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1. Readthrough protein associated with virions of barley yellow dwarf luteovirus and its potential role in regulating the efficiency of aphid transmission

Author

Stewart M. Gray, F.E. Gildow, C. Chay, and J.Y. Wang

Subjects
Avena, viruses, Luteovirus, Molecular Sequence Data, Transfection, Polymerase Chain Reaction, Virus, Open Reading Frames, Capsid, Virology, HSPA2, Escherichia coli, Animals, Cloning, Molecular, Cells, Cultured, DNA Primers, Plant Diseases, biology, Base Sequence, Protoplasts, fungi, Virion, food and beverages, Hordeum, Protoplast, biology.organism_classification, Stop codon, Recombinant Proteins, Open reading frame, Barley yellow dwarf, Aphids, Protein Biosynthesis, Electrophoresis, Polyacrylamide Gel
Abstract

Purified particles of barley yellow dwarf luteovirus (BYDV) contain a major 22-kDa protein and a minor protein of approximately 58 kDa. The 22-kDa capsid protein is encoded by open reading frame (ORF) 3. ORF 5 is immediately downstream and in frame with ORF 3 and a 72-kDa protein can be translated via a readthrough suppression of the ORF 3 termination codon. Antibodies were produced against two Escherichia coli expressed polypeptides that represent the amino- and carboxyl-terminal halves of a putative 50-kDa protein encoded by ORF 5. Immunological analyses indicated that the 58-kDa protein associated with purified virions contained sequences encoded by ORF 3 and ORF 5. The carboxyl terminal portion of the full-length (72 kDa) readthrough protein was absent from the 58-kDa protein. The full-length readthrough protein was detected in infected oat protoplasts and plant tissue, but was not associated with virus particles purified from plants. The carboxyl-terminal portion of the 72-kDa readthrough protein was not required for aphid transmission; however, virus was transmitted more efficiently from protoplast extracts containing virions and soluble 72-kDa readthrough protein than from mock-inoculated protoplast extracts to which plant purified virus was added. The full-length readthrough protein, although not required for transmission, may increase the transmission efficiency of BYDV by aphids.

Published
1995

2. Readthrough protein associated with virions of barley yellow dwarf luteovirus and its potential role in regulating the efficiency of aphid transmission.

Author

Wang JY, Chay C, Gildow FE, and Gray SM

Subjects
Animals, Avena, Base Sequence, Capsid biosynthesis, Capsid isolation & purification, Cells, Cultured, Cloning, Molecular, DNA Primers, Electrophoresis, Polyacrylamide Gel, Escherichia coli, Luteovirus isolation & purification, Luteovirus pathogenicity, Molecular Sequence Data, Open Reading Frames, Plant Diseases, Polymerase Chain Reaction, Protein Biosynthesis, Protoplasts, Recombinant Proteins biosynthesis, Recombinant Proteins isolation & purification, Recombinant Proteins metabolism, Transfection, Virion isolation & purification, Virion pathogenicity, Aphids virology, Capsid metabolism, Hordeum virology, Luteovirus physiology, Virion physiology
Abstract

Purified particles of barley yellow dwarf luteovirus (BYDV) contain a major 22-kDa protein and a minor protein of approximately 58 kDa. The 22-kDa capsid protein is encoded by open reading frame (ORF) 3. ORF 5 is immediately downstream and in frame with ORF 3 and a 72-kDa protein can be translated via a readthrough suppression of the ORF 3 termination codon. Antibodies were produced against two Escherichia coli expressed polypeptides that represent the amino- and carboxyl-terminal halves of a putative 50-kDa protein encoded by ORF 5. Immunological analyses indicated that the 58-kDa protein associated with purified virions contained sequences encoded by ORF 3 and ORF 5. The carboxyl terminal portion of the full-length (72 kDa) readthrough protein was absent from the 58-kDa protein. The full-length readthrough protein was detected in infected oat protoplasts and plant tissue, but was not associated with virus particles purified from plants. The carboxyl-terminal portion of the 72-kDa readthrough protein was not required for aphid transmission; however, virus was transmitted more efficiently from protoplast extracts containing virions and soluble 72-kDa readthrough protein than from mock-inoculated protoplast extracts to which plant purified virus was added. The full-length readthrough protein, although not required for transmission, may increase the transmission efficiency of BYDV by aphids.

Published
1995
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