Evidence map›Paper›PMID 32810871›Full record

ArticleGlycobiology2021

Characterization of the β-glucuronidase Pn3Pase as the founding member of glycoside hydrolase family GH169.

Paeton L Wantuch, Satya Jella, Jeremy A Duke, Jarrod J Mousa, Bernard Henrissat, John Glushka, Fikri Y Avci

Open access · greenAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Glycobiology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.5field-weighted citation impact, top 40% 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

4 citing papers in PubMed, 8 citations in OpenAlex.

  1. Functional domains ofFrontiers in microbiology · 2024
    Article
  2. Review
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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

7 authors at 2 institutions in 3 countries.

Paeton L WantuchDepartment of Biochemistry & Molecular Biology, University of Georgia, 325 Riverbend Rd, Athens GA 30602, USA.
Satya JellaCenter for Molecular Medicine, University of Georgia, 325 Riverbend Rd, Athens GA 30602, USA.
Jeremy A DukeDepartment of Biochemistry & Molecular Biology, University of Georgia, 325 Riverbend Rd, Athens GA 30602, USA.
Jarrod J MousaCenter for Vaccines and Immunology, College of Veterinary Medicine, University of Georgia, 501 D.W. Brooks Dr Athens, Athens GA 30602, USA.
Bernard HenrissatArchitecture et Fonction des Macromolécules Biologiques, CNRS, Aix-Marseille University, 163 Avenue de Luminy, Parc Scientifique et Technologique de Luminy, 13288 Marseille, France.
John GlushkaComplex Carbohydrate Research Center, University of Georgia, 315 Riverbend Rd, Athens GA 30602, USA.
Fikri Y AvciDepartment of Biochemistry & Molecular Biology, University of Georgia, 325 Riverbend Rd, Athens GA 30602, USA.
University of Georgia · USCentre National de la Recherche Scientifique · FR

Funding

Molecular Mechanisms for Carbohydrate Presentation to CD4+ T cells by MHCII PathwayR01AI123383 · NIAID · UNIVERSITY OF GEORGIA · PI Fikri Y Avci · 2016 to 2026
$4.2M
Glycoscience Training ProgramT32GM107004 · NIGMS · UNIVERSITY OF GEORGIA · PI AMSTER, I JONATHAN, HALTIWANGER, ROBERT S. · 2014 to 2021
$1.3M
Therapeutic antibodies to treat Pneumocystis pneumonia in a nonhuman primate model of HIV infectionK01OD026569 · OD · UNIVERSITY OF GEORGIA · PI MOUSA, JARROD · 2018 to 2020
$1.0M
NIAID NIH HHS R01 AI123383
6 · The paper itself

Abstract

Paenibacillus sp. 32352 is a soil-dwelling bacterium capable of producing an enzyme, Pn3Pase that degrades the capsular polysaccharide of Streptococcus pneumoniae serotype 3 (Pn3P). Recent reports on Pn3Pase have demonstrated its initial characterization and potential for protection against highly virulent S. pneumoniae serotype 3 infections. Initial experiments revealed this enzyme functions as an exo-β1,4-glucuronidase cleaving the β(1,4) linkage between glucuronic acid and glucose. However, the catalytic mechanism of this enzyme is still unknown. Here, we report the detailed biochemical analysis of Pn3Pase. Pn3Pase shows no significant sequence similarity to known glycoside hydrolase (GH) families, thus this novel enzyme establishes a new carbohydrate-active enzyme (CAZy) GH family. Site-directed mutagenesis studies revealed two catalytic residues along with truncation mutants defining essential domains for function. Pn3Pase and its mutants were screened for activity, substrate binding and kinetics. Additionally, nuclear magnetic resonance spectroscopy analysis revealed that Pn3Pase acts through a retaining mechanism. This study exhibits Pn3Pase activity at the structural and mechanistic level to establish the new CAZy GH family GH169 belonging to the large GH-A clan. This study will also serve toward generating Pn3Pase derivatives with optimal activity and pharmacokinetics aiding in the use of Pn3Pase as a novel therapeutic approach against type 3 S. pneumoniae infections.

Indexed as

GlucuronidaseGlycoside HydrolasesPaenibacillusPolysaccharidesStreptococcus pneumoniaeSubstrate SpecificityGlucuronidaseGlycoside HydrolasesPolysaccharidescapsular polysaccharidecarbohydrate-active enzymeglycoside hydrolaseStreptococcus pneumoniae

Identifiers

PMID32810871
PMCPMC8022930
OpenAlexW3072947307

What OpenQuestion holds

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Read underepoch 390

Registered trials

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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.