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Differentiation of Mediterranean plum pox virus isolates by coat protein analysis (1994)

LÓPEZ-MOYA, J. J. ; CANTO, T. ; LÓPEZ-ABELLA, D. ; [et al.]

Oxford, UK : Blackwell Publishing Ltd

Plant pathology 43 (1994), S. 0

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ISSN: 1365-3059

Source: Blackwell Publishing Journal Backfiles 1879-2005

Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition

Notes: Six isolates of plum pox potyvirus from different Mediterranean countries were compared by sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE), peptide mapping and Western blotting after improved purification of virions using a protease inhibitor cocktail that reduced coat protein degradation. One isolate (Spanish isolate 3.3 from plum) differed from the others in possessing a smaller coat protein (approximately 34 instead 36 kDa) with a possible deletion in the surface-exposed amino-terminal region. Infectivity of the viruses after proteolysis, assessed using a local lesion host, was significantly reduced. Protease digestion conditions were established to generate a 28 kDa resistant core of the viral coat protein. Such conditions (longer incubation times or an increase in the enzyme concentration) differed from the milder ones reported for other potyviruses. Implications of the results in relation to the production and screening of virus-specific monoclonal antibodies are discussed.

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1111/j.1365-3059.1994.tb00566.x

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Characterisation of genetically modified cucumber mosaic virus expressing histidine-tagged 1a and 2a proteins (2000)

Gal-On, A. ; Canto, T. ; Palukaitis, P.

Springer

Archives of virology 145 (2000), S. 37-50

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ISSN: 1432-8798

Source: Springer Online Journal Archives 1860-2000

Topics: Medicine

Notes: Summary. Biological active cDNA clones of cucumber mosaic virus (CMV) RNAs 1 and 2 were modified by addition of sequences that encode hexahistidine (His-tag) at the amino- (N-) or carboxy- (C-) terminus of the 1a and 2a proteins. These proteins are essential components of the viral RNA-dependent RNA polymerase (RdRp). In all but one case, addition of the His-tag did not significantly affect the yields of the corresponding viruses and the His-tag-encoding sequences were maintained after mechanical passages. No differences were observed among the in vitro activities of the modified vs. wild-type viral RdRps. Subcellular fractionation showed that 2a protein was found both membrane-associated and in the 30,000 × g soluble fraction. Both termini of the native His-tag 2a protein could bind to a resin containing nickel-nitrilotriacetic acid (Ni2+-NTA). Detergent-treated RdRp containing C-terminal His-tagged 1a and 2a proteins was chromatographed on Ni2+-NTA resin. The activity of the eluted RdRp was template- dependent, in contrast to pre-chromatography fractions. However, only a small proportion of the viral RdRp as well as numerous host proteins bound to and eluted from the resin under non-denaturing conditions.