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Article

The Disulfide Bond Cys255-Cys279 in the Immunoglobulin-Like Domain of Anthrax Toxin Receptor 2 Is Required for Membrane Insertion of Anthrax Protective Antigen Pore.

PloS one - 1 Jan 2015

Jacquez Pedro, Avila Gustavo, Boone Kyle, Altiyev Agamyrat, Puschhof Jens, Sauter Roland, Arigi Emma, Ruiz Blanca, Peng Xiuli, Almeida Igor, Sherman Michael, Xiao Chuan, Sun Jianjun

Abstract excerpt

Anthrax toxin receptors act as molecular clamps or switches that control anthrax toxin entry, pH-dependent pore formation, and translocation of enzymatic moieties across the endosomal membranes. We previously reported that reduction of the disulfide bonds in the immunoglobulin-like (Ig) domain of the anthrax toxin receptor 2 (ANTXR2) inhibited the function of the protective antigen (PA) pore. In the present...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Source

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Identifiers

PMID: 26107617
DOI: 10.1371/journal.pone.0130832
PMCID: PMC4479931

Genes

ANTXR2

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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