Use of OmpU porins for attachment and invasion of Crassostrea gigas immune cells by the oyster pathogen Vibrio splendidus

Marylise Duperthuy, Paulina Schmitt, Edwin Garzón, Audrey Caro, Rafael D. Rosa, Frédérique Le Roux, Nicole Lautrédou-Audouy, Patrice Got, Bernard Romestand, Julien De Lorgeril, Sylvie Kieffer-Jaquinod, Evelyne Bachère, Delphine Destoumieux-Garzón

Resultado de la investigación: Contribución a una revistaArtículorevisión exhaustiva

131 Citas (Scopus)

Resumen

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 β-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.

Idioma originalInglés
Páginas (desde-hasta)2993-2998
Número de páginas6
PublicaciónProceedings of the National Academy of Sciences of the United States of America
Volumen108
N.º7
DOI
EstadoPublicada - 15 feb. 2011
Publicado de forma externa

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