» Articles » PMID: 22123065

Antibodies for Biodefense

Overview
Journal MAbs
Date 2011 Nov 30
PMID 22123065
Citations 36
Authors
Affiliations
Soon will be listed here.
Abstract

Potential bioweapons are biological agents (bacteria, viruses, and toxins) at risk of intentional dissemination. Biodefense, defined as development of therapeutics and vaccines against these agents, has seen an increase, particularly in the US following the 2001 anthrax attack. This review focuses on recombinant antibodies and polyclonal antibodies for biodefense that have been accepted for clinical use. These antibodies aim to protect against primary potential bioweapons, or category A agents as defined by the Centers for Disease Control and Prevention (Bacillus anthracis, Yersinia pestis, Francisella tularensis, botulinum neurotoxins, smallpox virus, and certain others causing viral hemorrhagic fevers) and certain category B agents. Potential for prophylactic use is presented, as well as frequent use of oligoclonal antibodies or synergistic effect with other molecules. Capacities and limitations of antibodies for use in biodefense are discussed, and are generally applicable to the field of infectious diseases.

Citing Articles

Isolation and characterization of Hc-targeting chimeric heavy chain antibodies neutralizing botulinum neurotoxin type B.

Jiang Y, Wang R, Guo J, Cheng K, Chen L, Wang X Front Immunol. 2024; 15:1380694.

PMID: 38779676 PMC: 11109933. DOI: 10.3389/fimmu.2024.1380694.


Functional epitopes and neutralizing antibodies of vaccinia virus.

Peng F, Hu N, Liu Y, Xing C, Luo L, Li X Front Microbiol. 2023; 14:1255935.

PMID: 37954238 PMC: 10634548. DOI: 10.3389/fmicb.2023.1255935.


Centaur antibodies: Engineered chimeric equine-human recombinant antibodies.

Rosenfeld R, Alcalay R, Zvi A, Ben-David A, Noy-Porat T, Chitlaru T Front Immunol. 2022; 13:942317.

PMID: 36059507 PMC: 9437483. DOI: 10.3389/fimmu.2022.942317.


Therapeutic Antibodies Against Shiga Toxins: Trends and Perspectives.

Henrique I, Sacerdoti F, Ferreira R, Henrique C, Amaral M, Piazza R Front Cell Infect Microbiol. 2022; 12:825856.

PMID: 35223548 PMC: 8866733. DOI: 10.3389/fcimb.2022.825856.


Developing Recombinant Antibodies by Phage Display Against Infectious Diseases and Toxins for Diagnostics and Therapy.

Roth K, Wenzel E, Ruschig M, Steinke S, Langreder N, Heine P Front Cell Infect Microbiol. 2021; 11:697876.

PMID: 34307196 PMC: 8294040. DOI: 10.3389/fcimb.2021.697876.


References
1.
Rotz L, Khan A, Lillibridge S, Ostroff S, Hughes J . Public health assessment of potential biological terrorism agents. Emerg Infect Dis. 2002; 8(2):225-30. PMC: 2732458. DOI: 10.3201/eid0802.010164. View

2.
Nowakowski A, Wang C, Powers D, Amersdorfer P, Smith T, Montgomery V . Potent neutralization of botulinum neurotoxin by recombinant oligoclonal antibody. Proc Natl Acad Sci U S A. 2002; 99(17):11346-50. PMC: 123259. DOI: 10.1073/pnas.172229899. View

3.
Galimand M, Carniel E, Courvalin P . Resistance of Yersinia pestis to antimicrobial agents. Antimicrob Agents Chemother. 2006; 50(10):3233-6. PMC: 1610074. DOI: 10.1128/AAC.00306-06. View

4.
Boles J, Pitt M, LeClaire R, Gibbs P, Ulrich R, Bavari S . Correlation of body temperature with protection against staphylococcal enterotoxin B exposure and use in determining vaccine dose-schedule. Vaccine. 2003; 21(21-22):2791-6. DOI: 10.1016/s0264-410x(03)00222-6. View

5.
Adekar S, Mark Jones R, Elias M, Al-Saleem F, Root M, Simpson L . Hybridoma populations enriched for affinity-matured human IgGs yield high-affinity antibodies specific for botulinum neurotoxins. J Immunol Methods. 2008; 333(1-2):156-66. DOI: 10.1016/j.jim.2008.01.015. View