Two-dimensional electrophoresis and peptide mass fingerprinting of bacterial outer membrane proteins

2001 ◽  
Vol 22 (9) ◽  
pp. 1686-1696 ◽  
Author(s):  
Mark P. Molloy ◽  
Nikhil D. Phadke ◽  
Janine R. Maddock ◽  
Philip C. Andrews
2007 ◽  
Vol 75 (5) ◽  
pp. 2548-2561 ◽  
Author(s):  
Jenni K. Boonjakuakul ◽  
Helen L. Gerns ◽  
Yu-Ting Chen ◽  
Linda D. Hicks ◽  
Michael F. Minnick ◽  
...  

ABSTRACT Bartonella quintana is a fastidious, gram-negative, rod-shaped bacterium that causes prolonged bacteremia in immunocompetent humans and severe infections in immunocompromised individuals. We sought to define the outer membrane subproteome of B. quintana in order to obtain insight into the biology and pathogenesis of this emerging pathogen and to identify the predominant B. quintana antigens targeted by the human immune system during infection. We isolated the total membrane proteins of B. quintana and identified 60 proteins by two-dimensional sodium dodecyl sulfate-polyacrylamide gel electrophoresis and peptide mass fingerprinting. Using the newly constructed proteome map, we then utilized two-dimensional immunoblotting with sera from 21 B. quintana-infected patients to identify 24 consistently recognized, immunoreactive B. quintana antigens that have potential relevance for pathogenesis and diagnosis. Among the outer membrane proteins, the variably expressed outer membrane protein adhesins (VompA and VompB), peptidyl-prolyl cis-trans-isomerase (PpI), and hemin-binding protein E (HbpE) were recognized most frequently by sera from patients, which is consistent with surface expression of these virulence factors during human infection.


Author(s):  
Philip W. Pemberton ◽  
Robert W. Lobley ◽  
Raymond Holmes ◽  
Susanne H. Sørensen ◽  
Kenneth W. Simpson ◽  
...  

Author(s):  
Pantelis G. Bagos ◽  
Stavros J. Hamodrakas

ß-barrel outer membrane proteins constitute the second and less well-studied class of transmembrane proteins. They are present exclusively in the outer membrane of Gram-negative bacteria and presumably in the outer membrane of mitochondria and chloroplasts. During the last few years, remarkable advances have been made towards an understanding of their functional and structural features. It is now wellknown that ß-barrels are performing a large variety of biologically important functions for the bacterial cell. Such functions include acting as specific or non-specific channels, receptors for various compounds, enzymes, translocation channels, structural proteins, and adhesion proteins. All these functional roles are of great importance for the survival of the bacterial cell under various environmental conditions or for the pathogenic properties expressed by these organisms. This chapter reviews the currently available literature regarding the structure and function of bacterial outer membrane proteins. We emphasize the functional diversity expressed by a common structural motif such as the ß-barrel, and we provide evidence from the current literature for dozens of newly discovered families of transmembrane ß-barrels.


2007 ◽  
Vol 389 (4) ◽  
pp. 1033-1045 ◽  
Author(s):  
Ralf J. Braun ◽  
Norbert Kinkl ◽  
Monika Beer ◽  
Marius Ueffing

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