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Related Experiment Video

Updated: Jul 10, 2026

Opsono-Adherence Assay to Evaluate Functional Antibodies in Vaccine Development Against Bacillus anthracis and Other Encapsulated Pathogens

Opsono-Adherence Assay to Evaluate Functional Antibodies in Vaccine Development Against Bacillus anthracis and Other Encapsulated Pathogens

Published on: May 19, 2020

Catalytically inactive anthrax toxin(s) are potential prophylactic agents.

Megha Gupta¹, Sheeba Alam, Rakesh Bhatnagar

¹School of Biotechnology, Jawaharlal Nehru University, New Delhi 110067, India.

|November 6, 2007

Summary

Catalytic mutants of Bacillus anthracis lethal factor and edema factor, when combined with protective antigen, show potential as non-toxic anthrax prophylactics or therapeutics.

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Published on: January 31, 2018

Area of Science:

Microbiology
Toxicology
Immunology

Background:

Anthrax exotoxin, a key factor in Bacillus anthracis pathogenesis, comprises lethal toxin (protective antigen [PA] + lethal factor [LF]) and edema toxin (PA + edema factor [EF]).
Understanding the individual components and their interactions is crucial for developing targeted interventions against anthrax.

Purpose of the Study:

To investigate the potential of catalytically inactive mutants of LF and EF as non-toxic components of anthrax toxins.
To evaluate the prophylactic and therapeutic potential of these mutant proteins in combination with PA.

Main Methods:

Generation of catalytic mutants: LFE687A and EFH351A.
In vitro assessment of toxin-mediated activity inhibition.
In vivo evaluation of lethality and protection in mouse models.
Assessment of cell toxicity when combined with PA.

Main Results:

LFE687A and EFH351A competitively inhibited toxin activity in vitro and lethality in vivo.
PA combined with EFH351A was non-lethal; PA combined with LFE687A showed reduced virulence.
Full protection against lethal toxin challenge was achieved with PA combined with both LFE687A and EFH351A.
The mutant proteins were non-toxic to sensitive cell lines when combined with PA.

Conclusions:

Catalytically inactive LF and EF mutants can neutralize anthrax toxin activity.
These inactive mutants, when formulated with PA, represent promising candidates for anthrax prophylactics and therapeutics.
Further research into these mutant proteins could lead to novel strategies for anthrax prevention and treatment.