Spiralin: Major membrane protein specific for subgroup I-1 Spiroplasmas |
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Authors: | Robert F Whitcomb Joseph G Tully Henri Wróblewski |
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Institution: | 1. Insect Pathology Laboratory, Plant Protection Institute, Agricultural Research Service, U.S. Department of Agriculture, 20705, Beltsville, Maryland, USA 2. Mycoplasma Section, Laboratory of Molecular Microbiology, National Institute of Allergy and Infectious Disease, Frederick Cancer Research Center, Building 550, 21701, Frederick, Maryland, USA 3. Laboratoire de Biologie Cellulaire, Université de Rennes, Complexe de Beaulieu, Avenue du Général Leclerc, F-35042, Rennes Cédex, France
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Abstract: | Preparations of spiralin from membranes ofSpiroplasma citri, strain C189, purified by sequential solubilization with detergents followed by agarose-suspension electrophoresis induced rabbit antibodies that were largely specific forSpiroplasma citri Group I-1 spiroplasmas, as demonstrated by metabolic inhibition (MI), growth inhibition (GI), and deformation (DF) tests. By contrast, antibodies againstS. citri whole-membrane protein preparations reacted broadly with representative type cultures of seven subgroups of theS. citri complex. Neither antimembrane nor antispiralin sera reacted withS. floricola, S. mirum, or Group IV, (VI), (VII), or (VIII) spiroplasmas. Minor cross-reactions in MI and DF tests between antispiralin serum and Subgroup I-2 and I-3 antigens may have represented shared epitopes in a set of homologous membrane proteins of the three spiroplasmas, or antibodies against highly antigenic traces of other common membrane proteins in the purified spiralin preparations. The unique antigenic properties of spiralin, the most abundant protein in theS. citri membrane, explain in part the unique profiles shown by this spiroplasma species in comparative taxonomic serological tests. |
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