ArticleInfection and immunity2007
Pertussis toxin utilizes proximal components of the T-cell receptor complex to initiate signal transduction events in T cells.
Article in Infection and immunity, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed, 33 citations in OpenAlex.
- Mechanisms of Pertussis Toxin Action: ADP-Ribosylation and Its Role in Pertussis Pathogenesis.Toxins · 2026Review
- Hypofucosylation promotes pertussis toxin binding to cell surface glycococonjugates and pertussis toxin-induced intracellular ERK signaling.Glycobiology · 2026Article
- Structural basis for neutralizing antibody binding to pertussis toxin.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Structural Basis for Antibody Neutralization of Pertussis Toxin.bioRxiv : the preprint server for biology · 2024Article
- Eosinophils as drivers of bacterial immunomodulation and persistence.Infection and immunity · 2024Review
- The Neonatal Immune System and Respiratory Pathogens.Microorganisms · 2023Review
- Novel murine model reveals an early role for pertussis toxin in disrupting neonatal immunity toFrontiers in immunology · 2023Article
- Categorizing Sequences of Concern by Function To Better Assess Mechanisms of Microbial Pathogenesis.Infection and immunity · 2022Review
- Conquering the host:Frontiers in microbiology · 2022Review
- Contribution of a Novel Pertussis Toxin-Like Factor in Mediating Persistent Otitis Media.Frontiers in cellular and infection microbiology · 2022Article
- Safety testing of acellular pertussis vaccines: Use of animals and 3Rs alternatives.Human vaccines & immunotherapeutics · 2017Article
- The chromosomal nature of LT-II enterotoxins solved: a lambdoid prophage encodes both LT-II and one of two novel pertussis-toxin-like toxin family members in type II enterotoxigenic Escherichia coli.Pathogens and disease · 2016Article
- Single Amino Acid Polymorphisms of Pertussis Toxin Subunit S2 (PtxB) Affect Protein Function.PloS one · 2015Article
- Review
- Orexin/hypocretin receptor signalling cascades.British journal of pharmacology · 2014Review
- Toward a mechanism-based in vitro safety test for pertussis toxin.Human vaccines & immunotherapeutics · 2014Review
- Pertussis toxin B-pentamer mediates intercellular transfer of membrane proteins and lipids.PloS one · 2013Article
- Mechanistic insight into pertussis toxin and lectin signaling using T cells engineered to express a CD8α/CD3ζ chimeric receptor.Biochemistry · 2012Article
- Review
- Anaphylaxis and mortality induced by treatment of mice with anti-VLA-4 antibody and pertussis toxin.Journal of immunology (Baltimore, Md. : 1950) · 2011Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Pertussis toxin (PTx) is an AB(5) toxin produced by the human pathogen Bordetella pertussis. Previous work demonstrates that the five binding (B) subunits of PTx can have profound effects on T lymphocytes independent of the enzymatic activity of the A subunit. Stimulation of T cells with holotoxin (PTx) or the B subunit alone (PTxB) rapidly induces signaling events resulting in inositol phosphate accumulation, Ca(2+) mobilization, interleukin-2 (IL-2) production, and mitogenic cell growth. Although previous reports suggest the presence of PTx signaling receptors expressed on T cells, to date, the receptor(s) and membrane proximal signaling events utilized by PTx remain unknown. Here we genetically and biochemically define the membrane proximal components utilized by PTx to initiate signal transduction in T cells. Using mutants of the Jurkat T-cell line deficient for key components of the T-cell receptor (TCR) pathway, we have compared stimulation with PTx to that of anti-CD3 monoclonal antibody (MAb), which directly interacts with and activates the TCR complex. Our genetic data in combination with biochemical analysis show that PTx (via the B subunit) activates TCR signaling similar to that of anti-CD3 MAb, including activation of key signaling intermediates such as Lck, ZAP-70, and phospholipase C-gamma1. Moreover, the data indicate that costimulatory activity, as provided by CD28 ligation, is required for PTx to fully stimulate downstream indicators of T-cell activation such as IL-2 gene expression. By illuminating the signaling pathways that PTx activates in T cells, we provide a mechanistic understanding for how these signals deregulate immune system functions during B. pertussis infection.
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Registered trials
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.