Conformationally Restricted Peptides from Rice Proteins Elicit Antibodies That Recognize the Corresponding Native Protein in ELISA Assays
The rice hoja blanca virus (RHBV), transmitted by the planthopper insect Tagosodes orizicolus, is a disease that attacks rice and generates significant production losses in Colombia. Fedearroz 2000 and Colombia I commercial rice varieties, which have different resistance levels to the disease, were...
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MDPI AG
2018-09-01
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author | Nubia F. Barrera Luz M. Melgarejo Maribel Cruz-Gallego Lina Jimena Cortés Fanny Guzmán Julio C. Calvo |
author_facet | Nubia F. Barrera Luz M. Melgarejo Maribel Cruz-Gallego Lina Jimena Cortés Fanny Guzmán Julio C. Calvo |
author_sort | Nubia F. Barrera |
collection | DOAJ |
description | The rice hoja blanca virus (RHBV), transmitted by the planthopper insect Tagosodes orizicolus, is a disease that attacks rice and generates significant production losses in Colombia. Fedearroz 2000 and Colombia I commercial rice varieties, which have different resistance levels to the disease, were selected in this study. To identify proteins associated to the insect and virus signaling, a comparative proteomics study was performed. By comparing proteomic profiles, between virus-infected and control group plants in two-dimensional electrophoresis, proteins exhibiting significant changes in abundance were found. In another test, peptide dendrimers containing sequences conformationally restricted to α-helix from four of those rice proteins were synthesized. In the experiment, sera from mice inoculated with peptide dendrimers could recognize the corresponding native protein in ELISA assays. Reported comparative proteomic results provide new insights into the molecular mechanisms of plant response to the RHBV and comprehensive tools for the analysis of new crop varieties. Besides, results from conformational peptide dendrimer approach are promising and show that it is feasible to detect proteins as markers, and may have biological applications by decreasing the susceptibility to proteolytic degradation. |
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language | English |
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spelling | doaj.art-87f801ddf06946318c67a979800592d32022-12-22T02:27:34ZengMDPI AGMolecules1420-30492018-09-01239226210.3390/molecules23092262molecules23092262Conformationally Restricted Peptides from Rice Proteins Elicit Antibodies That Recognize the Corresponding Native Protein in ELISA AssaysNubia F. Barrera0Luz M. Melgarejo1Maribel Cruz-Gallego2Lina Jimena Cortés3Fanny Guzmán4Julio C. Calvo5Doctorado en Biotecnología, Universidad Nacional de Colombia, Carrera 30 No. 45-03, Edificio 224, Bogotá 110111, ColombiaLaboratorio de Fisiología y Bioquímica Vegetal, Departamento de Biología, Universidad Nacional de Colombia, Carrera 30 No. 45-03, Edificio 421, Bogotá 110111, ColombiaCentro Internacional de Agricultura Tropical, CIAT, Fondo Latinoamericano para Arroz de Riego, FLAR, Palmira, Valle 763537, ColombiaNúcleo de Biotecnología de Curauma, Pontificia Universidad Católica de Valparaíso, Valparaíso 2373223, ChileNúcleo de Biotecnología de Curauma, Pontificia Universidad Católica de Valparaíso, Valparaíso 2373223, ChileGrupo Proteoma UD, Facultad de Ciencias y Educación, Universidad Distrital Francisco José de Caldas, Carrera 4 No. 26B-54, Bogotá 110111, ColombiaThe rice hoja blanca virus (RHBV), transmitted by the planthopper insect Tagosodes orizicolus, is a disease that attacks rice and generates significant production losses in Colombia. Fedearroz 2000 and Colombia I commercial rice varieties, which have different resistance levels to the disease, were selected in this study. To identify proteins associated to the insect and virus signaling, a comparative proteomics study was performed. By comparing proteomic profiles, between virus-infected and control group plants in two-dimensional electrophoresis, proteins exhibiting significant changes in abundance were found. In another test, peptide dendrimers containing sequences conformationally restricted to α-helix from four of those rice proteins were synthesized. In the experiment, sera from mice inoculated with peptide dendrimers could recognize the corresponding native protein in ELISA assays. Reported comparative proteomic results provide new insights into the molecular mechanisms of plant response to the RHBV and comprehensive tools for the analysis of new crop varieties. Besides, results from conformational peptide dendrimer approach are promising and show that it is feasible to detect proteins as markers, and may have biological applications by decreasing the susceptibility to proteolytic degradation.http://www.mdpi.com/1420-3049/23/9/2262plant proteomicsRHBVrice hoja blanca virusColombian rice varietiespeptide dendrimershelix mimetics |
spellingShingle | Nubia F. Barrera Luz M. Melgarejo Maribel Cruz-Gallego Lina Jimena Cortés Fanny Guzmán Julio C. Calvo Conformationally Restricted Peptides from Rice Proteins Elicit Antibodies That Recognize the Corresponding Native Protein in ELISA Assays Molecules plant proteomics RHBV rice hoja blanca virus Colombian rice varieties peptide dendrimers helix mimetics |
title | Conformationally Restricted Peptides from Rice Proteins Elicit Antibodies That Recognize the Corresponding Native Protein in ELISA Assays |
title_full | Conformationally Restricted Peptides from Rice Proteins Elicit Antibodies That Recognize the Corresponding Native Protein in ELISA Assays |
title_fullStr | Conformationally Restricted Peptides from Rice Proteins Elicit Antibodies That Recognize the Corresponding Native Protein in ELISA Assays |
title_full_unstemmed | Conformationally Restricted Peptides from Rice Proteins Elicit Antibodies That Recognize the Corresponding Native Protein in ELISA Assays |
title_short | Conformationally Restricted Peptides from Rice Proteins Elicit Antibodies That Recognize the Corresponding Native Protein in ELISA Assays |
title_sort | conformationally restricted peptides from rice proteins elicit antibodies that recognize the corresponding native protein in elisa assays |
topic | plant proteomics RHBV rice hoja blanca virus Colombian rice varieties peptide dendrimers helix mimetics |
url | http://www.mdpi.com/1420-3049/23/9/2262 |
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