Gingipain-R, the major arginine-specific proteinase from Porphyromonas gingivalis, a causative agent of adult periodontal disease,

The investigators, including Stephen Dominy, MD, the chief scientific officer of Cortexyme, which has developed a gingipain inhibitor, CORE-388, identified the pathogen in the brains of patients with Alzheimer disease, as well as the organism’s gingipains—lysine-gingipain (Kgp), arginine-gingipain A (RgpA), and arginine-gingipain B (RgpB)—in the neurons of these patients.

This clinical trial is evaluating whether the investigational oral drug atuzaginstat is safe and can slow or halt the As a member of the wwPDB, the RCSB PDB curates and annotates PDB data according to agreed upon standards. The RCSB PDB also provides a variety of tools and resources. Users can perform simple and advanced searches based on annotations relating to sequence, structure and function. These molecules are visualized, downloaded, and analyzed by users who range from students to specialized scientists. The periodontal pathogen Porphyromonas gingivalis produces a unique class of cysteine proteinases termed gingipains that comprises Arg‐gingipain (Rgp) and Lys‐gingipain (Kgp). Growing evidence indicates that these 2 types of gingipains synergistically contribute to the entire virulence of the organism and increase the risk of periodontal disease (PD) by disrupting the host immune system This gingipain R structure is an excellent template for the rational design of drugs with a potential to cure and prevent periodontitis. Here we show the binding mode of an arginine-containing inhibitor in the active-site, thus identifying major interaction sites defining a suitable pharmacophor.

Gingipain

coli. Protein Tag: His-SUMO. Purity: Greater than 82.5% as determined by SDS-PAGE. From $88 Leupeptin, an Arg-gingipain-specific protease inhibitor, almost completely inhibited collagen degradation by P. gingivalis cells whereas cathepsin B inhibitor II, a Lys-gingipain inhibitor, did not. A purified preparation of Arg-gingipains A and B hydrolyzed gelatin but did not cleave type I collagen, suggesting that the enzymes must be attached to the cell surface to exert collagenase activity. 2015).

Recombinant Porphyromonas gingivalis Lys-gingipain (kgp), partial. Product Synonym Names. Lysine-specific cysteine proteinase Kgp. Product Gene Name. kgp

Lysine-specific cysteine proteinase Kgp. Product Gene Name. kgp It produces a variety of virulence factors, including the cysteine proteinases Arg- and Lys-gingipains [4]. Arg-gingipain activity is coded for by two genes (rgpA and Gingipains are a family of proteases secreted by Porphyromonas gingivalis.

Rgp gingipain activity was calculated as percent inhibition of the control RFU/min/ml values of the control (in the absence of Sanggenol A). Kgp gingipain activity was found to be more resistant to Sanggenol A (Table 2) compared to the Rgp gingipains. Sanggenol A up …

a, b, and c are representative images of Lys-gingipain in well differentiated (a), moderately differentiated (b), and poorly differentiated (c) ESCC tissues. This Recombinant Porphyromonas gingivalis Gingipain R1 (rgpA) with N-terminal 6xHis-tags is a partial protein expressed in yeast.
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Gingipain has been studied for its potential role in the development of Alzheimer's Disease. Gingipains are proteases secreted by P. gingivalis that play an indispensable role in the release of hemin from Hb. Among them, Kgp proteases are lysine-X-specific, while RgpA and RpB are arg-X-specific. From: Advances in Microbial Physiology, 2012. Download as PDF. Gingipain. Gingipains are proteases secreted by P. gingivalis that play an indispensable role in the release of hemin from Hb. Among them, Kgp proteases are lysine-X-specific, while RgpA and RpB are arg-X-specific.

This Recombinant Porphyromonas gingivalis Gingipain R1 (rgpA) with N-terminal 6xHis-tags is a partial protein expressed in yeast. Its encoding region corresponds to 228-720aa of rgpA of Porphyromonas gingivalis-origin. This recombinant rgpA protein was validated through SDS-PAGE and LC-MS/MS Analyses.
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Degradation of immunoglobulins is an effective strategy of bacteria to evade the immune system. We have tested whether human IgG is a substrate for gingipain K of Porphyromonas gingivalis and found that the enzyme can hydrolyze subclass 1 and 3 of human IgG. The heavy chain of IgG(1) was cleaved at a single site within the hinge region, generating Fab and Fc fragments.

Therefore, gingipains are often considered as therapeutic targets. Gingipains secreted by Porphyromonas gingivalis (P. gingivalis, Pg) play an important role in maintaining macrophage infiltrating.

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Arg-gingipains (RgpA and RgpB) and Lys-gingipain (Kgp) are responsible for the majority of bacterial proteolytic activity and play essential roles in bacterial virulence. Therefore, gingipains are often considered as therapeutic targets.

These also reversed AD-like changes in a mouse model of periodontal disease. Specifically, the gingipain inhibitor reduced deposits of lipids in the aortas of infected animals and prevented the progression of atherosclerosis linked to P. gingivalis infection.