Evidence map›Paper›PMID 35105886›Full record

ArticleNature communications2022

PplD is a de-N-acetylase of the cell wall linkage unit of streptococcal rhamnopolysaccharides.

Jeffrey S Rush, Prakash Parajuli, Alessandro Ruda, Jian Li, Amol Arunrao Pohane, Svetlana Zamakhaeva, Mohammad M Rahman, Jennifer C Chang, Artemis Gogos, Cameron W Kenner and 5 more

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2022. 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
4.4field-weighted citation impact, top 5% 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, 27 citations in OpenAlex.

  1. mBio · 2026
    Article
  2. bioRxiv : the preprint server for biology · 2026
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  13. Human oral lectin ZG16B acts as a cell wall polysaccharide probe to decode host-microbe interactions with oral commensals.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  14. 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

15 authors at 5 institutions in 3 countries.

Jeffrey S RushDepartment of Molecular and Cellular Biochemistry, University of Kentucky, Lexington, KY, USA.
Prakash ParajuliDepartment of Microbiology, Immunology and Molecular Genetics, University of Kentucky, Lexington, KY, USA.ORCID http://orcid.org/0000-0002-3384-2680
Alessandro RudaDepartment of Organic Chemistry, Arrhenius Laboratory, Stockholm University, Stockholm, Sweden.ORCID http://orcid.org/0000-0002-5918-5797
Jian LiDepartment of Molecular and Cellular Biochemistry, University of Kentucky, Lexington, KY, USA.
Amol Arunrao PohaneDepartment of Microbiology, Immunology and Molecular Genetics, University of Kentucky, Lexington, KY, USA.ORCID http://orcid.org/0000-0003-2574-0366
Svetlana ZamakhaevaDepartment of Microbiology, Immunology and Molecular Genetics, University of Kentucky, Lexington, KY, USA.
Mohammad M RahmanDepartment of Microbiology, Immunology and Molecular Genetics, University of Kentucky, Lexington, KY, USA.
Jennifer C ChangDepartment of Medicinal Chemistry and Pharmacognosy, University of Illinois at Chicago, Chicago, IL, USA.ORCID http://orcid.org/0000-0002-6175-1284
Artemis GogosDepartment of Medicinal Chemistry and Pharmacognosy, University of Illinois at Chicago, Chicago, IL, USA.ORCID http://orcid.org/0000-0002-0555-3814
Cameron W KennerDepartment of Microbiology, Immunology and Molecular Genetics, University of Kentucky, Lexington, KY, USA.
Gérard LambeauUniversité Côte d'Azur, Centre National de la Recherche Scientifique, Institut de Pharmacologie Moléculaire et Cellulaire, Valbonne Sophia Antipolis, France.ORCID http://orcid.org/0000-0002-9239-518X
Michael J FederleDepartment of Medicinal Chemistry and Pharmacognosy, University of Illinois at Chicago, Chicago, IL, USA.ORCID http://orcid.org/0000-0002-4554-543X
Konstantin V KorotkovDepartment of Molecular and Cellular Biochemistry, University of Kentucky, Lexington, KY, USA.ORCID http://orcid.org/0000-0002-2182-6843
Göran WidmalmDepartment of Organic Chemistry, Arrhenius Laboratory, Stockholm University, Stockholm, Sweden.ORCID http://orcid.org/0000-0001-8303-4481
Natalia KorotkovaDepartment of Molecular and Cellular Biochemistry, University of Kentucky, Lexington, KY, USA. nkorotkova@uky.edu.ORCID http://orcid.org/0000-0002-8696-4892
University of Kentucky · USUniversity of Illinois Chicago · USStockholm University · SECentre National de la Recherche Scientifique · FRUniversity of Kentucky HealthCare · US

Funding

A Synchrotron Radiation Structural Biology ResourcesP30GM133894 · NIGMS · STANFORD UNIVERSITY · PI Ritimukta Sarangi · 2020 to 2026
$43.3M
Biogenesis and Function of Streptococcus Pyogenes Cell WallR01AI143690 · NIAID · UNIVERSITY OF KENTUCKY · PI KOROTKOVA, NATALIA · 2020 to 2024
$1.9M
Biosynthesis, structure and function of cell wall in Streptococcus mutansR01DE028916 · NIDCR · UNIVERSITY OF KENTUCKY · PI KOROTKOVA, NATALIA · 2020 to 2024
$1.8M
NIAID NIH HHS R01 AI143690NIDCR NIH HHS R01 DE028916NIGMS NIH HHS P30 GM133894
6 · The paper itself

Abstract

The cell wall of the human bacterial pathogen Group A Streptococcus (GAS) consists of peptidoglycan decorated with the Lancefield group A carbohydrate (GAC). GAC is a promising target for the development of GAS vaccines. In this study, employing chemical, compositional, and NMR methods, we show that GAC is attached to peptidoglycan via glucosamine 1-phosphate. This structural feature makes the GAC-peptidoglycan linkage highly sensitive to cleavage by nitrous acid and resistant to mild acid conditions. Using this characteristic of the GAS cell wall, we identify PplD as a protein required for deacetylation of linkage N-acetylglucosamine (GlcNAc). X-ray structural analysis indicates that PplD performs catalysis via a modified acid/base mechanism. Genetic surveys in silico together with functional analysis indicate that PplD homologs deacetylate the polysaccharide linkage in many streptococcal species. We further demonstrate that introduction of positive charges to the cell wall by GlcNAc deacetylation protects GAS against host cationic antimicrobial proteins.

Indexed as

AcetylesteraseAcetylglucosamineBacterial ProteinsCell WallCrystallography, X-RayGlucosamineGlucosephosphatesHistonesHumansNitrous AcidPeptidoglycanPolysaccharides, BacterialStreptococcal InfectionsStreptococcusStreptococcus mutansAcetylesteraseAcetylglucosamineBacterial ProteinsGlucosamineglucosamine 1-phosphateGlucosephosphatesHistonesNitrous AcidPeptidoglycanPolysaccharides, Bacterial

Identifiers

PMID35105886
PMCPMC8807736
OpenAlexW4225604034

What OpenQuestion holds

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LicenceCC BY
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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.