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Infection and immunity1985; 48(2); 417-421; doi: 10.1128/iai.48.2.417-421.1985

Nonimmune binding of equine immunoglobulin by the causative organism of contagious equine metritis, Taylorella equigenitalis.

Abstract: This study identifies nonimmune binding of equine immunoglobulin by the causative organism of contagious equine metritis. Immunoglobulin binding to the bacterium was strongest for immunoglobulin G (IgG) and less for IgM; IgA was not bound. Binding of equine IgG was inhibited by human IgG, but not by IgG of domestic animals. Immunoglobulin binding by the bacterium appeared to be directed towards an epitope in the hinge region of the immunoglobulin molecule.
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Publication Date: 1985-05-01 PubMed ID: 4039299PubMed Central: PMC261330DOI: 10.1128/iai.48.2.417-421.1985Google 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 research focuses on the interaction of contagious equine metritis causing bacteria, Taylorella equigenitalis, with equine immunoglobulin, particularly IgG. The bacteria seem to bind non-immune equine immunoglobulins, suggesting a potential tactic in avoiding the horse’s immune defense.

Background of the Study

  • This research takes a detailed look at the binding mechanism between the bacterium, Taylorella equigenitalis, which causes contagious equine metritis (a sexually transmitted disease in horses), and equine immunoglobulins (protein molecules that play a key role in the immune response).
  • The strong binding activity taking place between the bacteria and immunoglobulin G (IgG) is the main focal point of the study. IgG is one of the five classes of immunoglobulin and is crucial for the immune defense against pathogens.

Key Findings of the Study

  • The study observed a binding between the bacterium and the immunoglobulins in horses, especially IgG, which seems to be the case less with IgM and none with IgA.
  • However, it was noted that the binding of equine IgG was inhibited by human IgG, suggesting a kind of cross-species protection. Yet, the same level of inhibition wasn’t observed in the case of IgG from other domestic animals, which indicates species-specificity in the interaction.
  • The locus of interaction between the bacterium and the IgG appears to be in the hinge region of the immunoglobulin molecule. This region is a flexible part of the immunoglobulin that enables it to bind antigens effectively.

Implications of the Study

  • The findings from this study provide insights into how Taylorella equigenitalis possibly circumvents the immune defense mechanisms of horses. By binding non-immune equine immunoglobulins, the bacteria may be making a strategic evasion of the immune system’s attempts to eliminate them.
  • Understanding these binding mechanisms could potentially aid in the development of targeted treatments or vaccines for better management of contagious equine metritis.

Cite This Article

APA
Widders PR, Stokes CR, Newby TJ, Bourne FJ. (1985). Nonimmune binding of equine immunoglobulin by the causative organism of contagious equine metritis, Taylorella equigenitalis. Infect Immun, 48(2), 417-421. https://doi.org/10.1128/iai.48.2.417-421.1985

Publication

Infection and immunity
ISSN: 0019-9567
NlmUniqueID: 0246127
Country: United States
Language: English
Volume: 48
Issue: 2
Pages: 417-421

Researcher Affiliations

Widders, P R
    Stokes, C R
      Newby, T J
        Bourne, F J

          MeSH Terms

          • Animals
          • Endometritis / microbiology
          • Endometritis / veterinary
          • Enzyme-Linked Immunosorbent Assay
          • Female
          • Gram-Negative Bacteria / metabolism
          • Horse Diseases / microbiology
          • Horses
          • Humans
          • Immunoglobulin A / metabolism
          • Immunoglobulin Fab Fragments / metabolism
          • Immunoglobulin Fc Fragments / metabolism
          • Immunoglobulin G / metabolism
          • Immunoglobulin M / metabolism
          • Immunoglobulins / metabolism
          • Species Specificity

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          Citations

          This article has been cited 7 times.
          1. Cooke DL, Borriello SP. Nonspecific binding of Clostridium difficile toxin A to murine immunoglobulins occurs via the fab component. Infect Immun 1998 May;66(5):1981-4.
            doi: 10.1128/IAI.66.5.1981-1984.1998pubmed: 9573079google scholar: lookup
          2. Sandt CH, Wang YD, Wilson RA, Hill CW. Escherichia coli strains with nonimmune immunoglobulin-binding activity. Infect Immun 1997 Nov;65(11):4572-9.
            doi: 10.1128/iai.65.11.4572-4579.1997pubmed: 9353035google scholar: lookup
          3. Mintz KP, Fives-Taylor PM. Identification of an immunoglobulin Fc receptor of Actinobacillus actinomycetemcomitans. Infect Immun 1994 Oct;62(10):4500-5.
            doi: 10.1128/iai.62.10.4500-4505.1994pubmed: 7927715google scholar: lookup
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            doi: 10.1128/iai.53.2.420-426.1986pubmed: 3525414google scholar: lookup
          5. Gogolewski RP, Schaefer DC, Wasson SK, Corbeil RR, Corbeil LB. Pulmonary persistence of Haemophilus somnus in the presence of specific antibody. J Clin Microbiol 1989 Aug;27(8):1767-74.
            doi: 10.1128/jcm.27.8.1767-1774.1989pubmed: 2768464google scholar: lookup
          6. Alexander AG, Lowes HR, Kenny GE. Identification of a mycoplasmal protein which binds immunoglobulins nonimmunologically. Infect Immun 1991 Jun;59(6):2147-51.
            doi: 10.1128/iai.59.6.2147-2151.1991pubmed: 2037376google scholar: lookup
          7. Janson H, Hedén LO, Grubb A, Ruan MR, Forsgren A. Protein D, an immunoglobulin D-binding protein of Haemophilus influenzae: cloning, nucleotide sequence, and expression in Escherichia coli. Infect Immun 1991 Jan;59(1):119-25.
            doi: 10.1128/iai.59.1.119-125.1991pubmed: 1987023google scholar: lookup
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