Evidence map›Paper›PMID 31212040›Full record

ArticleBiochimie2019

Proteolytic processing and activation of gingipain zymogens secreted by T9SS of Porphyromonas gingivalis.

Florian Veillard, Maryta Sztukowska, Zuzanna Nowakowska, Danuta Mizgalska, Ida B Thøgersen, Jan J Enghild, Matthew Bogyo, Barbara Potempa, Ky-Anh Nguyen, Jan Potempa

Open access · bronzeAbstract read
In one paragraph

Article in Biochimie, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
2.0field-weighted citation impact, top 14% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

17 citing papers in PubMed, 21 citations in OpenAlex.

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  10. Comparative analysis ofMicrobiology spectrum · 2024
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  16. Intermolecular latency regulates the essential C-terminal signal peptidase and sortase of theProceedings of the National Academy of Sciences of the United States of America · 2021
    Article
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

10 authors at 5 institutions in 5 countries.

Florian VeillardUniversité de Strasbourg, CNRS, Insect Models of Innate Immunity (M3I; UPR9022), 67084, Strasbourg, France; Department of Oral Immunity and Infectious Diseases, University of Louisville School of Dentistry, Louisville, KY, USA. Electronic address: florian.veillard@gmail.com.
Maryta SztukowskaDepartment of Oral Immunity and Infectious Diseases, University of Louisville School of Dentistry, Louisville, KY, USA; University of Information Technology and Management, Rzeszow, Poland.
Zuzanna NowakowskaDepartment of Microbiology, Faculty of Biochemistry, Biophysics and Biotechnology, Jagiellonian University, Krakow, Poland; Malopolska Centre of Biotechnology, Jagiellonian University, Krakow, Poland.
Danuta MizgalskaDepartment of Microbiology, Faculty of Biochemistry, Biophysics and Biotechnology, Jagiellonian University, Krakow, Poland.
Ida B ThøgersenInterdisciplinary Nanoscience Center (iNANO), and the Department of Molecular Biology and Genetics, Aarhus University, Aarhus, DK-8000, Denmark.
Jan J EnghildInterdisciplinary Nanoscience Center (iNANO), and the Department of Molecular Biology and Genetics, Aarhus University, Aarhus, DK-8000, Denmark.
Matthew BogyoDepartment of Pathology and Department of Microbiology and Immunology, Stanford University School of Medicine, Stanford, CA, USA.
Barbara PotempaDepartment of Oral Immunity and Infectious Diseases, University of Louisville School of Dentistry, Louisville, KY, USA.
Ky-Anh NguyenDiscipline of Life Sciences, School of Dentistry, University of Sydney, Sydney, NSW, 2006, Australia; Institute of Dental Research, Westmead Centre for Oral Health, Sydney, NSW, 2145, Australia.
Jan PotempaDepartment of Oral Immunity and Infectious Diseases, University of Louisville School of Dentistry, Louisville, KY, USA; Department of Microbiology, Faculty of Biochemistry, Biophysics and Biotechnology, Jagiellonian University, Krakow, Poland. Electronic address: jan.potempa@icloud.com.
University of Louisville · USAarhus University · DKJagiellonian University · PLStanford University · USUniversity of Sydney · AU

Funding

Bacterial peptidylarginine deiminase, a link between gums and joint diseaseR01DE022597 · NIDCR · UNIVERSITY OF LOUISVILLE · PI POTEMPA, JAN S · 2013 to 2023
$3.7M
Staphylococcus serine hydrolases as targets for therapeutic and imaging contrast agentsR01EB026332 · NIBIB · STANFORD UNIVERSITY · PI BOGYO, MATTHEW · 2018 to 2021
$1.4M
Protease - protease inhibitor system of Tannerella forsythiaR21DE026280 · NIDCR · UNIVERSITY OF LOUISVILLE · PI POTEMPA, JAN S · 2016 to 2017
$424k
NIBIB NIH HHS R01 EB026332NIDCR NIH HHS R01 DE022597NIDCR NIH HHS R21 DE026280
6 · The paper itself

Abstract

Porphyromonas gingivalis uses a type IX secretion system (T9SS) to deliver more than 30 proteins to the bacterial surface using a conserved C-terminal domain (CTD) as an outer membrane translocation signal. On the surface, the CTD is cleaved and an anionic lipopolysaccharide (A-PLS) is attached by PorU sortase. Among T9SS cargo proteins are cysteine proteases, gingipains, which are secreted as inactive zymogens requiring removal of an inhibiting N-terminal prodomain (PD) for activation. Here, we have shown that the gingipain proRgpB isolated from the periplasm of a T9SS-deficient P. gingivalis strain was stable and did not undergo autocatalytic activation. Addition of purified, active RgpA or RgpB, but not Lys-specific Kgp, efficiently cleaved the PD of proRgpB but catalytic activity remained inhibited because of inhibition of the catalytic domain in trans by the PD. In contrast, active RgpB was generated from the zymogen, although at a slow rate, by gingipain-null P. gingivalis lysate or intact bacterial cell suspension. This activation was dependent on the presence of the PorU sortase. Interestingly, maturation of proRgpB with the catalytic cysteine residues mutated to Ala expressed in the ΔRgpA mutant strain was indistinguishable from that in the parental strain. Cumulatively, this suggests that PorU not only has sortase activity but is also engaged in activation of gingipain zymogens on the bacterial cell surface.

Indexed as

Bacterial ProteinsEnzyme PrecursorsGingipain Cysteine EndopeptidasesPorphyromonas gingivalisProtein Processing, Post-TranslationalSecretory PathwayBacterial ProteinsEnzyme PrecursorsGingipain Cysteine EndopeptidasesInhibitionLimited proteolysisPeriodontal diseasePosttranslational modificationProdomainSecretionSortase

Identifiers

PMID31212040
PMCPMC6815250
OpenAlexW2949365390

What OpenQuestion holds

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Registered trials

None linked

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.