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| Authors: | V. Pallás, J.A. Sánchez-Navarro, J. Díez, J.C. Desvignes, A. Rowhani, M.A. Sánchez-Pina |
| Keywords: | Apple mosaic ilavirus, characterization, translation |
Abstract:
Genome coat protein and nucleoproteins of apple mosaic virus (ApMV) were characterized by using different electrophoretic systems.
Glyoxal-treated ApMV RNAs revealed a size of 3544 bases (b), 2493 b, 1753, b and 877 b for RNAs 1 to 4 respectively.
Coat protein migrated as a prominent band with a relative mass (Mr) of 28,800 in SDS-PAGE.
In vitro translation of the viral RNAs yield four major products of approximately the expected sizes.
Immunoprecipitation of the translation products with ApMV antiserum showed that a band with a Mr of 28,000 was the corresponding one to the coat protein.
Comparative sequence analysis of the ApMV RNA 4 and protein with those of other tripartite viruses revealed that, at the protein level, ApMV most closely resembles tobacco streak virus (TSV, 51% of similarity) whereas at the nucleic acid level no significant percentage of similarity was found except for 5' and 3' terminal sequences of alfalfa mosaic virus (AIMV) in which the sequence analysis showed 80% of identity.
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