ReviewEuropean journal of microbiology & immunology2011
Gingipains from Porphyromonas gingivalis - Complex domain structures confer diverse functions.
Review in European journal of microbiology & immunology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 67 papers.
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Who cites it
67 citing papers in PubMed, 107 citations in OpenAlex.
- Markerless gene deletion inMicrobiology spectrum · 2026Article
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- Virulence diversity amongJournal of oral microbiology · 2026Review
- Salivary proteins, proteases, and disease pathophysiology in oral health and precision diagnostics: a narrative review.Frontiers in dental medicine · 2026Review
- The Presence and Tissue Distribution ofInternational journal of dentistry · 2026Article
- Synergistic Roles of Fimbriae and Gingipain Genotypes inInternational journal of dentistry · 2026Article
- Porphromonas gingivalis infection induces gingipain-dependent changes in the brain vasculature of zebrafish larvae.Cell communication and signaling : CCS · 2025Article
- Microbial Coaggregation in the Oral Cavity: Molecular Interactions and Current Insights.International journal of molecular sciences · 2025Review
- The Role ofCancers · 2025Review
- Pathotype-Specific Expression of Granzyme-Perforin Pathway Genes and Their Association With Clinical Disease Activity in Early Rheumatoid Arthritis and in a Randomized Clinical Trial.Immune network · 2025Article
- In Silico Docking of Medicinal Herbs Against P. gingivalis for Chronic Periodontitis Intervention.International dental journal · 2025Article
- Review
- Exploring heme and iron acquisition strategies of Porphyromonas gingivalis-current facts and hypotheses.FEMS microbiology reviews · 2025Review
- Ozone ultrafine bubble water sterilizes Porphyromonas gingivalis and neutralizes its virulence factors.PloS one · 2025Article
- Microbiological and molecular aspects of periodontitis pathogenesis: an infection-induced inflammatory condition.Frontiers in cellular and infection microbiology · 2025Review
- Article
- Bacterial interactions with platelets: defining key themes.Frontiers in immunology · 2025Review
- Defining the role of Hmu and Hus systems in Porphyromonas gingivalis heme and iron homeostasis and virulence.Scientific reports · 2024Article
- Molecularly imprinted nanogels as synthetic recognition materials for the ultrasensitive detection of periodontal disease biomarkers.Analytical and bioanalytical chemistry · 2024Article
- Oral Pathobiont-Derived Outer Membrane Vesicles in the Oral-Gut Axis.International journal of molecular sciences · 2024Review
7 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Gingipains, a group of arginine or lysine specific cysteine proteinases (also known as RgpA, RgpB and Kgp), have been recognized as major virulence factors in Porphyromonas gingivalis. This bacterium is one of a handful of pathogens that cause chronic periodontitis. Gingipains are involved in adherence to and colonization of epithelial cells, haemagglutination and haemolysis of erythrocytes, disruption and manipulation of the inflammatory response, and the degradation of host proteins and tissues. RgpA and Kgp are multi-domain proteins composed of catalytic domains and haemagglutinin/adhesin (HA) regions. The structure of the HA regions have previously been defined by a gingipain domain structure hypothesis which is a set of putative domain boundaries derived from the sequences of fragments of these proteins extracted from the cell surface. However, multiple sequence alignments and hidden Markov models predict an alternative domain architecture for the HA regions of gingipains. In this alternate model, two or three repeats of the so-called "cleaved adhesin" domains (and one other undefined domain in some strains) are the modules which constitute the substructure of the HA regions. Recombinant forms of these putative cleaved adhesin domains are indeed stable folded protein modules and recently determined crystal structures support the hypothesis of a modular organisation of the HA region. Based on the observed K2 and K3 structures as well as multiple sequence alignments, it is proposed that all the cleaved adhesin domains in gingipains will share the same β-sandwich jelly roll fold. The new domain model of the structure for gingipains and the haemagglutinin (HagA) proteins of P. gingivalis will guide future functional studies of these virulence factors.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.