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Temperature-mediated recombinant anthrax protective antigen aggregate development: Implications for toxin formation

Juan C Amador-Molina¹, Esther D Valerdi-Madrigal¹, Rocío I Domínguez-Castillo¹

¹Center for Biologics Evaluation and Research, Food and Drug Administration, 10903 New Hampshire Avenue, Silver Spring, MD 20993, United States.

|July 2, 2016

Summary

Heat-induced aggregation of recombinant protective antigen (rPA) in anthrax vaccines significantly reduces its ability to neutralize lethal toxin (LeTx). This aggregation also impairs the antibody response in immunized mice, highlighting the need for stability testing.

Keywords:

Aggregation Anthrax Protective antigen Stability Vaccine

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Area of Science:

Biochemistry
Immunology
Vaccine Development

Background:

Anthrax vaccines utilize recombinant protective antigen (rPA) as a key antigen.
rPA is susceptible to aggregation at elevated temperatures (≥40°C), compromising its efficacy.
Aggregated rPA loses its capacity to form lethal toxin (LeTx) with Lethal Factor.

Purpose of the Study:

To investigate the impact of rPA aggregation on its immunogenicity and ability to neutralize lethal toxin.
To evaluate the correlation between rPA's functional activity and the immune response it elicits.
To assess the utility of different assays for quality control of rPA in vaccine formulations.

Main Methods:

Subjecting rPA to various time and temperature conditions to induce aggregation.
Analyzing rPA aggregation using gel electrophoresis.
Measuring LeTx formation and activity using a macrophage lysis assay (MLA).
Assessing antibody titers in immunized mice via Toxicity Neutralization Assay (TNA) and Enzyme Linked Immunosorbent Assay (ELISA).

Main Results:

Heat treatment (50°C for 30 min) induced high-mass rPA aggregates, significantly reducing LeTx activity (approx. 30-fold decrease).
Mice immunized with heat-treated rPA showed substantially lower antibody titers (approx. 49-fold lower by TNA) compared to those immunized with native rPA.
ELISA revealed only a 2-7 fold decrease in anti-rPA titers, suggesting TNA is more sensitive to functional impairment.

Conclusions:

rPA's ability to form LeTx directly correlates with its capacity to generate neutralizing antibodies.
Protein aggregation critically impairs the immunogenic potential of rPA in anthrax vaccines.
MLA shows potential as an in-process quality test, while TNA remains superior for assessing vaccine potency due to its sensitivity to functional antibody responses.