Evidence map›Paper›PMID 16617115›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2006

ADP-ribosylating and vacuolating cytotoxin of Mycoplasma pneumoniae represents unique virulence determinant among bacterial pathogens.

T R Kannan, Joel B Baseman

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 135 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
135citing papers in PubMed, 1 pooled it
6.3field-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

135 citing papers in PubMed, 1 synthesis or guideline pooled it, 223 citations in OpenAlex.

  1. Pooled it
  2. Research progress on detection technologies for Mycoplasma pneumoniae.European journal of clinical microbiology & infectious diseases : official publication of the European Society of Clinical Microbiology · 2026
    Review
  3. Article
  4. Coinfection Patterns ofInternational journal of molecular sciences · 2026
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  5. Review
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  7. Article
  8. The Post-Pandemic Return ofJournal of clinical medicine · 2026
    Article
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  11. Article
  12. Review
  13. Review
  14. A multi-epitope vaccine targetingFrontiers in immunology · 2026
    Article
  15. Prediction models for refractoryFrontiers in pediatrics · 2026
    Article
  16. Article
  17. Breathe (Sheffield, England) · 2025
    Review
  18. Article
  19. Germs · 2025
    Article
  20. The Immune Modulatory Role of Surfactants inJournal of inflammation research · 2025
    Review

75 more citing papers are in PubMed but not listed here.

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

2 authors at 1 institution in 1 country.

T R KannanDepartment of Microbiology and Immunology, University of Texas Health Science Center, 7703 Floyd Curl Drive, San Antonio, TX 78229, USA.
Joel B Baseman
The University of Texas Health Science Center at San Antonio · US

Funding

MYCOPLASMA PNEUMONIAE - AIRWAY INTERPLAYR01AI045737 · NIAID · UNIVERSITY OF TEXAS HLTH SCI CTR SAN ANT · PI BASEMAN, JOEL BARRY · 2000 to 2004
$1.7M
NIAID NIH HHS AI45737NIAID NIH HHS R01 AI045737
6 · The paper itself

Abstract

Unlike many bacterial pathogens, Mycoplasma pneumoniae is not known to produce classical toxins, and precisely how M. pneumoniae injures the respiratory epithelium has remained a mystery for >50 years. Here, we report the identification of a virulence factor (MPN372) possibly responsible for airway cellular damage and other sequelae associated with M. pneumoniae infections in humans. We show that M. pneumoniae MPN372 encodes a 68-kDa protein that possesses ADP-ribosyltransferase (ART) activity. Within its N terminus, MPN372 contains key amino acids associated with NAD binding and ADP-ribosylating activity, similar to pertussis toxin (PTX) S1 subunit (PTX-S1). Interestingly, MPN372 ADP ribosylates both identical and distinct mammalian proteins when compared with PTX-S1. Remarkably, MPN372 elicits extensive vacuolization and ultimate cell death of mammalian cells, including distinct and progressive patterns of cytopathology in tracheal rings in organ culture that had been previously ascribed to infection with WT virulent M. pneumoniae. We observed dramatic seroconversion to MPN372 in patients diagnosed with M. pneumoniae-associated pneumonia, indicating that this toxin is synthesized in vivo and possesses highly immunogenic epitopes.

Indexed as

Adenosine Diphosphate RiboseADP Ribose TransferasesAmino Acid SequenceAnimalsAntibodies, BacterialBacterial ProteinsCHO CellsCommunity-Acquired InfectionsCricetinaeCytotoxinsGenes, BacterialHumansMolecular Sequence DataMutagenesis, Site-DirectedMycoplasma pneumoniaeOrgan Culture TechniquesAdenosine Diphosphate RiboseADP Ribose TransferasesAntibodies, BacterialBacterial ProteinsCytotoxinsRecombinant ProteinsVirulence Factors

Identifiers

PMID16617115
PMCPMC1458948
OpenAlexW2085510436

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.