Physicochemical properties of bean rugose mosaic virus
Material type:![Article](/opac-tmpl/lib/famfamfam/AR.png)
- Phaseolus vulgaris
- Cultivars
- Resistance
- BEAN RUGOSE MOSAIC VIRUS
- DISEASE PHYSIOLOGY AND BIOCHEMISTRY
- Costa Rica
- Central America
- DISEASES AND PATHOGENS
- Pests
- Viroses
- Phaseolus vulgaris
- Cultivares
- Resistencia
- VIRUS DEL MOSAICO RUGOSO DEL FRIJOL
- FISIOLOGIA Y BIOQUIMICA DE LA ENFERMEDAD
- Costa Rica
- Journal articles
- Artículos en revistas
- Frijol
- Beans
- Electronic documents
- Documentos electrónicos
- Journal article
- 31809
Item type | Current library | Collection | Call number | Copy number | Status | Date due | Barcode | Item holds | |
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CIAT Library Web | Electronic Document | 31809 (Browse shelf(Opens below)) | Not For Loan (Restricted Access) | |||||
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CIAT Library Document collection CINFOS | Document Collection CINFOS | 31809 (Browse shelf(Opens below)) | c.1 | Short Loan | 100046790 |
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Los cv. de frijol susceptibles infectados con BRMV producen 3 componentes de sedimentacion en gradientes isopicnico y zonal. El componente superior contiene conchas vacias; los componentes medio e inferior, necesarios para la infeccion, contienen moleculas diferenciadas de ARN de p.mol. 1.4 y 2.1x10(6), resp. Un polipeptido grande (41 K) y 2 pequenos (21 y 23 K) se hallan en todos los componentes. Al parecer el polipeptido 21 K se deriva por division proteolitica del polipeptido 23 K. Cada ARN contiene un peptido (VPg) unido por genoma en el extremo 5' y una cola poli-A en el extremo 3' de la molecula. Todas estas propiedades apoyan claramente la inclusion del BRMV en el grupo de los comovirus, como se propuso anteriormente con base en la immunoreactividad. (RA- CIAT) spa
Susceptible bean cv. infected with BRMV yield 3 sedimentation components in isopycnic and zonal gradients. The top component contains empty shells; the middle and bottom components, both required for infection, contain distinct RNA molecules of mol. wt. 1.4 and 2.1x10(6), resp. One large (41 K) and 2 small polypeptides (21 and 23 K) are found in all components. The 21 K polypeptide appears to be derived by proteolytic cleavage from the 23 K polypeptide. In addition, each RNA contains a genome-bound peptide (VPg) on the 5' end and a poly-A tail on the 3' end of the molecule. All of these properties clearly support the inclusion of BRMV in the comovirus group, as previously proposed on the basis of immunoreactivity. (AS) eng