Evidence map›Paper›PMID 26375454›Full record

ArticlePloS one2015

Single Amino Acid Polymorphisms of Pertussis Toxin Subunit S2 (PtxB) Affect Protein Function.

Scott H Millen, Mineo Watanabe, Eiji Komatsu, Fuminori Yamaguchi, Yuki Nagasawa, Eri Suzuki, Haleigh Monaco, Alison A Weiss

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
0.5field-weighted citation impact, top 33% 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

6 citing papers in PubMed, 8 citations in OpenAlex.

  1. Review
  2. Structural basis for neutralizing antibody binding to pertussis toxin.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  3. Article
  4. Review
  5. Review
  6. 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

8 authors at 2 institutions in 2 countries.

Scott H MillenDepartment of Molecular Genetics, Biochemistry, and Microbiology, University of Cincinnati, Cincinnati, Ohio, United States of America.
Mineo WatanabeGraduate School of Infection Control Sciences, Kitasato University, Minato-ku, Tokyo, Japan.
Eiji KomatsuGraduate School of Infection Control Sciences, Kitasato University, Minato-ku, Tokyo, Japan.
Fuminori YamaguchiGraduate School of Infection Control Sciences, Kitasato University, Minato-ku, Tokyo, Japan.
Yuki NagasawaGraduate School of Infection Control Sciences, Kitasato University, Minato-ku, Tokyo, Japan.
Eri SuzukiGraduate School of Infection Control Sciences, Kitasato University, Minato-ku, Tokyo, Japan.
Haleigh MonacoDepartment of Molecular Genetics, Biochemistry, and Microbiology, University of Cincinnati, Cincinnati, Ohio, United States of America.
Alison A WeissDepartment of Molecular Genetics, Biochemistry, and Microbiology, University of Cincinnati, Cincinnati, Ohio, United States of America.
Kitasato University · JPUniversity of Cincinnati · US

Funding

VIRULENCE MUTANTS OF BORDETELLA PERTUSSISR01AI023695 · NIAID · VIRGINIA COMMONWEALTH UNIVERSITY · PI MILLER, WILLIAM E, MONACO, JOHN J. · 1986 to 2010
$2.4M
NIAID NIH HHS R01 AI023695NIAID NIH HHS R01AI23695
6 · The paper itself

Abstract

Whooping cough due to Bordetella pertussis is increasing in incidence, in part due to accumulation of mutations which increase bacterial fitness in highly vaccinated populations. Polymorphisms in the pertussis toxin, ptxA and ptxB genes, and the pertactin, prn genes of clinical isolates of Bordetella pertussis collected in Cincinnati from 1989 through 2005 were examined. While the ptxA and prn genotypes were variable, all 48 strains had the ptxB2 genotype; ptxB1 encodes glycine at amino acid 18 of the S2 subunit of pertussis toxin, while ptxB2 encodes serine. We investigated antigenic and functional differences of PtxB1 and PtxB2. The S2 protein was not very immunogenic. Only a few vaccinated or individuals infected with B. pertussis developed antibody responses to the S2 subunit, and these sera recognized both polymorphic forms equally well. Amino acid 18 of S2 is in a glycan binding domain, and the PtxB forms displayed differences in receptor recognition and toxicity. PtxB1 bound better to the glycoprotein, fetuin, and Jurkat T cells in vitro, but the two forms were equally effective at promoting CHO cell clustering. To investigate in vivo activity of Ptx, one μg of Ptx was administered to DDY mice and blood was collected on 4 days after injection. PtxB2 was more effective at promoting lymphocytosis in mice.

Indexed as

Amino Acid SubstitutionPolymorphism, GeneticAllelesAnimalsBase SequenceCHO CellsCricetinaeCricetulusFemaleHumansMiceModels, MolecularPertussis ToxinProtein MultimerizationProtein Structure, QuaternaryPertussis Toxin

Identifiers

PMID26375454
PMCPMC4573519
OpenAlexW2214991143

What OpenQuestion holds

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LicenceCC BY
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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.