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Updated: Aug 14, 2026
Immuno-fluorescence Assay of Leptospiral Surface-exposed Proteins
Published on: July 1, 2011
Identification of Salmonella enteritidis outer membrane proteins expressed during attachment to human intestinal
A A Fadl1, K S Venkitanarayanan, M I Khan
1Department of Pathobiology, University of Connecticut, Storrs, CT 06269, USA.
Aims:
To express and identify the Salmonella enterica ser. Enteritidis outer membrane proteins that are involved in the attachment to human intestinal epithelial cells.
Methods And Results:
Salmonella Enteritidis attachment proteins were expressed by infection of human intestinal epithelial cells (int-407) with Salm. Enteritidis strain SE28, followed by pulse labelling with [35S]-methionine. Outer membrane proteins were separated by TritonX-114 phase partitioning, and were detected by Salm. Enteritidis-specific polyclonal antibody. Outer membrane proteins of molecular weights 82.3, 75.6, 49.3, 35.5 and 19.3 kDa were newly synthesized. Expression of 31.2 and 16 kDa proteins was up-regulated, whereas the expression of 40.7 kDa protein was down-regulated. Polyclonal antibodies against the 82.3 and 75.6 kDa proteins significantly (P < 0.05) reduced the binding of Salm. Enteritidis to int-407 cells in vitro.
Conclusions:
Outer membrane proteins 82.3 and 75.6 kDa are potentially involved in the attachment of Salm. Enteritidis to the intestinal mucosa.
Significance And Impact Of The Study:
Outer membrane proteins 82.3 and 75.6 kDa identified in this study could be used as potential vaccines to block or reduce Salm. Enteritidis colonization in chickens.
