A Viral Nanoparticle with Dual Function as an Anthrax Antitoxin and Vaccine | Zendy

Darly J. Manayani | Zendy; Diane Thomas | Zendy; Kelly A. Dryden | Zendy; Vijay Reddy | Zendy; Marc E Siladi | Zendy; John Marlett | Zendy; G. Jonah Rainey | Zendy; Michael E. Pique | Zendy; Heather M. Scobie | Zendy; Mark Yeager | Zendy; John A. T. Young | Zendy; Marianne Manchester | Zendy; Anette Schneemann | Zendy

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A Viral Nanoparticle with Dual Function as an Anthrax Antitoxin and Vaccine

Author(s) -

Darly J. Manayani,

Diane Thomas,

Kelly A. Dryden,

Vijay Reddy,

Marc E Siladi,

John Marlett,

G. Jonah Rainey,

Michael E. Pique,

Heather M. Scobie,

Mark Yeager,

John A. T. Young,

Marianne Manchester,

Anette Schneemann

Publication year - 2007

Publication title -

plos pathogens

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 3.719

H-Index - 206

eISSN - 1553-7374

pISSN - 1553-7366

DOI - 10.1371/journal.ppat.0030142

Subject(s) - anthrax toxin , bacillus anthracis , anthrax vaccines , antitoxin , virology , microbiology and biotechnology , toxin , biology , virus , diphtheria toxin , adjuvant , antibody , chemistry , recombinant dna , fusion protein , immunization , immunology , dna vaccination , biochemistry , bacteria , genetics , gene

The recent use of Bacillus anthracis as a bioweapon has stimulated the search for novel antitoxins and vaccines that act rapidly and with minimal adverse effects. B. anthracis produces an AB-type toxin composed of the receptor-binding moiety protective antigen (PA) and the enzymatic moieties edema factor and lethal factor. PA is a key target for both antitoxin and vaccine development. We used the icosahedral insect virus Flock House virus as a platform to display 180 copies of the high affinity, PA-binding von Willebrand A domain of the ANTXR2 cellular receptor. The chimeric virus-like particles (VLPs) correctly displayed the receptor von Willebrand A domain on their surface and inhibited lethal toxin action in in vitro and in vivo models of anthrax intoxication. Moreover, VLPs complexed with PA elicited a potent toxin-neutralizing antibody response that protected rats from anthrax lethal toxin challenge after a single immunization without adjuvant. This recombinant VLP platform represents a novel and highly effective, dually-acting reagent for treatment and protection against anthrax.

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