Purification and partial characterization of figaren, an RNase-like novel antiviral protein from Cucumis figarei
An antiviral protein, designated figaren, was purified from leaves of Cucumis figarei and partially characterized. Column chromatography, SDS-polyacrylamide gel electrophoresis and periodic acid-Schiff staining revealed that figaren is a glycoprotein with a molecular weight of 23 kDa. Figaren was st...
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Veröffentlicht in: | Journal of general plant pathology : JGPP 2001-05, Vol.67 (2), p.152-158 |
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Sprache: | eng |
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Zusammenfassung: | An antiviral protein, designated figaren, was purified from leaves of Cucumis figarei and partially characterized. Column chromatography, SDS-polyacrylamide gel electrophoresis and periodic acid-Schiff staining revealed that figaren is a glycoprotein with a molecular weight of 23 kDa. Figaren was stable at pH 2 to 12 and below 90 deg C. N-termmal amino acid sequencing indicated that figaren contained the conserved region for the S-allele-associated ribonucleases (RNases). In-gel RNase assay showed that figaren digested yeast RNAs. Figaren also digested double-stranded RNAs extracted from Cucumber mosaic virus (CMV)-infected tobacco tissues. Fluorescence in situ hybridization revealed that figaren and RNases (beef pancrease and RNase T sub(1) at 1 micro g /ml similarly inhibited CMV infection in cowpea leaves. Figaren and the RNases at 5 - 500 ng /ml had similar inhibitory effect on local lesion formation by CMV. These data suggest that figaren is a novel RNase-like antiviral protein. |
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ISSN: | 1345-2630 1610-739X |
DOI: | 10.1007/pl00013002 |