Laboratório de Física Biológica. Rio de Janeiro, RJ, Brasil.
Fundação Oswaldo Cruz. Instituto Oswaldo Cruz. Departamento de Fisiologia e Farmacodinâmica. Rio de Janeiro, RJ. Brasil.
Fundação Oswaldo Cruz. Instituto Oswaldo Cruz. Departamento de Fisiologia e Farmacodinâmica. Rio de Janeiro, RJ. Brasil.
Universidade Federal do Rio de Janeiro. Instituto de Biofísica Carlos Chagas Filho. Unidade Multidisciplinar de Genômica. Rio de Janeiro, RJ, Brasil / Universidade Federal do Rio de Janeiro. Instituto de Biofísica Carlos Chagas Filho. Laboratório de Física Biológica. Rio de Janeiro, RJ, Brasil.
Universidade Federal do Rio de Janeiro. Instituto de Biofísica Carlos Chagas Filho. Unidade Multidisciplinar de Genômica. Rio de Janeiro, RJ, Brasil.
Abstract: The PhoB/PhoR-dependent response to inorganic phosphate (Pi)-starvation in Vibrio cholerae O1 includes the expression of vc0719 for the response regulator PhoB, vca0033 for an alkaline phosphatase and vca1008 for an outer membrane protein (OMP). Sequences with high identity to these genes have been found in the genome of clinical and environmental strains, suggesting that the Pi-starvation response in V. cholerae is well conserved. VCA1008, an uncharacterized OMP involved in V. cholerae pathogenicity, presents sequence similarity to porins of Gram-negative bacteria such as phosphoporin PhoE from Escherichia coli. A three-dimensional model shows that VCA1008 is a 16-stranded pore-forming beta-barrel protein that shares three of the four conserved lysine residues responsible for PhoE anionic specificity with PhoE. VCA1008 beta-barrel apparently forms trimers that collapse into monomers by heating. Properties such as heat modifiability and resistance to denaturation by sodium dodecyl sulfate at lower temperatures permitted us to suggest that VCA1008 is a classical porin, more precisely, a phosphoporin due to its Pi starvation-induced PhoB-dependent expression, demonstrated by electrophoretic mobility shift assay and promoter fusion-lacZ assays.
Keywords: Vibrio cholerae
VCA1008
phosphoporin
outer membrane protein
keywords: Vibrio cholerae
fosfoporina
proteína da membrana externa
Issue Date: 2009
Publisher: Oxford University Press
Citation: GOULART, Carolina L. et al. Molecularanalysis ofVCA1008: a putative phosphoporin of Vibrio cholerae. FEMS Microbiol Lett., v.298, p.241–248, 2009.
DOI: 10.1111/j.1574-6968.2009.01727.x
ISSN: 0378-1097
Copyright: restricted access
Appears in Collections:IOC - Artigos de Periódicos

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