• Castellano
  • English
  • Valenciá
Página de inicio de ReDivia
Página de la Generalitat ValenciáPágina de IVIA
View Item 
  •   ReDivia Home
  • 1.- Investigación
  • 1.1.- Artículos de revista académica
  • View Item
  •   ReDivia Home
  • 1.- Investigación
  • 1.1.- Artículos de revista académica
  • View Item
JavaScript is disabled for your browser. Some features of this site may not work without it.

Mutagenic Analysis and Localization of a Highly Conserved Epitope Near the Amino-Terminal End of the Citrus Tristeza Closterovirus Capsid Protein

Export
untranslatedRefworks
URI
http://hdl.handle.net/20.500.11939/4316
DOI
10.1094/Phyto-85-1311
Derechos de acceso
openAccess
Metadata
Show full item record
Author
Pappu, H. R.; Pappu, S. S.; Kano, T.; Koizumi, M.; Cambra, Mariano; Moreno, Pedro; Su, H. J.; Garnsey, Stephen M.; Lee, R. F.; Niblett, C. L.
Date
1995
Cita bibliográfica
Pappu, H. R., Pappu, S. S., Kano, T., Koizumi, M., Cambra, M., Moreno, P., Su, H. J., Garnsey, S. M., Lee, R. F., Niblett, C. L. (1995). Mutagenic Analysis and Localization of a Highly Conserved Epitope Near the Amino-Terminal End of the Citrus Tristeza Closterovirus Capsid Protein. Phytopathology, 85(10), 1311-1315.
Abstract
The monoclonal antibody (MAb) 3DF1 is the first commercially available citrus tristeza closterovirus (CTV)-specific MAb. It detects a broad spectrum of CTV isolates from various parts of the world. To precisely map the antigenic determinant recognized by 3DF1, the capsid protein (CP) genes of four 3DF1-nonreactive isolates were cloned as complementary DNA and their nucleotide sequences determined. Comparison of the deduced CP sequences of the four nonreactive isolates with those of previously sequenced 3DF1-reactive isolates revealed differences at three positions near their amino terminal ends. The amino acids Asp-2, Lys-13, and Phe-28 were conserved in all the 3DF1-reactive isolates, but they were replaced by Gly, Thr/Asp, and Tyr, respectively, in the CPs of the nonreactive isolates. Site-specific mutations were introduced into the cloned CP genes of the 3DF1-nonreactive isolate B215 and the 3DF1-reactive isolate T36. The serological reactivities of the wild-type and mutant CPs of B215 and T36 expressed as recombinant fusion proteins in Escherichia coli were evaluated by Western blot analysis. A point mutation (A-->G) resulting in an Asp-->Gly change at amino acid position 2 of the CP of isolate T36 abolished the reactivity with the MAb, whereas a reverse mutation resulting in a Gly-->Asp change at the same position conferred reactivity on the CP of the nonreactive B215 isolate. The implications of the observed antigenic diversity on virus detection are discussed.
Collections
  • 1.1.- Artículos de revista académica

Browse

All of ReDiviaCommunities & CollectionsBy Issue DateAuthorsTitlesSubjetcsCategoriesIVIA CentersThis CollectionBy Issue DateAuthorsTitlesSubjetcsCategoriesIVIA Centers

My Account

LoginRegister

Statistics

View Usage Statistics

Of interest

IVIA Open Access PolicyIntellectual property and copyrightAutoarchiveFrequently Asked Questions

Indexers

Recolectauntranslated

El contenido de este sitio está bajo una licencia Creative Commons - No comercial - Sin Obra Derivada (by-nc-nd), salvo que se indique lo contrario.