Endoglucanase A from<i>Cellulomonas fimi</i>in which the hinge sequence of human IgA1 is substituted for the linker connecting its two domains is hydrolyzed by IgA proteases from<i>Neisseria gonorrhoeae</i>

Miller, P B; Shen, Hua; Gilkes, Neil R.; Kilburn, Douglas G.; Miller, Robert C.; Plaut, Andrew G.; Warren, R. A. J.

doi:10.1111/j.1574-6968.1992.tb05259.x

Cited by 7 publications

(2 citation statements)

References 15 publications

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“…anthracis CBD BA from G171-K245 region of AmiBA2446 were amplified from plasmids carrying the corresponding genes encoding lysostaphin and AmiBA2446, respectively. The amplified CBD SA was subcloned into plasmid PET28a between NcoI and AscI containing enhanced green fluorescent protein (EGFP), IgA hinge linker (SPSTPPTPSPSTPP), and AgNP BP (WSWRSPTPHVVT) in this specific order at the C-terminus and a Hisx6 tag and thrombin cleavage site (LVPRGS) at the N-terminus. The amplified CBD BA was subcloned into the aforementioned plasmid and restriction site but containing mRUBY in the place of EGFP.…”

Section: Experimental Sectionmentioning

confidence: 99%

Selective Killing of Pathogenic Bacteria by Antimicrobial Silver Nanoparticle—Cell Wall Binding Domain Conjugates

Kim

Kwon

et al. 2018

ACS Appl. Mater. Interfaces

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Broad-spectrum antibiotics indiscriminately kill bacteria, removing nonpathogenic microorganisms and leading to evolution of antibiotic resistant strains. Specific antimicrobials that could selectively kill pathogenic bacteria without targeting other bacteria in the natural microbial community or microbiome may be able to address this concern. In this work, we demonstrate that silver nanoparticles, suitably conjugated to a selective cell wall binding domain (CBD), can efficiently target and selectively kill bacteria. As a relevant example, CBD from Bacillus anthracis selectively bound to B. anthracis in a mixture with Bacillus subtilis, as well in a mixture with Staphylococcus aureus. This new biologically-assisted hybrid strategy, therefore, has the potential to provide selective decontamination of pathogenic bacteria with minimal impact on normal microflora.

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Section: Experimental Sectionmentioning

confidence: 99%

Selective Killing of Pathogenic Bacteria by Antimicrobial Silver Nanoparticle—Cell Wall Binding Domain Conjugates

Kim

Kwon

et al. 2018

ACS Appl. Mater. Interfaces

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“…Construction of Expression Vectors and Preparation of Biotinylated Cellulase Modules. Plasmids encoding (1) CD CelD , (2) family 3a CBM from a cellulosome-integrating protein of Clostridium thermocellum (CBM3a), 23 and (3) family 4 CBM from the second N-terminal domain of endoglucanase C from Cellulomonas f imi (CBM4), 24 all with an IgA hinge linker (SPSTPPTPSPSTPP), 25 a biotin acceptor peptide (AviTag; GGLNDIFEAQKIEWH), 26 and a polyhistidine tag (HHHHHH), in that order, at the C-termini (Figure S1, Supporting Information), were used as previously produced (pRA2b-bioCelD, pRA2b-bioCipA, and pRA2b-bioCBD2endc, respectively), 14,15 to prepare CD CelD , CBM3a, and CBM4 with AviTag.…”

Section: ■ Experimental Sectionmentioning

confidence: 99%

Hybrid Nanocellulosome Design from Cellulase Modules on Nanoparticles: Synergistic Effect of Catalytically Divergent Cellulase Modules on Cellulose Degradation Activity

et al. 2013

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Cellulosomes, which are assemblies of cellulases with various catalytic functions on a giant scaffoldin protein with a carbohydrate-binding module (CBM), efficiently degrade solid cellulosic biomass by means of synergistically coupled hydrolysis reactions. In this study, we constructed hybrid nanocellulosomes from the biotinylated catalytic domains (CDs) of two catalytically divergent cellulases (an endoglucanase and a processive endoglucanase) and biotinylated CBMs by clustering the domains and modules on streptavidin-conjugated nanoparticles. Nanocellulosomes constructed by separately clustering each type of CD with multiple CBMs on nanoparticles showed 5-fold enhancement in cellulase degradation activity relative to that of the corresponding free CDs, and mixtures of the two types of nanocellulosomes gradually and synergistically enhanced cellulase degradation activity as the CBM valency increased (finally, 2.5 times). Clustering the two types of CD together on the same nanoparticle resulted in a greater synergistic effect that was independent of CBM valency; consequently, nanocellulosomes composed of equal amounts of the endo and endoprocessive CDs clustered on a nanoparticle along with multiple CBMs (CD/CBM = 7:23) showed the best cellulose degradation activity, producing 6.5 and 2.4 times the amount of reducing sugars produced from amorphous and crystalline cellulose, respectively, by the native free CDs and CBMs in the same proportions. Our results demonstrate that hybrid nanocellulosomes constructed from the building blocks of cellulases and cellulosomes modules have the potential to serve as high-performance artificial cellulosomes.

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Versatile Substrates and Probes for IgA1 Protease Activity

et al. 2013

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Bacterial meningitis is a severe infectious disease with high mortality. Gram-positive and Gram-negative bacteria that cause meningitis secrete immunoglobulin A1 (IgA1) proteases to assist in mucosal colonization, invasion, and immune evasion. IgA1 proteases have unique selectivity, with few reported substrates other than IgA1 from human tissue. Here we describe the design, characterization, and application of peptide substrates for diverse IgA1 proteases from Neisseria, Haemophilus, and Streptococcus bacteria. IgA1 proteases from diverse strains showed unexpected selectivity profiles among peptide substrates derived from autoproteolytic sites. A fluorescence probe derived from one of these peptides was used to quantitate IgA1 protease activity in buffer and in human cerebrospinal fluid; it was able to detect recombinant Haemophilus influenzae type 1 IgA1 protease at less than 1 μg mL(-1) . We also used the probe to establish the first high-throughput screen for IgA1 protease inhibitors. This work provides tools that will help investigate the roles of IgA1 proteases in bacterial colonization, immune evasion, and infection.

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Endoglucanase A fromCellulomonas fimiin which the hinge sequence of human IgA1 is substituted for the linker connecting its two domains is hydrolyzed by IgA proteases fromNeisseria gonorrhoeae

Cited by 7 publications

References 15 publications

Selective Killing of Pathogenic Bacteria by Antimicrobial Silver Nanoparticle—Cell Wall Binding Domain Conjugates

Selective Killing of Pathogenic Bacteria by Antimicrobial Silver Nanoparticle—Cell Wall Binding Domain Conjugates

Hybrid Nanocellulosome Design from Cellulase Modules on Nanoparticles: Synergistic Effect of Catalytically Divergent Cellulase Modules on Cellulose Degradation Activity

Versatile Substrates and Probes for IgA1 Protease Activity

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