Proteomics-Based Analysis of Phalaenopsis amabilis in Response toward Cymbidium Mosaic Virus and/or Odontoglossum Ringspot Virus Infection

Copyright © 2013 Tongfei Lai et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. Stress response at the protein level to viral infection in orchid plants has not been extensively investigated to date. To understand the proteomic basis of Phalaenopsis amabilis’s responses to Cymbidium Mosaic virus (CymMV), and/or Odontoglossum ring spot virus (ORSV), the total proteins were extracted from Phalaenopsis amabilis leaves infected with CymMV, ORSV, or both respectively. Differentially expressed proteins were identified by two-dimensional elec-trophoresis, and 27 of these proteins that had significant changes were further examined by mass spectrometry. Com-paring CymMV-infected leaves with mock-inoculated ones, 2 proteins were significantly up-regulated, 9 were signifi-cantly down-regulated and 1 previously undetected protein was identified. 10 proteins were significantly up-regulated, 3 significantly down-regulated and 1 previously undetected protein was identified in ORSV-infected leaves. 6 proteins were significantly up-regulated and 9 significantly down-regulated proteins were found in co-infected leaves. These identified proteins are involved in disease resistance, stress response, transcriptional regulation, energy metabolism, protein modification and the previously unknown proteins were not involved with known protein pathways. Proteins significantly up-regulated were ATP sulfurylase, down-regulated proteins included glutamate decarboxylase isozyme 2