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Toxicon : official journal of the International Society on Toxinology2012; 60(6); 1215-1221; doi: 10.1016/j.toxicon.2012.07.015

Horse IgG- and ostrich IgY-F(ab’)₂ groups have different affinities for mice erythrocytes and lymphocytes. Implications for avian immunoglobulin therapeutic usefulness.

Abstract: We used high sensitivity and resolution fluorescence microscopy to study the interaction of ostrich IgY, horse F(ab')₂ and horse IgG with mice lymphocyte and erythrocyte plasma membrane. The immunoglobulins were labeled with fluorescein isotiocyanate (FITC). Our results show an interaction of IgY with lymphocyte plasma membrane which does not result in endocytosis of the labeled protein. Less IgG and its F(ab')₂ fraction bind to lymphocytes, and this binding seems to be followed by endocytosis producing a diffuse cytoplasmic fluorescence in most lymphocytes exposed to FITC-IgG or FITC-F(ab')₂. Cytoplasmic fluorescence resembling FITC was not observed in lymphocytes exposed to FITC-IgY. Receptors in the erythrocyte membrane also differentiate between avian and horse Ig; while erythrocytes exposed to horse Igs became intensely fluorescent for at least 5 h, no erythrocyte labeling occurred when FITC-IgY was used. Our results suggest that IgY may be a stronger activator of adaptive immunity than horse IgG in mammals. Adaptive immunity against IgY is detrimental to its IV therapeutic use in humans and other mammals.
Publication Date: 2012-08-13 PubMed ID: 22921580DOI: 10.1016/j.toxicon.2012.07.015Google Scholar: Lookup
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  • Journal Article
  • Research Support
  • Non-U.S. Gov't

Summary

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This study used high-resolution fluorescence microscopy to observe the interaction of various immunoglobulins from horses and ostriches with mouse cell membranes, finding that ostrich IgY may potentially promote adaptive immunity more than horse IgG, which could affect its therapeutic uses.

Research Methodology

  • This study had researchers using delicate and precise fluorescence microscopy to examine the interaction between ostrich immunoglobulin (IgY), horse immunoglobulin (IgG), and the F(ab’)₂ fraction of horse IgG with the plasma membranes of lymphocytes and erythrocytes in mice.
  • The immunoglobulins were tagged with fluorescein isothiocyanate (FITC), a fluorescent dye, to allow for their tracking and observation under the microscope.

Findings and Observations

  • The researchers observed that there was an interaction between IgY and the lymphocyte plasma membrane, but this did not lead to endocytosis (the process where cells absorb proteins).
  • In contrast, less IgG and its F(ab’)₂ fraction seemed to bind to the lymphocytes, and this binding was followed by endocytosis, resulting in a widespread cytoplasmic fluorescence in-most lymphocytes exposed to FITC-IgG or FITC-F(ab’)₂.
  • The study found no similar cytoplasmic fluorescence in lymphocytes exposed to FITC-IgY, suggesting that endocytosis did not occur with the ostrich immunoglobulin.
  • The team also observed differences in the reactions of erythrocytes (red blood cells) exposed to horse and ostrich immunoglobulins. The erythrocytes became intensely fluorescent for at least five hours when exposed to horse Igs, representing an interaction between the substances. However, the researchers saw no labeling or fluorescence when they exposed the erythrocytes to FITC-IgY.

Implications of the Research

  • The findings suggest that ostrich IgY may stimulate adaptive immunity more than horse IgG in mammals, which could have important implications for therapeutic applications.
  • The fact that adaptive immunity against IgY could be harmful poses a challenge for its intravenous therapeutic use in humans and other mammals. The body’s immune response might react negatively to IgY, reducing its effectiveness as a therapeutic agent.

Cite This Article

APA
Sevcik C, D'Suze G, Salazar V, Díaz P, Vázquez H. (2012). Horse IgG- and ostrich IgY-F(ab’)₂ groups have different affinities for mice erythrocytes and lymphocytes. Implications for avian immunoglobulin therapeutic usefulness. Toxicon, 60(6), 1215-1221. https://doi.org/10.1016/j.toxicon.2012.07.015

Publication

ISSN: 1879-3150
NlmUniqueID: 1307333
Country: England
Language: English
Volume: 60
Issue: 6
Pages: 1215-1221
PII: S0041-0101(12)00560-0

Researcher Affiliations

Sevcik, Carlos
  • Laboratory on Cellular Neuropharmacology, Centro de Biofísica y Bioquímica, Instituto Venezolano de Investigaciones Científicas-IVIC, Apartado 20632, Caracas 1020A, Venezuela. csevcik@ivic.gob.ve
D'Suze, Gina
    Salazar, Víctor
      Díaz, Patricia
        Vázquez, Hilda

          MeSH Terms

          • Animals
          • Antibody Affinity
          • Cell Membrane / drug effects
          • Erythrocytes / immunology
          • Fluorescein-5-isothiocyanate / chemistry
          • Horses
          • Immunoglobulin Fab Fragments / immunology
          • Immunoglobulin G / immunology
          • Immunoglobulins / immunology
          • Lymphocytes / immunology
          • Male
          • Mice
          • Mice, Inbred BALB C
          • Microscopy, Fluorescence
          • Struthioniformes

          Citations

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