Purification of surface-exposed integral outer membrane proteins of Actinobacillus pleuropneumoniae and their role in opsonophagocytosis

Richard N. Thwaits From the Department of Animal Science (Thwaits), College of Biology and Agriculture, Brigham Young University, Provo, UT 84602, and the Department of Medical Microbiology, College of Veterinary Medicine, University of Georgia, Athens, GA 30602 (Kadis). Dr. Kadis is currently retired.

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Soloman Kadis From the Department of Animal Science (Thwaits), College of Biology and Agriculture, Brigham Young University, Provo, UT 84602, and the Department of Medical Microbiology, College of Veterinary Medicine, University of Georgia, Athens, GA 30602 (Kadis). Dr. Kadis is currently retired.

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Summary

Previously identified 39-, 50-, and 76-kd integral outer membrane proteins (iomp) of Actinobacillus pleuropneumoniae, a respiratory tract pathogen, were separated by electroelution of sodium dodecyl sulfate-polyacrylamide gel electrophoresis-obtained fragments and their role in opsonophagocytosis by porcine leukocytes was investigated by flow cytometry of fluorescein-labeled A pleuropneumoniae. Using specific antisera, immunoblot analysis indicated that the 3 proteins were antigenically distinct. Antibodies against each iomp have an important role as opsonins for phagocytosis by porcine leukocytes. The effect of using a combination of all 3 of the specific antisera was minimal. Antiserum absorbed against intact A pleuropneumoniae and Escherichia coli organisms indicated that the antibodies to the 39-, 50-, and 76-kd iomp were specific for A pleuropneumoniae antigens. Nonheat-treated antiserum did not increase phagocytosis, compared with heat-inactivated antiserum, indicating that complement may not have a major role in opsonization of A pleuropneumoniae.

Summary

Previously identified 39-, 50-, and 76-kd integral outer membrane proteins (iomp) of Actinobacillus pleuropneumoniae, a respiratory tract pathogen, were separated by electroelution of sodium dodecyl sulfate-polyacrylamide gel electrophoresis-obtained fragments and their role in opsonophagocytosis by porcine leukocytes was investigated by flow cytometry of fluorescein-labeled A pleuropneumoniae. Using specific antisera, immunoblot analysis indicated that the 3 proteins were antigenically distinct. Antibodies against each iomp have an important role as opsonins for phagocytosis by porcine leukocytes. The effect of using a combination of all 3 of the specific antisera was minimal. Antiserum absorbed against intact A pleuropneumoniae and Escherichia coli organisms indicated that the antibodies to the 39-, 50-, and 76-kd iomp were specific for A pleuropneumoniae antigens. Nonheat-treated antiserum did not increase phagocytosis, compared with heat-inactivated antiserum, indicating that complement may not have a major role in opsonization of A pleuropneumoniae.

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