Epitopes and Mechanism of Action of the Clostridium difficile Toxin A-Neutralizing Antibody Actoxumab

Journal of Molecular Biology

Volumn 429, Issue 7, 2017, Pages 1030-1044

  Hernandez, Lorraine D ^a   Kroh, Heather K ^b   Hsieh, Edward ^a   Yang, Xiaoyu ^a   Beaumont, Maribel ^a   Sheth, Payal R ^a   DiNunzio, Edward ^a   Rutherford, Stacey A ^b   Ohi, Melanie D ^b   Ermakov, Grigori ^a   Xiao, Li ^a   Secore, Susan ^a   Karczewski, Jerzy ^a,c   Racine, Fred ^a   Mayhood, Todd ^a   Fischer, Paul ^a   Sher, Xinwei ^a   Gupta, Pulkit ^a,d   Lacy, D Borden ^b   Therien, Alex G ^a,e  

^a MERCK RESEARCH LABORATORIES   (United States)

^b VANDERBILT UNIVERSITY SCHOOL OF MEDICINE   (United States)

^c Fraunhofer USA Inc   (United States)

^d Merck Exploratory Science Center (ESC)   (United States)

^e AG Therien   (Canada)

Author keywords

Clostridium difficile infection; epitope mapping; monoclonal antibody; TcdA; toxin neutralization

Indexed keywords

ACTOXUMAB; BEZLOTOXUMAB; CLOSTRIDIUM DIFFICILE TOXIN A; EPITOPE; IMMUNOGLOBULIN F(AB) FRAGMENT; BACTERIAL TOXIN; ENTEROTOXIN; MONOCLONAL ANTIBODY; NEUTRALIZING ANTIBODY; PROTEIN AGGREGATE; PROTEIN BINDING; TCDA PROTEIN, CLOSTRIDIUM DIFFICILE;

AMINO ACID SEQUENCE; ANTIGEN ANTIBODY COMPLEX; ANTIGEN BINDING; ARTICLE; BINDING SITE; CELL SURFACE; CLOSTRIDIUM DIFFICILE INFECTION; COMBINED REPETITIVE OLIGOPEPTIDE DOMAIN; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; DISSOCIATION CONSTANT; DRUG BINDING SITE; DRUG MECHANISM; DRUG POTENCY; EC50; FLOW CYTOMETRY; HOST CELL; HT-29 CELL LINE; IN VITRO STUDY; IN VIVO STUDY; MOLECULAR WEIGHT; NONHUMAN; PEPTOCLOSTRIDIUM DIFFICILE; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN STRUCTURE; RECEPTOR BINDING; SIZE EXCLUSION CHROMATOGRAPHY; SURFACE PLASMON RESONANCE; VERO CELL LINE; ANTAGONISTS AND INHIBITORS; METABOLISM;

ANTIBODIES, MONOCLONAL; ANTIBODIES, NEUTRALIZING; BACTERIAL TOXINS; BINDING SITES; ENTEROTOXINS; EPITOPES; PROTEIN AGGREGATES; PROTEIN BINDING;

EID: 85014067221     PISSN: 00222836     EISSN: 10898638     Source Type: Journal    
DOI: 10.1016/j.jmb.2017.02.010     Document Type: Article

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