Anthrax toxin-neutralizing antibody reconfigures the protective antigen heptamer into a supercomplex

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Title

Anthrax toxin-neutralizing antibody reconfigures the protective antigen heptamer into a supercomplex

Content partner

The University of Auckland Library

Collection

ResearchSpace@Auckland

Description

The tripartite protein exotoxin secreted by Bacillus anthracis, a major contributor to its virulence and anthrax pathogenesis, consists of binary complexes of the protective antigen (PA) heptamer (PA63h), produced by proteolytic cleavage of PA, together with either lethal factor or edema factor. The mouse monoclonal anti- PA antibody 1G3 was previously shown to be a potent antidote that shares FC domain dependency with the human monoclonal antibody MDX-1303 currently under clinical developmen...

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Format

Research paper

Research format

Journal article

Date created

2010-08-10

Creator

Radjainia, Mazdak / Hyun, Jae / Leysath, CE / Leppla, SH / Mitra, Alok

URL

http://hdl.handle.net/2292/13370

Related subjects

anthrax toxin / neutralizing antibody 1G3 / passive immunization / protein therapeutics / single-particle analysis / BACILLUS-ANTHRACIS / CRYSTAL-STRUCTURE / LETHAL FACTOR / MONOCLONAL-ANTIBODIES / ELECTRON-MICROSCOPY / CELL-RECEPTOR / PROPHYLAXIS / COMPONENT / BINDING

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