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Infection and immunity1991; 59(7); 2412-2417; doi: 10.1128/iai.59.7.2412-2417.1991

A monoclonal antibody defines a geographically conserved surface protein epitope of Babesia equi merozoites.

Abstract: Babesiosis is a tick-borne hemoparasitic disease affecting horses worldwide. To investigate mechanisms of immunity to this parasite, the antibody response of infected horses to Babesia equi merozoite proteins was evaluated. Immunoprecipitation of B. equi merozoite antigens with sera from infected horses revealed 11 major proteins of 210, 144, 108, 88, 70, 56, 44, 36, 34, 28, and 25 kDa. Monoclonal antibody (MAb) 36/133.97, which binds to live merozoites, immunoprecipitated proteins of 44, 36, 34, and 28 kDa. When immunoprecipitations were performed with in vitro translation products of merozoite mRNA, MAb 36/133.97 immunoprecipitated proteins of 38, 28, 26, and 23 kDa which comigrated with proteins immunoprecipitated by sera from infected horses at 10(-3) to 10(-4) dilutions. In Western blot analysis, MAb 36/133.97 recognized proteins of 44, 36, 34, and 28 kDa, and a 28-kDa protein was identified by sera from infected horses at a dilution of 10(-4). MAb 36/133.97 bound to B. equi isolates from Florida and Europe. Furthermore, the binding of MAb 36/133.97 to merozoite proteins was inhibited by sera of infected horses from 19 countries. Collectively, these data indicate MAb 36/133.97 binds to a geographically conserved peptide epitope on multiple B. equi merozoite proteins, including a merozoite surface protein, and MAb 36/133.97 reacts with a B. equi protein immunodominant in infected horses.
Publication Date: 1991-07-11 PubMed ID: 1711016PubMed Central: PMC258026DOI: 10.1128/iai.59.7.2412-2417.1991Google Scholar: Lookup
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  • Comparative Study
  • Journal Article
  • Research Support
  • U.S. Gov't
  • Non-P.H.S.

Summary

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The research article discusses the study of Babesiosis, a tick-borne disease infecting horses, and how a specific monoclonal antibody (MAb 36/133.97) binds to proteins of the Babesia equi merozoites (parasite’s infective stage), including an immunodominant surface protein recognized by infected horses’ immune system. This antibody-antigen interaction is consistent across various geographic regions.

Research Methodology and Findings

  • The researchers commenced by examining the antibody response of infected horses to Babesia equi merozoite proteins. They established through precipitation of these antigens with sera from infected horses that there were 11 major proteins. Sizes of these proteins were specified in kilodaltons (kDa), denoting the mass of the protein molecules.
  • The monoclonal antibody (MAb) 36/133.97, which attaches to live merozoites, was found to precipitate proteins of 44, 36, 34, and 28 kDa. This indicated a specific interaction between these proteins and the antibody.
  • Further evaluation was done using in vitro translated products of merozoite mRNA. Here, cellular machinery in a lab setting was used to convert the merozoite’s mRNA into functional protein products. The MAb 36/133.97 then immunoprecipitated proteins of 38, 28, 26, and 23 kDa which migrated similarly to proteins precipitated by sera from infected horses at certain dilutions. This reaffirmed the antibody’s affinity for these proteins.
  • In Western blot analysis, a technique for detecting specific protein molecules, MAb 36/133.97 identified proteins of 44, 36, 34, and 28 kDa, further highlighting the presence and importance of these proteins.

Geographical Conservation and Immune Response to Merozoite Proteins

  • The researchers found that the binding of MAb 36/133.97 was consistent with B. equi isolates from different geographical locations including Florida and Europe, hence proving the geographical conservation of this protein-antibody interaction.
  • Moreover, it was discovered that the binding of MAb 36/133.97 to these merozoite proteins was inhibited by sera of infected horses from 19 countries. This revealed that these horses’ immune systems identified and responded to these proteins similarly, regardless of geographical location.
  • The data collected indicated MAb 36/133.97 binds to a geographically conserved peptide epitope on multiple B. equi merozoite proteins. One of these proteins is a merozoite surface protein which was found to be immunodominant, meaning it invoked a strong immune response in infected horses.

Cite This Article

APA
Knowles DP, Perryman LE, Goff WL, Miller CD, Harrington RD, Gorham JR. (1991). A monoclonal antibody defines a geographically conserved surface protein epitope of Babesia equi merozoites. Infect Immun, 59(7), 2412-2417. https://doi.org/10.1128/iai.59.7.2412-2417.1991

Publication

ISSN: 0019-9567
NlmUniqueID: 0246127
Country: United States
Language: English
Volume: 59
Issue: 7
Pages: 2412-2417

Researcher Affiliations

Knowles, D P
  • Animal Disease Research Unit, U.S. Department of Agriculture, Pullman, Washington 99164-7030.
Perryman, L E
    Goff, W L
      Miller, C D
        Harrington, R D
          Gorham, J R

            MeSH Terms

            • Animals
            • Antibodies, Monoclonal / immunology
            • Antibodies, Protozoan / immunology
            • Antigens, Protozoan / chemistry
            • Antigens, Protozoan / immunology
            • Antigens, Surface / immunology
            • Babesia / immunology
            • Babesiosis / immunology
            • Cross Reactions
            • Epitopes
            • Fluorescent Antibody Technique
            • Geography
            • Horse Diseases / immunology
            • Horse Diseases / parasitology
            • Horses
            • Molecular Weight
            • Precipitin Tests
            • Protozoan Proteins / chemistry
            • Protozoan Proteins / immunology

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