Structural basis for CSPG4 as a receptor for TcdB and a therapeutic target in Clostridioides difficile infection

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Trends in U.S. Burden of Clostridioides difficile Infection and Outcomes

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Clostridioides difficileinfection damages colonic stem cells via TcdB, impairing epithelial repair and recovery from disease

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Ribotype Classification of Clostridioides difficile Isolates Is Not Predictive of the Amino Acid Sequence Diversity of the Toxin Virulence Factors TcdA and TcdB

(2020) Zhenghui Li et al.   Frontiers in Microbiology

Subtyping analysis reveals new variants and accelerated evolution of Clostridioides difficile toxin B

(2020) Enhui Shen et al.   Communications Biology

Phylogenomics of 8,839 Clostridioides difficile genomes reveals recombination-driven evolution and diversification of toxin A and B

(2020) Michael J. Mansfield et al.   PLoS Pathogens

Receptor Binding Domains of TcdB from Clostridioides difficile for Chondroitin Sulfate Proteoglycan-4 and Frizzled Proteins Are Functionally Independent and Additive

(2020) Daniel Henkel et al.   Toxins

Structure of the full-length Clostridium difficile toxin B

(2019) Peng Chen et al.   NATURE STRUCTURAL & MOLECULAR BIOLOGY

Toxin B Variants from Clostridium difficile Strains VPI 10463 and NAP1/027 Share Similar Substrate Profile and Cellular Intoxication Kinetics but Use Different Host Cell Entry Factors

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Designed Ankyrin Repeat Protein (DARPin) Neutralizers of TcdB from Clostridium difficile Ribotype 027

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Structural basis for recognition of frizzled proteins byClostridium difficiletoxin B

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Structural deciphering of the NG2/CSPG4 proteoglycan multifunctionality

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Structural insight into Wnt signaling inhibition by Clostridium difficile toxin B

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Functional defects inClostridium difficileTcdB toxin uptake identify CSPG4 receptor-binding determinants

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(2017) Ali Punjani et al.   NATURE METHODS

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Developing a Multiplexed Quantitative Cross-Linking Mass Spectrometry Platform for Comparative Structural Analysis of Protein Complexes

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Developing an Acidic Residue Reactive and Sulfoxide-Containing MS-Cleavable Homobifunctional Cross-Linker for Probing Protein–Protein Interactions

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Antibodies to Toxin B Are Protective AgainstClostridium difficileInfection Recurrence

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Frizzled proteins are colonic epithelial receptors for C. difficile toxin B

(2016) Liang Tao et al.   NATURE

Chemical and Stress Resistances of Clostridium difficile Spores and Vegetative Cells

(2016) Adrianne N. Edwards et al.   Frontiers in Microbiology

Exposure of Neutralizing Epitopes in the Carboxyl-terminal Domain of TcdB Is Altered by a Proximal Hypervariable Region

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AAV-expressed eCD4-Ig provides durable protection from multiple SHIV challenges

(2015) Matthew R. Gardner et al.   NATURE

Defining the Roles of TcdA and TcdB in Localized Gastrointestinal Disease, Systemic Organ Damage, and the Host Response during Clostridium difficile Infections

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Broad Coverage of Genetically Diverse Strains of Clostridium difficile by Actoxumab and Bezlotoxumab Predicted byIn VitroNeutralization and Epitope Modeling

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Chondroitin sulfate proteoglycan 4 functions as the cellular receptor for Clostridium difficile toxin B

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Critical Roles of Clostridium difficile Toxin B Enzymatic Activities in Pathogenesis

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Mechanism of Action and Epitopes ofClostridium difficileToxin B-neutralizing Antibody Bezlotoxumab Revealed by X-ray Crystallography

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A Segment of 97 Amino Acids within the Translocation Domain of Clostridium difficile Toxin B Is Essential for Toxicity

(2013) Yongrong Zhang et al.   PLoS One

Clostridium difficile 027/BI/NAP1 Encodes a Hypertoxic and Antigenically Variable Form of TcdB

(2013) Jordi M. Lanis et al.   PLoS Pathogens

Protection Against Clostridium difficile Infection With Broadly Neutralizing Antitoxin Monoclonal Antibodies

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Development of a Novel Cross-linking Strategy for Fast and Accurate Identification of Cross-linked Peptides of Protein Complexes

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Variations in TcdB Activity and the Hypervirulence of Emerging Strains of Clostridium difficile

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Toxin B is essential for virulence of Clostridium difficile

(2009) Dena Lyras et al.   NATURE

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(2009) Jacek R Wiśniewski et al.   NATURE METHODS

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A Mouse Model of Clostridium difficile–Associated Disease

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