The Escherichia coli O157:H7 cattle immunoproteome includes outer membrane protein A (OmpA), a modulator of adherence to bovine rectoanal junction squamous epithelial (RSE) cells. Issue 11 (9th March 2015)

• Record Type: Journal Article
• Authors: Kudva, Indira T.; Krastins, Bryan; Torres, Alfredo G.; Griffin, Robert W.; Sheng, Haiqing; Sarracino, David A.; Hovde, Carolyn J.; Calderwood, Stephen B.; John, Manohar
• Is Part Of: Proteomics. Volume 15:Issue 11(2015:Jun.)
• Page Start: 1829
• Page End: 1842
• Publication Date: 2015-03-09
• Subjects: Proteins -- Separation -- Periodicals; Bioinformatics -- Periodicals; Proteomics -- Periodicals; Genomes -- Periodicals; Molecular genetics -- Periodicals; 572.605
• DOI: 10.1002/pmic.201400432
• Languages: English
• ISSNs: 1615-9853

Abstract

<abstract abstract-type="main"> <title> <x xml:space="preserve">Abstract</x> </title> <p>Building on previous studies, we defined the repertoire of proteins comprising the immunoproteome (IP) of <italic>Escherichia coli</italic> O157:H7 (O157) cultured in DMEM supplemented with norepinephrine (O157 IP), a β‐adrenergic hormone that regulates <italic>E. coli</italic> O157 gene expression in the gastrointestinal tract, using a variation of a novel proteomics‐based platform proteome mining tool for antigen discovery, called "proteomics‐based expression library screening" (PELS; Kudva et al., 2006). The <italic>E. coli</italic> O157 IP (O157‐IP) comprised 91 proteins, and included those identified previously using proteomics‐based expression library screening, and also proteins comprising DMEM and bovine rumen fluid proteomes. Outer membrane protein A (OmpA), a common component of the above proteomes, and reportedly a contributor to <italic>E. coli</italic> O157 adherence to cultured HEp‐2 epithelial cells, was interestingly found to be a modulator rather than a contributor to <italic>E. coli</italic> O157 adherence to bovine rectoanal junction squamous epithelial cells. Our results point to a role for yet to be identified members of the O157‐IP in <italic>E. coli</italic> O157 adherence to rectoanal junction squamous epithelial cells, and additionally implicate a possible role for the outer membrane protein A regulator, TdcA, in the expression of such adhesins. Our observations have implications for the development of efficacious vaccines for preventing <italic>E. coli</italic> O157 colonization of the bovine gastrointestinal tract.</p> </abstract>