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פותח על ידי קלירמאש פתרונות בע"מ -
OmpA of a septicemic Escherichia coli O78 - Secretion and convergent evolution
Year:
2004
Authors :
רוזן, רן
;
.
Volume :
294
Co-Authors:
Gophna, U., Dept. Molec. Microbiol. and Biotech., George S. Wise Fac. of Life Sciences, Tel Aviv University, Tel Aviv, Israel
Ideses, D., Dept. Molec. Microbiol. and Biotech., George S. Wise Fac. of Life Sciences, Tel Aviv University, Tel Aviv, Israel
Rosen, R., Dept. Molec. Microbiol. and Biotech., George S. Wise Fac. of Life Sciences, Tel Aviv University, Tel Aviv, Israel
Grundland, A., Dept. Molec. Microbiol. and Biotech., George S. Wise Fac. of Life Sciences, Tel Aviv University, Tel Aviv, Israel
Ron, E.Z., Dept. Molec. Microbiol. and Biotech., George S. Wise Fac. of Life Sciences, Tel Aviv University, Tel Aviv, Israel
Facilitators :
From page:
373
To page:
381
(
Total pages:
9
)
Abstract:
OmpA is an important constituent of the outer membrane of Gram-negative bacteria. OmpA is involved in a variety of host-bacteria interactions, including crossing of the blood-brain barrier by E. coli strains causing newborn meningitis, and elicits a significant response by the immune system of the host. The bactericidal effect of neutrophil elastase (NE) is also attributed to degradation of the bacterial OmpA. Here we examined the OmpA of septicemic E. coli O78 strains and show that two surface-exposed loops are conserved among invasive strains of E. coli and other pathogenic Enterobacteriaceae. In addition, there is evidence for convergent evolution, implying the existence of selective pressure. Our results also indicate that large quantities of OmpA are secreted into the medium during all phases of growth, where it is present both in secreted vesicles and as a soluble secreted protein. We assume that secreted OmpA can play a role in protection of bacteria from NE by competitive inhibition. Support for this assumption was obtained from experiments indicating that addition of exogenous, purified OmpA reduces killing of bacteria by NE. © 2004 Elsevier GmbH. All rights reserved.
Note:
Related Files :
bacterial strain
Enterobacteriaceae
gene sequence
Molecular Evolution
Outer membrane proteins
Shigella flexneri
unclassified drug
עוד תגיות
תוכן קשור
More details
DOI :
10.1016/j.ijmm.2004.08.004
Article number:
Affiliations:
Database:
סקופוס
Publication Type:
מאמר
;
.
Language:
אנגלית
Editors' remarks:
ID:
29388
Last updated date:
02/03/2022 17:27
Creation date:
17/04/2018 00:46
Scientific Publication
OmpA of a septicemic Escherichia coli O78 - Secretion and convergent evolution
294
Gophna, U., Dept. Molec. Microbiol. and Biotech., George S. Wise Fac. of Life Sciences, Tel Aviv University, Tel Aviv, Israel
Ideses, D., Dept. Molec. Microbiol. and Biotech., George S. Wise Fac. of Life Sciences, Tel Aviv University, Tel Aviv, Israel
Rosen, R., Dept. Molec. Microbiol. and Biotech., George S. Wise Fac. of Life Sciences, Tel Aviv University, Tel Aviv, Israel
Grundland, A., Dept. Molec. Microbiol. and Biotech., George S. Wise Fac. of Life Sciences, Tel Aviv University, Tel Aviv, Israel
Ron, E.Z., Dept. Molec. Microbiol. and Biotech., George S. Wise Fac. of Life Sciences, Tel Aviv University, Tel Aviv, Israel
OmpA of a septicemic Escherichia coli O78 - Secretion and convergent evolution
OmpA is an important constituent of the outer membrane of Gram-negative bacteria. OmpA is involved in a variety of host-bacteria interactions, including crossing of the blood-brain barrier by E. coli strains causing newborn meningitis, and elicits a significant response by the immune system of the host. The bactericidal effect of neutrophil elastase (NE) is also attributed to degradation of the bacterial OmpA. Here we examined the OmpA of septicemic E. coli O78 strains and show that two surface-exposed loops are conserved among invasive strains of E. coli and other pathogenic Enterobacteriaceae. In addition, there is evidence for convergent evolution, implying the existence of selective pressure. Our results also indicate that large quantities of OmpA are secreted into the medium during all phases of growth, where it is present both in secreted vesicles and as a soluble secreted protein. We assume that secreted OmpA can play a role in protection of bacteria from NE by competitive inhibition. Support for this assumption was obtained from experiments indicating that addition of exogenous, purified OmpA reduces killing of bacteria by NE. © 2004 Elsevier GmbH. All rights reserved.
Scientific Publication
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