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1.
BMC Microbiol ; 8: 108, 2008 Jun 27.
Artigo em Inglês | MEDLINE | ID: mdl-18588687

RESUMO

BACKGROUND: The Burkholderia cepacia complex (Bcc) is a collection of nine genotypically distinct but phenotypically similar species. They show wide ecological diversity and include species that are used for promoting plant growth and bio-control as well species that are opportunistic pathogens of vulnerable patients. Over recent years the Bcc have emerged as problematic pathogens of the CF lung. Pseudomonas aeruginosa is another important CF pathogen. It is able to synthesise hydrogen cyanide (HCN), a potent inhibitor of cellular respiration. We have recently shown that HCN production by P. aeruginosa may have a role in CF pathogenesis. This paper describes an investigation of the ability of bacteria of the Bcc to make HCN. RESULTS: The genome of Burkholderia cenocepacia has 3 putative HCN synthase encoding (hcnABC) gene clusters. B. cenocepacia and all 9 species of the Bcc complex tested were able to make cyanide at comparable levels to P. aeruginosa, but only when grown surface attached as colonies or during biofilm growth on glass beads. In contrast to P. aeruginosa and other cyanogenic bacteria, cyanide was not detected during planktonic growth of Bcc strains. CONCLUSION: All species in the Bcc are cyanogenic when grown as surface attached colonies or as biofilms.


Assuntos
Biofilmes , Complexo Burkholderia cepacia/metabolismo , Complexo Burkholderia cepacia/fisiologia , Cianeto de Hidrogênio/metabolismo , Ágar , Sequência de Aminoácidos , Meios de Cultura , Genoma Bacteriano , Vidro , Dados de Sequência Molecular , Oxirredutases atuantes sobre Doadores de Grupo CH-NH2/metabolismo , Fenótipo , Pseudomonas aeruginosa/metabolismo , Pseudomonas aeruginosa/fisiologia , Alinhamento de Sequência
2.
J Biol Chem ; 281(13): 8756-64, 2006 Mar 31.
Artigo em Inglês | MEDLINE | ID: mdl-16434390

RESUMO

Rho-family proteins play a central role in most actin-dependent processes, including the control and maintenance of cell shape, adhesion, motility, and phagocytosis. Activation of these GTP-binding proteins is tightly regulated spatially and temporally; however, very little is known of the mechanisms involved in their recruitment and activation in vivo. Because of its inducible, restricted signaling, phagocytosis offers an ideal physiological system to delineate the pathways linking surface receptors to actin remodeling via Rho GTPases. In this study, we investigated the involvement of early regulators of Fcgamma receptor signaling in Rac recruitment and activation. Using a combination of receptor mutagenesis, cellular, molecular, and pharmacological approaches, we show that Src family and Syk kinases control Rac and Vav function during phagocytosis. Importantly, both the immunoreceptor tyrosine-based activation motif within Fcgamma receptor cytoplasmic domain and Src kinase control the recruitment of Vav and Rac. However, Syk activity is dispensable for Vav and Rac recruitment. Moreover, we show that Rac and Cdc42 activities coordinate F-actin accumulation at nascent phagosomes. Our results provide new insights in the understanding of the spatiotemporal regulation of Rho-family GTPase function, and of Rac in particular, during phagocytosis. We believe they will contribute to a better understanding of more complex cellular processes, such as cell adhesion and migration.


Assuntos
Fagocitose , Receptores de IgG/metabolismo , Proteínas rac de Ligação ao GTP/metabolismo , Actinas/metabolismo , Animais , Células COS , Linhagem Celular , Chlorocebus aethiops , Ativação Enzimática , Fluoresceína-5-Isotiocianato , Técnica Indireta de Fluorescência para Anticorpo , Corantes Fluorescentes , Peptídeos e Proteínas de Sinalização Intracelular/metabolismo , Macrófagos/metabolismo , Camundongos , Microscopia Confocal , Modelos Biológicos , Proteínas Opsonizantes/farmacologia , Faloidina , Fosforilação , Proteínas Tirosina Quinases/metabolismo , Proteínas Proto-Oncogênicas c-vav/análise , Proteínas Proto-Oncogênicas c-vav/metabolismo , Quinase Syk , Proteínas rac de Ligação ao GTP/análise , Quinases da Família src/metabolismo
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