Outer membrane vesicles are vehicles for the delivery of Vibrio tasmaniensis virulence factors to oyster immune cells
|Author(s)||Vanhove Audrey1, 2, 3, 4, 5, Duperthuy Marylise2, 6, Charriere Guillaume1, 2, 3, 4, 5, Le Roux Frederique7, 8, 9, Goudenege David7, 8, 9, Gourbal Benjamin10, Kieffer-Jaquinod Sylvie11, 12, 13, Coute Yohann11, 12, 13, Wai Sun Nyunt6, Destoumieux-Garzon Delphine1, 2, 3, 4, 5|
|Affiliation(s)||1 : CNRS, UMR 5119, Ecol Coastal Marine Syst, F-34095 Montpellier, France.
2 : IFREMER, Ecol Coastal Marine Syst, F-34095 Montpellier, France.
3 : Univ Montpellier I, Ecol Coastal Marine Syst, F-34095 Montpellier, France.
4 : Univ Montpellier 2, Ecol Coastal Marine Syst, F-34095 Montpellier, France.
5 : IRD, F-34095 Montpellier, France.
6 : Umea Univ, Dept Mol Biol, Lab Mol Infect Med Sweden MIMS, S-90187 Umea, Sweden.
7 : IFREMER, Unite Physiol Fonct Organismes Marins, F-29280 Plouzane, France.
8 : Univ Paris 04, Univ Paris 06, Integrat Biol Marine Models, F-29688 Roscoff, France.
9 : CNRS, Stn Biol Roscoff, UMR 8227, Integrat Biol Marine Models, F-29688 Roscoff, France.
10 : Univ Perpignan, CNRS, UMR 5244, Ecol & Evolut Interact, F-66860 Perpignan, France.
11 : Univ Grenoble Alpes, U1038, F-38054 Grenoble, France.
12 : CEA Grenoble, Biol Grande Echelle, IRTSV, F-38054 Grenoble, France.
13 : INSERM, U1038, F-38054 Grenoble, France.
|Source||Environmental Microbiology (1462-2912) (Wiley-blackwell), 2015-04 , Vol. 17 , N. 4 , P. 1152-1165|
|WOS© Times Cited||50|
|Note||Special Issue: Pathogen ecology and lifestyles|
|Abstract||Vibrio tasmaniensis LGP32, a facultative intracellular pathogen of oyster haemocytes, was shown here to release outer membrane vesicles (OMVs) both in the extracellular milieu and inside haemocytes. Intracellular release of OMVs occurred inside phagosomes of intact haemocytes having phagocytosed few vibrios as well as in damaged haemocytes containing large vacuoles heavily loaded with LGP32. The OMV proteome of LGP32 was shown to be rich in hydrolases (25%) including potential virulence factors such as proteases, lipases, phospholipases, haemolysins and nucleases. One major caseinase/gelatinase named Vsp for vesicular serine protease was found to be specifically secreted through OMVs in which it is enclosed. Vsp was shown to participate in the virulence phenotype of LGP32 in oyster experimental infections. Finally, OMVs were highly protective against antimicrobial peptides, increasing the minimal inhibitory concentration of polymyxin B by 16-fold. Protection was conferred by OMV titration of polymyxin B but did not depend on the activity of Vsp or another OMV-associated protease. Altogether, our results show that OMVs contribute to the pathogenesis of LGP32, being able to deliver virulence factors to host immune cells and conferring protection against antimicrobial peptides.|