Defining a core set of actin cytoskeletal proteins critical for actin-based motility of Rickettsia.
Cell Host Microbe
; 7(5): 388-98, 2010 May 20.
Article
em En
| MEDLINE
| ID: mdl-20478540
ABSTRACT
Many Rickettsia species are intracellular bacterial pathogens that use actin-based motility for spread during infection. However, while other bacteria assemble actin tails consisting of branched networks, Rickettsia assemble long parallel actin bundles, suggesting the use of a distinct mechanism for exploiting actin. To identify the underlying mechanisms and host factors involved in Rickettsia parkeri actin-based motility, we performed an RNAi screen targeting 115 actin cytoskeletal genes in Drosophila cells. The screen delineated a set of four core proteins-profilin, fimbrin/T-plastin, capping protein, and cofilin--as crucial for determining actin tail length, organizing filament architecture, and enabling motility. In mammalian cells, these proteins were localized throughout R. parkeri tails, consistent with a role in motility. Profilin and fimbrin/T-plastin were critical for the motility of R. parkeri but not Listeria monocytogenes. Our results highlight key distinctions between the evolutionary strategies and molecular mechanisms employed by bacterial pathogens to assemble and organize actin.
Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Rickettsia
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Glicoproteínas de Membrana
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Proteínas de Capeamento de Actina
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Fatores de Despolimerização de Actina
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Profilinas
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Proteínas dos Microfilamentos
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Movimento (Física)
Tipo de estudo:
Prognostic_studies
Limite:
Animals
Idioma:
En
Revista:
Cell Host Microbe
Ano de publicação:
2010
Tipo de documento:
Article