Evidence map›Paper›PMID 32365117›Full record

ArticlePLoS pathogens2020

Structure and functional analysis of the Legionella pneumophila chitinase ChiA reveals a novel mechanism of metal-dependent mucin degradation.

Saima Rehman, Lubov S Grigoryeva, Katherine H Richardson, Paula Corsini, Richard C White, Rosie Shaw, Theo J Portlock, Benjamin Dorgan, Zeinab S Zanjani, Arianna Fornili and 2 more

Open access · goldAbstract read
In one paragraph

Article in PLoS pathogens, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
5.9field-weighted citation impact, top 3% 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

26 citing papers in PubMed, 44 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Mucin stimulates the growth ofMicrobiology (Reading, England) · 2026
    Article
  5. Molecular evolution and adaptations ofFrontiers in cellular and infection microbiology · 2026
    Review
  6. mBio · 2025
    Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Review
  12. Article
  13. Protein sociology of ProA, Mip and other secreted virulence factors at theFrontiers in cellular and infection microbiology · 2023
    Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Microorganisms · 2022
    Review
  19. Article
  20. Review
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

12 authors at 3 institutions in 2 countries.

Saima RehmanCentre for Host-Microbiome Interactions, Dental Institute, King's College London, London, United Kingdom.
Lubov S GrigoryevaDepartment of Microbiology and Immunology, Feinberg School of Medicine, Northwestern University, Chicago, Illinois, United States of America.ORCID 0000-0002-9083-8805
Katherine H RichardsonChemistry and Biochemistry Department, School of Biological and Chemical Sciences, Queen Mary University of London, London, United Kingdom.
Paula CorsiniCentre for Host-Microbiome Interactions, Dental Institute, King's College London, London, United Kingdom.ORCID 0000-0002-4987-2235
Richard C WhiteDepartment of Microbiology and Immunology, Feinberg School of Medicine, Northwestern University, Chicago, Illinois, United States of America.ORCID 0000-0003-1970-692X
Rosie ShawChemistry and Biochemistry Department, School of Biological and Chemical Sciences, Queen Mary University of London, London, United Kingdom.
Theo J PortlockCentre for Host-Microbiome Interactions, Dental Institute, King's College London, London, United Kingdom.ORCID 0000-0001-5971-3847
Benjamin DorganCentre for Host-Microbiome Interactions, Dental Institute, King's College London, London, United Kingdom.
Zeinab S ZanjaniChemistry and Biochemistry Department, School of Biological and Chemical Sciences, Queen Mary University of London, London, United Kingdom.
Arianna ForniliChemistry and Biochemistry Department, School of Biological and Chemical Sciences, Queen Mary University of London, London, United Kingdom.ORCID 0000-0001-6554-3979
Nicholas P CianciottoDepartment of Microbiology and Immunology, Feinberg School of Medicine, Northwestern University, Chicago, Illinois, United States of America.ORCID 0000-0002-9572-8322
James A GarnettCentre for Host-Microbiome Interactions, Dental Institute, King's College London, London, United Kingdom.ORCID 0000-0001-7621-8223
Queen Mary University of London · GBNorthwestern University · USKing's College London · GB

Funding

CELLULAR &MOLECULAR BASIS OF DISEASE TRAINING PROGRAMT32GM008061 · NIGMS · NORTHWESTERN UNIVERSITY · PI CARTHEW, RICHARD W. · 1985 to 2022
$17.1M
TRAINING PROGRAM IN IMMUNOLOGY &MOLECULAR PATHOGENESIST32AI007476 · NIAID · NORTHWESTERN UNIVERSITY AT CHICAGO · PI Edward Benjamin Thorp · 1996 to 2026
$6.6M
TYPE II SECRETION AND LEGIONELLA PNEUMOPHILA INFECTIONR01AI043987 · NIAID · NORTHWESTERN UNIVERSITY AT CHICAGO · PI CIANCIOTTO, NICHOLAS P · 1999 to 2017
$4.8M
Cancer Research UK FC001029Medical Research Council FC001029Medical Research Council MC_U117533887Medical Research Council MR/M009920/1Medical Research Council MR/R017662/1NIAID NIH HHS R01 AI043987NIAID NIH HHS T32 AI007476NIGMS NIH HHS T32 GM008061Wellcome Trust FC001029
6 · The paper itself

Abstract

Chitinases are important enzymes that contribute to the generation of carbon and nitrogen from chitin, a long chain polymer of N-acetylglucosamine that is abundant in insects, fungi, invertebrates and fish. Although mammals do not produce chitin, chitinases have been identified in bacteria that are key virulence factors in severe respiratory, gastrointestinal and urinary diseases. However, it is unclear how these enzymes are able to carry out this dual function. Legionella pneumophila is the causative agent of Legionnaires' disease, an often-fatal pneumonia and its chitinase ChiA is essential for the survival of L. pneumophila in the lung. Here we report the first atomic resolution insight into the pathogenic mechanism of a bacterial chitinase. We derive an experimental model of intact ChiA and show how its N-terminal region targets ChiA to the bacterial surface after its secretion. We provide the first evidence that L. pneumophila can bind mucins on its surface, but this is not dependent on ChiA. This demonstrates that additional peripheral mucin binding proteins are also expressed in L. pneumophila. We also show that the ChiA C-terminal chitinase domain has novel Zn2+-dependent peptidase activity against mammalian mucin-like proteins, namely MUC5AC and the C1-esterase inhibitor, and that ChiA promotes bacterial penetration of mucin gels. Our findings suggest that ChiA can facilitate passage of L. pneumophila through the alveolar mucosa, can modulate the host complement system and that ChiA may be a promising target for vaccine development.

Indexed as

AcetylglucosamineBacterial ProteinsChitinChitinasesGene Expression Regulation, BacterialLegionella pneumophilaLegionnaires' DiseaseMetalsMucin-1MucinsProteolysisStructure-Activity RelationshipVirulence FactorsAcetylglucosamineBacterial ProteinsChitinchitinase ChiAChitinasesMetalsMucin-1MucinsVirulence Factors

Identifiers

PMID32365117
PMCPMC7224574
OpenAlexW3022934745

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.