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PloS one2021; 16(10); e0258317; doi: 10.1371/journal.pone.0258317

Development of ELISA based on Bacillus anthracis capsule biosynthesis protein CapA for naturally acquired antibodies against anthrax.

Abstract: Anthrax is a zoonotic disease caused by the gram-positive spore-forming bacterium Bacillus anthracis. Detecting naturally acquired antibodies against anthrax sublethal exposure in animals is essential for anthrax surveillance and effective control measures. Serological assays based on protective antigen (PA) of B. anthracis are mainly used for anthrax surveillance and vaccine evaluation. Although the assay is reliable, it is challenging to distinguish the naturally acquired antibodies from vaccine-induced immunity in animals because PA is cross-reactive to both antibodies. Although additional data on the vaccination history of animals could bypass this problem, such data are not readily accessible in many cases. In this study, we established a new enzyme-linked immunosorbent assay (ELISA) specific to antibodies against capsule biosynthesis protein CapA antigen of B. anthracis, which is non-cross-reactive to vaccine-induced antibodies in horses. Using in silico analyses, we screened coding sequences encoded on pXO2 plasmid, which is absent in the veterinary vaccine strain Sterne 34F2 but present in virulent strains of B. anthracis. Among the 8 selected antigen candidates, capsule biosynthesis protein CapA (GBAA_RS28240) and peptide ABC transporter substrate-binding protein (GBAA_RS28340) were detected by antibodies in infected horse sera. Of these, CapA has not yet been identified as immunoreactive in other studies to the best of our knowledge. Considering the protein solubility and specificity of B. anthracis, we prepared the C-terminus region of CapA, named CapA322, and developed CapA322-ELISA based on a horse model. Comparative analysis of the CapA322-ELISA and PAD1-ELISA (ELISA uses domain one of the PA) showed that CapA322-ELISA could detect anti-CapA antibodies in sera from infected horses but was non-reactive to sera from vaccinated horses. The CapA322-ELISA could contribute to the anthrax surveillance in endemic areas, and two immunoreactive proteins identified in this study could be additives to the improvement of current or future vaccine development.
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Publication Date: 2021-10-11 PubMed ID: 34634075PubMed Central: PMC8504768DOI: 10.1371/journal.pone.0258317Google Scholar: Lookup
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Summary

This research summary has been generated with artificial intelligence and may contain errors and omissions. Refer to the original study to confirm details provided. Submit correction.

This study discusses the development of an Enzyme-Linked Immunosorbent Assay (ELISA) method that is specific for identifying naturally acquired anthrax antibodies in animals. Instead of relying on the commonly used protective antigen (PA) which can lead to confusion between natural and vaccine-acquired immunity, this ELISA method uses the CapA from Bacillus anthracis, a protein distinct from what’s included in existing vaccines.

Development of the CapA322-ELISA

  • The need for a new ELISA method arose due to the difficulty in differentiating natural immunity against anthrax from vaccinated immunity in animals using the existing methods which primarily rely on the protective antigen (PA).
  • The authors initially screened the pXO2 plasmid, a sequence not present in the common veterinary vaccine but found in virulent B. anthracis strains, using in silico analyses.
  • Out of 8 antigen candidates, they found that capsule biosynthesis protein CapA and peptide ABC transporter substrate-binding protein could be detected by antibodies present in the sera of infected horses.
  • Among these, CapA was unique because it had not been previously identified as immunoreactive. They prepared the C-terminus region of CapA, named CapA322, and developed CapA322-ELISA.

Comparison and Results of CapA322-ELISA

  • The authors then compared the performance of CapA322-ELISA with PAD1-ELISA which relies on the PA’s domain one.
  • Results showed that CapA322-ELISA was able to detect anti-CapA antibodies from sera of infected horses but had no reaction to sera from vaccinated horses. This differentiated it from PAD1-ELISA which is cross-reactive to both antibodies.

