PURIFICATION OF SURFACE-EXPOSED INTEGRAL OUTER-MEMBRANE PROTEINS OF ACTINOBACILLUS-PLEUROPNEUMONIAE AND THEIR ROLE IN OPSONOPHAGOCYTOSIS

Citation
Rn. Thwaits et S. Kadis, PURIFICATION OF SURFACE-EXPOSED INTEGRAL OUTER-MEMBRANE PROTEINS OF ACTINOBACILLUS-PLEUROPNEUMONIAE AND THEIR ROLE IN OPSONOPHAGOCYTOSIS, American journal of veterinary research, 54(9), 1993, pp. 1462-1470
Citations number
25
Categorie Soggetti
Veterinary Sciences
ISSN journal
00029645
Volume
54
Issue
9
Year of publication
1993
Pages
1462 - 1470
Database
ISI
SICI code
0002-9645(1993)54:9<1462:POSIOP>2.0.ZU;2-V
Abstract
Previously identified 39-, 50-, and 76-kd integral outer membrane prot eins (IOMP) of Actinobacillus pleuropneumoniae, a respiratory tract pa thogen, were separated by electroelution of sodium dodecyl sulfate-pol yacrylamide gel electrophoresis-obtained fragments and their role in o psonophagocytosis by porcine leukocytes was investigated by flow cytom etry of fluorescein-labeled A pleuropneumoniae. Using specific antiser a, immunoblot analysis indicated that the 3 proteins were antigenicall y distinct. Antibodies against each iomp have an important role as ops onins for phagocytosis by porcine leukocytes. The effect of using a co mbination of all 3 of the specific antisera was minimal. Antiserum abs orbed against intact A pleuropneumoniae and Escherichia coli organisms indicated that the antibodies to the 39-, 50-, and 76-kd IOMP were sp ecific for A pleuropneumoniae antigens. Nonheat-treated antiserum did not increase phagocytosis, compared with heat-inactivated antiserum, i ndicating that complement may not have a major role in opsonization of A pleuropneumoniae.