| Registro completo |
| Provedor de dados: |
ArchiMer
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| País: |
France
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| Título: |
Use of OmpU porins for attachment and invasion of Crassostrea gigas immune cells by the oyster pathogen Vibrio splendidus
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| Autores: |
Duperthuy, Marylise
Schmitt, Paulina
Garzon, Edwin
Caro, Audrey
Rosa, Rafael D.
Le Roux, Frederique
Lautredou-audouy, Nicole
Got, Patrice
Romestand, Bernard
De Lorgeril, Julien
Kieffer-jaquinod, Sylvie
Bachere, Evelyne
Destoumieux-garzon, Delphine
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| Data: |
2011-02
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| Ano: |
2011
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| Palavras-chave: |
Host-pathogen interaction
Innate immunity
Invertebrate
Mollusk
Oxidative burst
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| Resumo: |
OmpU porins are increasingly recognized as key determinants of pathogenic host Vibrio interactions. Although mechanisms remain incompletely understood, various species, including the human pathogen Vibrio cholera, require OmpU for host colonization and virulence. We have shown previously that OmpU is essential for virulence in the oyster pathogen Vibrio splendidus LGP32. Here, we showed that V. splendidus LGP32 invades the oyster immune cells, the hemocytes, through subversion of host-cell actin cytoskeleton. In this process, OmpU serves as an adhesin/invasin required for beta-integrin recognition and host cell invasion. Furthermore, the major protein of oyster plasma, the extracellular superoxide dismutase Cg-EcSOD, is used as an opsonin mediating the OmpU-promoted phagocytosis through its RGD sequence. Finally, the endocytosed bacteria were found to survive intracellularly, evading the host defense by preventing acidic vacuole formation and limiting reactive oxygen species production. We conclude that (i) V. splendidus is a facultative intracellular pathogen that manipulates host defense mechanisms to enter and survive in host immune cells, and (ii) that OmpU is a major determinant of host cell invasion in Vibrio species, used by V. splendidus LGP32 to attach and invade oyster hemocytes through opsonisation by the oyster plasma Cg-EcSOD.
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| Tipo: |
Text
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| Idioma: |
Inglês
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| Identificador: |
http://archimer.ifremer.fr/doc/00031/14177/12166.pdf
DOI:10.1073/pnas.1015326108
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| Editor: |
Natl Acad Sciences
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| Relação: |
http://archimer.ifremer.fr/doc/00031/14177/
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| Formato: |
application/pdf
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| Fonte: |
Proceedings Of The National Academy Of Sciences Of The United States Of America (0027-8424) (Natl Acad Sciences), 2011-02 , Vol. 108 , N. 7 , P. 2993-2998
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| Direitos: |
2011 by the National Academy of Sciences
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