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. 1992 Dec;30(12):3122–3126. doi: 10.1128/jcm.30.12.3122-3126.1992

Antibody to a recombinant merozoite protein epitope identifies horses infected with Babesia equi.

D P Knowles Jr 1, L S Kappmeyer 1, D Stiller 1, S G Hennager 1, L E Perryman 1
PMCID: PMC270599  PMID: 1280648

Abstract

Horses infected with Babesia equi were previously identified by the presence of antibodies reactive with a merozoite surface protein epitope (D. P. Knowles, Jr., L. E. Perryman, L. S. Kappmeyer, and S. G. Hennager. J. Clin. Microbiol. 29:2056-2058, 1991). The antibodies were detected in a competitive inhibition enzyme-linked immunosorbent assay (CI ELISA) by using monoclonal antibody 36/133.97, which defines a protein epitope on the merozoite surface. The gene encoding this B. equi merozoite epitope was cloned and expressed in Escherichia coli. The recombinant merozoite protein, designated equi merozoite antigen 1 (EMA-1), was evaluated in the CI ELISA. Recombinant EMA-1 bound antibody from the sera of B. equi-infected horses from 18 countries. The antibody response to EMA-1 was then measured in horses experimentally infected with B. equi via transmission by the tick vector Boophilus microplus or by intravenous inoculation. Anti-EMA-1 antibody was detected 7 weeks post-tick exposure and remained, without reexposure to B. equi, for the 33 weeks of the evaluation period. The data indicate that recombinant EMA-1 can be used in the CI ELISA to detect horses infected with B. equi.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Anderson J. Use of monoclonal antibody in a blocking ELISA to detect group specific antibodies to bluetongue virus. J Immunol Methods. 1984 Nov 16;74(1):139–149. doi: 10.1016/0022-1759(84)90375-2. [DOI] [PubMed] [Google Scholar]
  2. Frerichs W. M., Holbrook A. A., Johnson A. J. Equine piroplasmosis: complement-fixation titers of horses infected with Babesia caballi. Am J Vet Res. 1969 May;30(5):697–702. [PubMed] [Google Scholar]
  3. Frerichs W. M., Holbrook A. A., Johnson A. J. Equine piroplasmosis: production of antigens for the complement-fixation test. Am J Vet Res. 1969 Aug;30(8):1337–1341. [PubMed] [Google Scholar]
  4. Friedhoff K. T. Die Piroplasmen der Equiden--Bedeutung für den internationalen Pferdeverkehr. Berl Munch Tierarztl Wochenschr. 1982 Oct 1;95(19):368–374. [PubMed] [Google Scholar]
  5. Goldberg A. L. Degradation of abnormal proteins in Escherichia coli (protein breakdown-protein structure-mistranslation-amino acid analogs-puromycin). Proc Natl Acad Sci U S A. 1972 Feb;69(2):422–426. doi: 10.1073/pnas.69.2.422. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Gubler U., Hoffman B. J. A simple and very efficient method for generating cDNA libraries. Gene. 1983 Nov;25(2-3):263–269. doi: 10.1016/0378-1119(83)90230-5. [DOI] [PubMed] [Google Scholar]
  7. Holbrook A. A. Biology of equine piroplasmosis. J Am Vet Med Assoc. 1969 Jul 15;155(2):453–454. [PubMed] [Google Scholar]
  8. Knowles D. P., Jr, Perryman L. E., Goff W. L., Miller C. D., Harrington R. D., Gorham J. R. A monoclonal antibody defines a geographically conserved surface protein epitope of Babesia equi merozoites. Infect Immun. 1991 Jul;59(7):2412–2417. doi: 10.1128/iai.59.7.2412-2417.1991. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Knowles D. P., Jr, Perryman L. E., Kappmeyer L. S., Hennager S. G. Detection of equine antibody to Babesia equi merozoite proteins by a monoclonal antibody-based competitive inhibition enzyme-linked immunosorbent assay. J Clin Microbiol. 1991 Sep;29(9):2056–2058. doi: 10.1128/jcm.29.9.2056-2058.1991. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. McGuire T. C., Van Hoosier G. L., Jr, Henson J. B. The complement-fixation reaction in eguine infectious anemia: demonstration of inhibition by IgG (T). J Immunol. 1971 Dec;107(6):1738–1744. [PubMed] [Google Scholar]
  11. Palmer D. A., Buening G. M., Carson C. A. Cryopreservation of Babesia bovis for in vitro cultivation. Parasitology. 1982 Jun;84(Pt 3):567–572. doi: 10.1017/s0031182000052835. [DOI] [PubMed] [Google Scholar]
  12. Short J. M., Fernandez J. M., Sorge J. A., Huse W. D. Lambda ZAP: a bacteriophage lambda expression vector with in vivo excision properties. Nucleic Acids Res. 1988 Aug 11;16(15):7583–7600. doi: 10.1093/nar/16.15.7583. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Towbin H., Gordon J. Immunoblotting and dot immunobinding--current status and outlook. J Immunol Methods. 1984 Sep 4;72(2):313–340. doi: 10.1016/0022-1759(84)90001-2. [DOI] [PubMed] [Google Scholar]
  14. Young R. A., Davis R. W. Efficient isolation of genes by using antibody probes. Proc Natl Acad Sci U S A. 1983 Mar;80(5):1194–1198. doi: 10.1073/pnas.80.5.1194. [DOI] [PMC free article] [PubMed] [Google Scholar]

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