Implications and Future Work

  • CapA322-ELISA could be an effective tool in anthrax surveillance specifically in areas where the disease is endemic.
  • In addition, the newly identified immunoreactive proteins may be useful in enhancing existing or developing new vaccines.
  • However, since this study only used horse sera, further research might be needed to test its applicability to other animals.

Cite This Article

APA
Zorigt T, Furuta Y, Simbotwe M, Ochi A, Tsujinouchi M, Shawa M, Shimizu T, Isoda N, Enkhtuya J, Higashi H. (2021). Development of ELISA based on Bacillus anthracis capsule biosynthesis protein CapA for naturally acquired antibodies against anthrax. PLoS One, 16(10), e0258317. https://doi.org/10.1371/journal.pone.0258317

Publication

PloS one
ISSN: 1932-6203
NlmUniqueID: 101285081
Country: United States
Language: English
Volume: 16
Issue: 10
Pages: e0258317

Researcher Affiliations

Zorigt, Tuvshinzaya
  • Division of Infection and Immunity, International Institute for Zoonosis Control (Former Research Center for Zoonosis Control), Hokkaido University, Sapporo, Japan.
  • Graduate School of Infectious Diseases, School of Veterinary Medicine, Hokkaido University, Sapporo, Japan.
Furuta, Yoshikazu
  • Division of Infection and Immunity, International Institute for Zoonosis Control (Former Research Center for Zoonosis Control), Hokkaido University, Sapporo, Japan.
  • Graduate School of Infectious Diseases, School of Veterinary Medicine, Hokkaido University, Sapporo, Japan.
Simbotwe, Manyando
  • Division of Infection and Immunity, International Institute for Zoonosis Control (Former Research Center for Zoonosis Control), Hokkaido University, Sapporo, Japan.
Ochi, Akihiro
  • Equine Research Institute, Japan Racing Association, Shimotsuke, Tochigi, Japan.
Tsujinouchi, Mai
  • Division of Infection and Immunity, International Institute for Zoonosis Control (Former Research Center for Zoonosis Control), Hokkaido University, Sapporo, Japan.
Shawa, Misheck
  • Division of Infection and Immunity, International Institute for Zoonosis Control (Former Research Center for Zoonosis Control), Hokkaido University, Sapporo, Japan.
  • Graduate School of Infectious Diseases, School of Veterinary Medicine, Hokkaido University, Sapporo, Japan.
Shimizu, Tomoko
  • Division of Infection and Immunity, International Institute for Zoonosis Control (Former Research Center for Zoonosis Control), Hokkaido University, Sapporo, Japan.
Isoda, Norikazu
  • Laboratory of Microbiology, School of Veterinary Medicine, Hokkaido University, Sapporo, Japan.
Enkhtuya, Jargalsaikhan
  • Laboratory of Food Hygiene, Institute of Veterinary Medicine, Ulaanbaatar, Mongolia.
Higashi, Hideaki
  • Division of Infection and Immunity, International Institute for Zoonosis Control (Former Research Center for Zoonosis Control), Hokkaido University, Sapporo, Japan.
  • Graduate School of Infectious Diseases, School of Veterinary Medicine, Hokkaido University, Sapporo, Japan.

MeSH Terms

  • Animals
  • Anthrax / immunology
  • Anthrax Vaccines / immunology
  • Antibodies, Bacterial / immunology
  • Antigens, Bacterial / immunology
  • Bacillus anthracis / immunology
  • Bacterial Capsules / immunology
  • Bacterial Proteins / immunology
  • Bacterial Proteins / isolation & purification
  • Enzyme-Linked Immunosorbent Assay / methods
  • Heat-Shock Proteins / immunology
  • Heat-Shock Proteins / isolation & purification
  • Horses
  • Immunoglobulin G / immunology
  • Plasmids / metabolism
  • Sequence Homology, Amino Acid
  • Spores, Bacterial / immunology

Conflict of Interest Statement

The authors have declared that no competing interests exist.

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