Protein D2 porin of the <i>Pseudomonas aeruginosa</i> outer membrane bears the protease activity

Yoshihara, Eisaku; Gotoh, Naomasa; Nishino, Takeshi; Nakae, Taiji

doi:10.1016/0014-5793(96)00945-3

Cited by 19 publications

(15 citation statements)

References 15 publications

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“…Specifically, conformation specific mAbs can allosterically augment the intrinsic activity of coagulation factor VIIa (46) and intrinsic factor X-activating complex (47), as well as the protease activity of protein D2 on the outer membrane of Pseudomonas aeruginosa (48). Binding studies of TCR with SEB in the presence of mAbs (20B1, 14G8, and 6D3) show that binding was reduced when mAb 20B1, mAb 14G8, and mAb 6D3 were bound to SEB.…”

Section: Discussionmentioning

confidence: 99%

Mechanisms Mediating Enhanced Neutralization Efficacy of Staphylococcal Enterotoxin B by Combinations of Monoclonal Antibodies

Dutta

Varshney

Franklin

et al. 2015

Journal of Biological Chemistry

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Background: Staphylococcal enterotoxin B is a potent superantigen that causes lethal toxic shock syndrome. Results: Ternary and binary complex of SEB with SEB specific mAbs identified three distinct epitopes. Conclusion: Two different mechanisms illustrate how cocktails of mAbs enhance neutralization efficacy. Significance: SEB neutralization via combination of mAbs is superior to monotherapy and can include non-neutralizing mAbs.

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Section: Discussionmentioning

confidence: 99%

Mechanisms Mediating Enhanced Neutralization Efficacy of Staphylococcal Enterotoxin B by Combinations of Monoclonal Antibodies

Dutta

Varshney

Franklin

et al. 2015

Journal of Biological Chemistry

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“…OprD appeared monomeric when the OM was solubilized in SDS at low temperature (245). It was claimed to be a protease (762). However, the k cat reported was insignificant (about 10 Ϫ5 s Ϫ1 ), indicating that one cleavage occurs after tens of generations of the bacterium; clearly, this does not have any physiological relevance.…”

Section: Specific Channelsmentioning

confidence: 98%

Molecular Basis of Bacterial Outer Membrane Permeability Revisited

Nikaido

2003

Microbiol Mol Biol Rev

3,768

3,800

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Gram-negative bacteria characteristically are surrounded by an additional membrane layer, the outer membrane. Although outer membrane components often play important roles in the interaction of symbiotic or pathogenic bacteria with their host organisms, the major role of this membrane must usually be to serve as a permeability barrier to prevent the entry of noxious compounds and at the same time to allow the influx of nutrient molecules. This review summarizes the development in the field since our previous review (H. Nikaido and M. Vaara, Microbiol. Rev. 49:1-32, 1985) was published. With the discovery of protein channels, structural knowledge enables us to understand in molecular detail how porins, specific channels, TonB-linked receptors, and other proteins function. We are now beginning to see how the export of large proteins occurs across the outer membrane. With our knowledge of the lipopolysaccharide-phospholipid asymmetric bilayer of the outer membrane, we are finally beginning to understand how this bilayer can retard the entry of lipophilic compounds, owing to our increasing knowledge about the chemistry of lipopolysaccharide from diverse organisms and the way in which lipopolysaccharide structure is modified by environmental conditions

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“…In this study we explore the possibility of using mAbs as an alternative approach to obtain information about structural features determining the activity of FVIIa. The literature covering antibodies that induce catalytic activity of serine proteases is limited (21)(22)(23)(24). We describe the isolation and characterization of two groups of mAbs capable of enhancing the intrinsic activity of FVIIa.…”

Section: Blood Coagulation Factor VII (Fvii)mentioning

confidence: 99%

Antibody-induced Enhancement of Factor VIIa Activity through Distinct Allosteric Pathways

Andersen

Andreasen

Svendsen

et al. 2012

Journal of Biological Chemistry

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Background:The enzymatic activity of coagulation factor VIIa (FVIIa) is allosterically controlled by tissue factor (TF). Results: Monoclonal antibodies (mAbs) can allosterically augment the intrinsic activity of FVIIa through mechanisms distinct from that of TF. Conclusion: Different modes of allosteric activation of FVIIa appear to exist. Significance: Artificial activators of FVIIa can be tools to study the zymogen-to-protease transition.

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Protein D2 porin of the Pseudomonas aeruginosa outer membrane bears the protease activity

Cited by 19 publications

References 15 publications

Mechanisms Mediating Enhanced Neutralization Efficacy of Staphylococcal Enterotoxin B by Combinations of Monoclonal Antibodies

Mechanisms Mediating Enhanced Neutralization Efficacy of Staphylococcal Enterotoxin B by Combinations of Monoclonal Antibodies

Molecular Basis of Bacterial Outer Membrane Permeability Revisited

Antibody-induced Enhancement of Factor VIIa Activity through Distinct Allosteric Pathways

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