Abstract
Interactions between pathogenic bacteria and host cells are often mediated by proteins found on the surfaces of the bacteria. The Gram-negative bacterium Helicobacter pylori is predicted to produce at least 50 surface-exposed outer membrane proteins, but there has been relatively little progress in experimentally analyzing the cell-surface proteome of this organism. Herein, we describe in detail a protocol that allows biotinylation and purification of surface-exposed H. pylori proteins. A comparative analysis of surface-exposed proteins identified by this biotinylation-based approach and by several other independent methods is described in a recent publication (Voss et al., 2014).
Keywords: Outer membrane proteins, Autotransporter, Type V secretion, Adhesin, Helicobacter pylori
Materials and Reagents
Equipment
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Notes
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Acknowledgments
The biotinylation protocol described here and in Voss et al. (2014) is modified from a protocol described in Sabarth et al. (2002). Supported by the Department of Veterans Affairs, Merit Review grant 2I01 BX000627.
References
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