Journal ArticleDOI
Degradation of outer membrane protein A in Escherichia coli killing by neutrophil elastase
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TLDR
It is found that neutrophil elastase degraded outer membrane protein A (OmpA), localized on the surface of Gram-negative bacteria, defining a mechanism of nonoxidative bacterial killing by NE and point to OmpA as a bacterial target in host defense.Abstract:
In determining the mechanism of neutrophil elastase (NE)-mediated killing of Escherichia coli, we found that NE degraded outer membrane protein A (OmpA), localized on the surface of Gram-negative bacteria. NE killed wild-type, but not OmpA-deficient, E. coli. Also, whereas NE-deficient mice had impaired survival in response to E. coli sepsis, as compared to wild-type mice, the presence or absence of NE had no influence on survival in response to sepsis that had been induced with OmpA-deficient E. coli. These findings define a mechanism of nonoxidative bacterial killing by NE and point to OmpA as a bacterial target in host defense.read more
Citations
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Myeloperoxidase: friend and foe
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Neutrophil Elastase, Proteinase 3, and Cathepsin G as Therapeutic Targets in Human Diseases
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References
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Journal ArticleDOI
Mice lacking neutrophil elastase reveal impaired host defense against gram negative bacterial sepsis.
Abderrazzaq Belaaouaj,Ronald McCarthy,Mary Baumann,Zhimin Gao,Timothy J. Ley,Soman N. Abraham,Steven D. Shapiro +6 more
TL;DR: It is shown that NE−/− mice are more susceptible than their normal littermates to sepsis and death following intraperitoneal infection with Cram negative (Klebsiella pneumoniae and Escherichia coli) but not Cram positive (Staphylococcus aureus) bacteria.
Journal ArticleDOI
Cloning and characterization of a unique elastolytic metalloproteinase produced by human alveolar macrophages.
TL;DR: HME is a unique human metalloproteinase that possesses elastolytic activity and is expressed in alveolar macrophages; it is therefore a candidate molecule for the causation of diseases characterized by damage to the extracellular matrix.
Journal ArticleDOI
Porin channels in Escherichia coli: studies with liposomes reconstituted from purified proteins.
Hiroshi Nikaido,E Y Rosenberg +1 more
TL;DR: The results suggest that PhoE specializes in the uptake of negatively charged solutes, and no sign of true solute specificity was found in OmpF and OmpC channels; peptides diffused through both of these channels at rates expected from their molecular size, hydrophobicity, and charge.
Journal ArticleDOI
Outer membrane protein A of Escherichia coli contributes to invasion of brain microvascular endothelial cells.
Nemani V. Prasadarao,Carol A. Wass,Jeffrey N. Weiser,Monique F. Stins,Sheng H.E. Huang,Kwang Sik Kim +5 more
TL;DR: Outer membrane protein A (OmpA), a highly conserved 35-kDa protein, was examined for its role in E. coli invasion of brain microvascular endothelial cells (BMEC) and it is suggested that OmpA is the first microbial structure identified to enhanceE.
Journal ArticleDOI
Outer membrane protein A (OmpA) contributes to serum resistance and pathogenicity of Escherichia coli K-1.
TL;DR: Results suggest that OmpA contributes to E. coli K-1 pathogenesis by a mechanism which may involve increased serum resistance, and the ompA mutant was more sensitive to the bactericidal effect of pooled human serum by the classical pathway of complement activation.