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Glycoconjugate journal2005; 22(1-2); 27-34; doi: 10.1007/s10719-005-0228-2

PNA-binding glycans are expressed at high levels on horse mature and immature T lymphocytes and a subpopulation of B lymphocytes.

Abstract: In mammals, the binding of peanut agglutinin (PNA) on the plasma membrane defines subpopulations among lymphocytes from peripheral blood and lymphoid organs. PNA binds Galbeta 1,3GalNAc residues provided that they are not sialylated. Here, we studied the expression of PNA-binding glycans on healthy horse peripheral blood, thymus, lymph node and spleen lymphocytes. We first demonstrated the binding specificity of PNA for galactose residues by competition experiments and the inhibitory role of sialic acids in PNA binding by sialidase digestion. Unlike human and murine lymphocytes, all equine lymphocytes were found positive by flow cytometry analysis. Double-staining analyses showed that lymphocytes expressing high levels of PNA-binding glycans (PNA(high) lymphocytes) were made up of the great majority of CD5(+), CD4(+) and CD8(+) cells, and of 30 and 50% of sIg-bearing lymphocytes in peripheral blood and in lymph nodes or spleen, respectively. Lectin histochemistry suggested that lymph node germinal centres contained PNA(high) B cells. Contrary to what is found in humans and mice, PNA staining intensity on CD5(+), CD4(+) and CD8(+) cells did not differentiate immature from mature T lymphocytes in the equine thymus. The functional consequences of these differences are discussed.
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Publication Date: 2005-05-03 PubMed ID: 15864432DOI: 10.1007/s10719-005-0228-2Google Scholar: Lookup
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  • Journal Article
  • Research Support
  • Non-U.S. Gov't

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 investigates how peanut agglutinin (PNA), a type of plant protein, interacts with different types of cells in the immune systems of horses. Results suggest that all types of equine immune cells show some level of PNA binding, and this binding does not differentiate between mature and immature cells contrary to what is observed in humans and mice.

Research Aims and Methods

  • The primary objective of this research was to study the expression of PNA-binding glycans on healthy horse peripheral blood, thymus, lymph node and spleen lymphocytes and to understand any functional consequences of these interactions.
  • To demonstrate the binding specificity, competition experiments were conducted, and the inhibitory role of sialic acids in PNA binding was also explored.
  • PNA’s affinity for galactose residues was demonstrated using inhibition experiments with sialidase digestion, a process that removes sialic acids responsible for negatively affecting PNA binding.
  • The intensity of PNA binding on different cells was tested using flow cytometry analysis and double-staining techniques. This helped differentiate cells high and low in PNA-binding glycans.

Findings and Conclusion

  • Unlike human and murine lymphocytes, all equine lymphocytes were found positive for PNA by flow cytometry analysis. This means that the binding of PNA to cell membranes is a universal characteristic of equine lymphocytes.
  • Most cells tagged as CD5(+), CD4(+), and CD8(+), which are markers for different types of lymphocytes, expressed high level of PNA-binding glycans. The process also revealed that 30% to 50% of sIg-bearing lymphocytes in peripheral blood and in lymph nodes or spleen also exhibited the same trait.
  • Lectin histochemistry suggested that lymph node germinal centres contained PNA(high) B cells, suggesting a wider spread of PNA interaction in the equine immune system.
  • Unlike in humans and mice, PNA staining intensity on CD5(+), CD4(+), and CD8(+) cells did not differentiate immature from mature T lymphocytes in the equine thymus, a finding that could have broad implications for understanding equine immunity and disease resistance.

Implications

  • The study provides pivotal insights into the binding of plant proteins to horse immune cells and its implications.
  • Understanding this interaction is critical in examining the immune responses of horses and could be beneficial for the development of new therapeutic strategies or the improvement of existing ones in equine health.

Cite This Article

APA
Mérant C, Messouak A, Cadoré JL, Monier JC. (2005). PNA-binding glycans are expressed at high levels on horse mature and immature T lymphocytes and a subpopulation of B lymphocytes. Glycoconj J, 22(1-2), 27-34. https://doi.org/10.1007/s10719-005-0228-2

Publication

Glycoconjugate journal
ISSN: 0282-0080
NlmUniqueID: 8603310
Country: United States
Language: English
Volume: 22
Issue: 1-2
Pages: 27-34

Researcher Affiliations

Mérant, Catherine
  • Laboratoire d'Immunopathologie, Service de Médecine, Ecole Nationale Vétérinaire de Lyon, Marcy-l'Etoile, France. CMerant@aol.com
Messouak, Ali
    Cadoré, Jean-Luc
      Monier, Jean-Claude

        MeSH Terms

        • Animals
        • Cell Membrane / metabolism
        • Female
        • Flow Cytometry
        • Histocytochemistry
        • Horses
        • Lymph Nodes / cytology
        • Lymph Nodes / metabolism
        • Male
        • Organ Specificity
        • Peanut Agglutinin / metabolism
        • Polysaccharides / biosynthesis
        • Protein Binding
        • Spleen / cytology
        • Spleen / metabolism
        • T-Lymphocyte Subsets / metabolism
        • T-Lymphocytes / metabolism
        • Thymus Gland / cytology
        • Thymus Gland / metabolism

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        Citations

        This article has been cited 1 times.
        1. Balen B, Krsnik-Rasol M, Zamfir AD, Zadro I, Vakhrushev SY, Peter-Katalinic J. Assessment of N-glycan heterogeneity of cactus glycoproteins by one-dimensional gel electrophoresis and matrix-assisted laser desorption/ionization time-of-flight mass spectrometry. J Biomol Tech 2007 Jul;18(3):162-72.
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