Evidence map›Paper›PMID 35225652›Full record

ArticleInfection and immunity2022

The AmiC/NlpD Pathway Dominates Peptidoglycan Breakdown in Neisseria meningitidis and Affects Cell Separation, NOD1 Agonist Production, and Infection.

Jia Mun Chan, Kathleen T Hackett, Katelynn L Woodhams, Ryan E Schaub, Joseph P Dillard

Open access · greenAbstract read
In one paragraph

Article in Infection and immunity, 2022. 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
0.9field-weighted citation impact, top 30% 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, 7 citations in OpenAlex.

  1. Article
  2. Article
  3. Mutation ofJournal of bacteriology · 2023
    Article
  4. Mutation ofbioRxiv : the preprint server for biology · 2023
    Article
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

5 authors at 1 institution in 1 country.

Jia Mun ChanUniversity of Wisconsin-Madison, Department of Medical Microbiology and Immunology, School of Medicine and Public Health, Madison, Wisconsin, USA.
Kathleen T HackettUniversity of Wisconsin-Madison, Department of Medical Microbiology and Immunology, School of Medicine and Public Health, Madison, Wisconsin, USA.
Katelynn L WoodhamsUniversity of Wisconsin-Madison, Department of Medical Microbiology and Immunology, School of Medicine and Public Health, Madison, Wisconsin, USA.
Ryan E SchaubUniversity of Wisconsin-Madison, Department of Medical Microbiology and Immunology, School of Medicine and Public Health, Madison, Wisconsin, USA.ORCID 0000-0001-5300-2403
Joseph P DillardUniversity of Wisconsin-Madison, Department of Medical Microbiology and Immunology, School of Medicine and Public Health, Madison, Wisconsin, USA.ORCID 0000-0003-1711-7670
University of Wisconsin–Madison · US

Funding

Peptidoglycan metabolism and fragment releaseR01AI097157 · NIAID · UNIVERSITY OF WISCONSIN-MADISON · PI DILLARD, JOSEPH P · 2012 to 2022
$5.6M
HHS | NIH | National Institute of Allergy and Infectious Diseases (NIAID) R01AI097157NIAID NIH HHS R01 AI097157
6 · The paper itself

Abstract

The human-restricted pathogen Neisseria meningitidis, which is best known for causing invasive meningococcal disease, has a nonpathogenic lifestyle as an asymptomatic colonizer of the human naso- and oropharyngeal space. N. meningitidis releases small peptidoglycan (PG) fragments during growth. It was demonstrated previously that N. meningitidis releases low levels of tripeptide PG monomer, which is an inflammatory molecule recognized by the human intracellular innate immune receptor NOD1. In the present study, we demonstrated that N. meningitidis released more PG-derived peptides than PG monomers. Using a reporter cell line overexpressing human NOD1, we showed that N. meningitidis activates NOD1 using PG-derived peptides. The generation of such peptides required the presence of the periplasmic

Indexed as

Bacterial ProteinsLipoproteinsNeisseria meningitidisNod1 Signaling Adaptor ProteinPeptidoglycanCell SeparationCell WallHumansMeningococcal InfectionsBacterial ProteinsLipoproteinsNlpD protein, bacteriaNOD1 protein, humanNod1 Signaling Adaptor ProteinPeptidoglycanAmiCamidaseNeisseria meningitidisNlpDNOD1peptidoglycanpeptidoglycan hydrolasespeptidoglycan hydrolysis

Identifiers

PMID35225652
PMCPMC8929373
OpenAlexW4214558746

What OpenQuestion holds

Textmetadata
Read underepoch 390

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.