A heterodimer of a VHH (variable domains of camelid heavy chain-only) antibody that inhibits anthrax toxin cell binding linked to a VHH antibody that blocks oligomer formation is highly protective in an anthrax spore challenge model

Journal of Biological Chemistry

Volumn 290, Issue 10, 2015, Pages 6584-6595

  Moayeri, Mahtab ^a   Leysath, Clinton E ^a,c   Tremblay, Jacqueline M ^b   Vrentas, Catherine ^a   Crown, Devorah ^a   Leppla, Stephen H ^a   Shoemaker, Charles B ^a,b  

^a TUFTS UNIVERSITY   (United States)

^b NATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASES   (United States)

^c TEXAS A AND M HEALTH SCIENCE CENTER   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIOLOGY; CELL MEMBRANES; CELLS; CHAINS; CYTOLOGY; DISEASES; EPITOPES; MAMMALS; MOBILE SECURITY; MOLECULAR BIOLOGY; OLIGOMERS; TOXIC MATERIALS;

ANTHRAX TOXINS; BACILLUS ANTHRACIS SPORES; CELLULAR RECEPTORS; NEUTRALIZING AGENTS; OLIGOMER FORMATIONS; PROTECTIVE ANTIGENS; TOXICITY ASSAYS; VARIABLE DOMAIN;

ANTIBODIES;

ANTHRAX TOXIN; ANTITOXIN; BACTERIAL ANTIGEN; PROTECTIVE ANTIGEN; UNCLASSIFIED DRUG; VARIABLE DOMAINS OF CAMELID HEAVY CHAIN ONLY ANTIBODY NEUTRALIZING AGENT; BACTERIAL TOXIN; BACTERIUM ANTIBODY; EPITOPE; IMMUNOGLOBULIN HEAVY CHAIN;

ALPACA; ANIMAL CELL; ANIMAL EXPERIMENT; ANIMAL MODEL; ANTHRAX; ANTIGEN BINDING; ARTICLE; ARTIODACTYLA; BACILLUS ANTHRACIS; CELL ASSAY; CELL SURFACE; CONTROLLED STUDY; DRUG EFFICACY; DRUG MECHANISM; DRUG POTENCY; ENDOCYTOSIS; FEMALE; INHIBITION KINETICS; MOLECULAR RECOGNITION; MOLECULAR WEIGHT; MOUSE; NONHUMAN; PHAGE DISPLAY; PRIORITY JOURNAL; PROTECTION; ANIMAL; ANTAGONISTS AND INHIBITORS; BACTERIAL SPORE; HUMAN; IMMUNOLOGY; MICROBIOLOGY; NEW WORLD CAMELID; PATHOGENICITY; PATHOLOGY;

BACILLUS ANTHRACIS; CAMELIDAE; MUS;

ANIMALS; ANTHRAX; ANTIBODIES, BACTERIAL; ANTIGENS, BACTERIAL; BACILLUS ANTHRACIS; BACTERIAL TOXINS; CAMELIDS, NEW WORLD; EPITOPES; HUMANS; IMMUNOGLOBULIN HEAVY CHAINS; MICE; SPORES;

EID: 84924787113     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M114.627943     Document Type: Article

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