Journal
MICROBIOLOGICAL RESEARCH
Volume 182, Issue -, Pages 109-115Publisher
ELSEVIER GMBH, URBAN & FISCHER VERLAG
DOI: 10.1016/j.micres.2015.10.004
Keywords
Enterohemorrhagic Escherichia coli; Outer membrane protein A; Peptidoglycan binding; Stress resistance; Cell adhesion
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Funding
- National Natural Science Foundation of China (NSFC) [81201257]
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Outer membrane protein A (OmpA) plays multiple roles in the physiology and pathogenesis of the zoonotic pathogen enterohemorrhagic Escherichia coli (EHEC). The N-terminus of OmpA forms a transmembrane domain (OmpA(TM)), and the roles of this domain in bacterial pathogenesis have been well studied. However, how its C-terminal domain (OmpAper), which is located at the periplasmic space in the bacterial membrane, contributes to virulence remains unclear. Herein, we report that OmpAper forms a dimer and binds to peptidoglycan in vitro. Furthermore, OmpAper is responsible for bacterial resistance to acidic conditions, high osmotic pressure and high SDS environments. In addition, OmpAper contributes to the adhesion of bacteria to HeLa cells in vitro and ex vivo. These results provide an additional understanding of the role of OmpA in EHEC physiology and pathogenesis. (c) 2015 Elsevier GmbH. All rights reserved.
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