Analysis of outer membrane vesicle associated proteins isolated from the plant pathogenic bacterium Xanthomonas campestris pv. campestris
Sidhu VK, Vorhölter F-J, Niehaus K, Watt SA (2008)
BMC Microbiology 8(1): 87.
Zeitschriftenaufsatz
| Veröffentlicht | Englisch
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Autor*in
Sidhu, Vishaldeep K.;
Vorhölter, Frank-JörgUniBi;
Niehaus, KarstenUniBi;
Watt, Steven A.
Einrichtung
Abstract / Bemerkung
Background: Outer membrane vesicles (OMVs) are released from the outer membrane of many Gram-negative bacteria. These extracellular compartments are known to transport compounds involved in cell-cell signalling as well as virulence associated proteins, e. g. the cytolysine from enterotoxic E. coli. Results: We have demonstrated that Xanthomonas campestris pv. campestris (Xcc) releases OMVs into the culture supernatant during growth. A proteome study identified 31 different proteins that associate with the OMV fraction of which half are virulence-associated. A comparison with the most abundant outer membrane ( OM) proteins revealed that some proteins are enriched in the OMV fraction. This may be connected to differences in the LPS composition between the OMVs and the OM. Furthermore, a comparison of the OMV proteomes from two different culture media indicated that the culture conditions have an impact on the protein composition. Interestingly, the proteins that are common to both culture conditions are mainly involved in virulence. Conclusion: Outer membrane vesicles released from the OM of Xcc contain membrane- and virulence-associated proteins. Future experiments will prove whether these structures can serve as "vehicles" for the transport of virulence factors into the host membrane.
Erscheinungsjahr
2008
Zeitschriftentitel
BMC Microbiology
Band
8
Ausgabe
1
Seite(n)
87
ISSN
1471-2180
Page URI
https://pub.uni-bielefeld.de/record/1587298
Zitieren
Sidhu VK, Vorhölter F-J, Niehaus K, Watt SA. Analysis of outer membrane vesicle associated proteins isolated from the plant pathogenic bacterium Xanthomonas campestris pv. campestris. BMC Microbiology. 2008;8(1):87.
Sidhu, V. K., Vorhölter, F. - J., Niehaus, K., & Watt, S. A. (2008). Analysis of outer membrane vesicle associated proteins isolated from the plant pathogenic bacterium Xanthomonas campestris pv. campestris. BMC Microbiology, 8(1), 87. https://doi.org/10.1186/1471-2180-8-87
Sidhu, Vishaldeep K., Vorhölter, Frank-Jörg, Niehaus, Karsten, and Watt, Steven A. 2008. “Analysis of outer membrane vesicle associated proteins isolated from the plant pathogenic bacterium Xanthomonas campestris pv. campestris”. BMC Microbiology 8 (1): 87.
Sidhu, V. K., Vorhölter, F. - J., Niehaus, K., and Watt, S. A. (2008). Analysis of outer membrane vesicle associated proteins isolated from the plant pathogenic bacterium Xanthomonas campestris pv. campestris. BMC Microbiology 8, 87.
Sidhu, V.K., et al., 2008. Analysis of outer membrane vesicle associated proteins isolated from the plant pathogenic bacterium Xanthomonas campestris pv. campestris. BMC Microbiology, 8(1), p 87.
V.K. Sidhu, et al., “Analysis of outer membrane vesicle associated proteins isolated from the plant pathogenic bacterium Xanthomonas campestris pv. campestris”, BMC Microbiology, vol. 8, 2008, pp. 87.
Sidhu, V.K., Vorhölter, F.-J., Niehaus, K., Watt, S.A.: Analysis of outer membrane vesicle associated proteins isolated from the plant pathogenic bacterium Xanthomonas campestris pv. campestris. BMC Microbiology. 8, 87 (2008).
Sidhu, Vishaldeep K., Vorhölter, Frank-Jörg, Niehaus, Karsten, and Watt, Steven A. “Analysis of outer membrane vesicle associated proteins isolated from the plant pathogenic bacterium Xanthomonas campestris pv. campestris”. BMC Microbiology 8.1 (2008): 87.
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2019-09-06T08:48:00Z
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Wengelnik K, Bonas U., J. Bacteriol. 178(12), 1996
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Wengelnik K, Bonas U., J. Bacteriol. 178(12), 1996
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Mazia D, Schatten G, Sale W., J. Cell Biol. 66(1), 1975
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Balcerzak M, Malinowska A, Thouverey C, Sekrecka A, Dadlez M, Buchet R, Pikula S., Proteomics 8(1), 2008
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Proteomic identification of endothelial proteins isolated in situ from atherosclerotic aorta via systemic perfusion.
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