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Purification and Partial Characterization of Rice Transitory Yellowing Virus. Ren -Jong Chiu, Professor, Agricultural Biotechnology Laboratories, National Chung Hsing University, Taichung 40227, Taiwan; Yau-Heiu Hsu(2), Moh-Jih Chen(3), Ching-Chung Chen(4), R. Cheng-Reu Lee(5), Mei-Chao Lin(6), Shu-Mei Lin(7), and Tsong-Teh Kuo(8). (2)(7)Professors and research assistant, Agricultural Biotechnology Laboratories, National Chung Hsing University, Taichung 40227, Taiwan; (3)Professor, Department of Plant Pathology, National Chung Hsing University, Taichung 40227, Taiwan; (4)Taichung District Agricultural Improvement Station, Changhua 51501, Taiwan; (5)(6)(8)Research assistants and research fellow, Institute of Botany, Academia Sinica, Nankang, Taipei 11529, Republic of China. Phytopathology 80:777-783. Accepted for publication 8 February 1990. Copyright 1990 The American Phytopathological Society. DOI: 10.1094/Phyto-80-777.

Rice transitory yellowing virus (RTYV) was purified by procedures that included steps of density gradient centrifugation in 30% Percoll and subsequent fractionation on Sepharose CL-4B column for removal of Percoll particles. Electrophoresis of sodium dodecyl sulfate-disrupted virus in polyacrylamide gels yielded three major proteins of 90K, 63K, and 32K daltons and two minor proteins of 200K and 43K daltons. These represent the virion proteins L, G, N, NS, and M, respectively, in decreasing order of their molecular weights. Antisera prepared to RTYV and potato yellow dwarf virus were tested by enzyme-linked immunosorbent assay and by immunoblotting with homologous as well as heterologous antigens. There was no serological relationship between the two plant rhabdoviruses. When examined in the electron microscope by negative staining, unfixed particles of purified RTYV were bullet shaped, measuring 124 ? 93 nm. These estimates are consistent with previous size measurements for particles in dip preparations.