Evidence map›Paper›PMID 15385509›Full record

ArticleInfection and immunity2004

A Vibrio cholerae classical TcpA amino acid sequence induces protective antibody that binds an area hypothesized to be important for toxin-coregulated pilus structure.

Ronald K Taylor, Thomas J Kirn, Michael D Meeks, Terri K Wade, William F Wade

Open access · greenAbstract read
In one paragraph

Article in Infection and immunity, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
1.2field-weighted citation impact, top 21% 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

14 citing papers in PubMed, 28 citations in OpenAlex.

  1. Applied and environmental microbiology · 2026
    Article
  2. Strain-dependentFrontiers in microbiology · 2026
    Article
  3. Article
  4. Article
  5. Article
  6. InactivatedJournal of microbiology and biotechnology · 2022
    Article
  7. Article
  8. Cholera Toxin Production inFrontiers in microbiology · 2020
    Article
  9. Replication ofProceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. 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.

Ronald K TaylorDepartment of Microbiology and Immunology, Dartmouth Medical School, Lebanon, New Hampshire 03756, USA.
Thomas J Kirn
Michael D Meeks
Terri K Wade
William F Wade

Funding

Genetic Determinants of Virulence in Vibrio choleraeR37AI025096 · NIAID · DARTMOUTH COLLEGE · PI TAYLOR, RONALD K · 2007 to 2015
$4.3M
GENTICS DETERMINATION OF VIRULENCE OF VIBRIO CHOLERAER01AI025096 · NIAID · UNIVERSITY OF TENNESSEE HEALTH SCI CTR · PI SKORUPSKI, KAREN A · 1989 to 2016
$3.1M
GENETIC DETERMINANTS OF VIRULENCE IN VIBRIO CHOLERAER22AI025096 · NIAID · UNIVERSITY OF TENNESSEE HEALTH SCI CTR · PI TAYLOR, RONALD K · 1987 to 1991
–
NIAID NIH HHS AI25096NIAID NIH HHS AI 47373NIAID NIH HHS R01 AI025096NIAID NIH HHS R37 AI025096
6 · The paper itself

Abstract

Vibrio cholerae is a gram-negative bacterium that has been associated with cholera pandemics since the early 1800s. Whole-cell, killed, and live-attenuated oral cholera vaccines are in use. We and others have focused on the development of a subunit cholera vaccine that features standardized epitopes from various V. cholerae macromolecules that are known to induce protective antibody responses. TcpA protein is assembled into toxin-coregulated pilus (TCP), a type IVb pilus required for V. cholerae colonization, and thus is a strong candidate for a cholera subunit vaccine. Polypeptides (24 to 26 amino acids) in TcpA that can induce protective antibody responses have been reported, but further characterization of their amino acid targets relative to tertiary or quaternary TCP structures has not been done. We report a refinement of the TcpA sequences that can induce protective antibody. One sequence, TcpA 15 (residues 170 to 183), induces antibodies that bind linear TcpA in a Western blot as well as weakly bind soluble TcpA in solution. These antibodies bind assembled pili at high density and provide 80 to 100% protection in the infant mouse protection assay. This is in sharp contrast to other anti-TcpA peptide sera (TcpA 11, TcpA 13, and TcpA 17) that bind very strongly in Western blot and solution assays yet do not provide protection or effectively bind TCP, as evidenced by immunoelectron microscopy. The sequences of TcpA 15 that induce protective antibody were localized on a model of assembled TCP. These sequences are centered on a site that is predicted to be important for TCP structure.

Indexed as

Amino Acid SequenceAnimalsAnimals, NewbornAntibodies, BacterialAntibody SpecificityCholeraCholera VaccinesEnzyme-Linked Immunosorbent AssayFemaleFimbriae, BacterialFimbriae ProteinsImmune SeraMiceModels, MolecularProtein ConformationRabbitsAntibodies, BacterialCholera VaccinesFimbriae ProteinsImmune SeraRecombinant ProteinsTcpA protein, Vibrio cholerae

Identifiers

PMID15385509
PMCPMC517590
OpenAlexW2136897229

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.