| Literature DB >> 29802510 |
Esau Megias1, Lílian Silveira Travassos do Carmo1, Cícero Nicolini2, Luciano Paulino Silva1, Rosana Blawid3, Tatsuya Nagata3, Angela Mehta4.
Abstract
Tymovirus is a genus of plant pathogenic viruses that infects several dicotyledonous plants worldwide, causing serious diseases in economically important crops. The known cytopathic effect on the host cell organelles involves chloroplast membrane deformation and the induction of vesicles in its periphery. These vesicles are known to be the location where tymoviral genomic RNA replication occurs. Tomato blistering mosaic virus (ToBMV) is a tymovirus recently identified in tomato plants in Brazil, which is able to infect several other plants, including tobacco. In this work, we investigated the chloroplast proteomic profile of ToBMV-infected N. benthamiana using bidimensional electrophoresis (2-DE) and mass spectrometry, aiming to study the virus-host interaction related to the virus replication and infection. A total of approximately 200 spots were resolved, out of which 36 were differentially abundant. Differential spots were identified by mass spectrometry including photosynthesis-related and defense proteins. We identified proteins that may be targets of a direct interaction with viral proteins, such as ATP synthase β subunit, RNA polymerase beta-subunit, 50S ribosomal protein L6 and Trigger factor-like protein. The identification of these candidate proteins gives support for future protein-protein interaction studies to confirm their roles in virus replication and disease development.Entities:
Keywords: 2-DE; Mass spectrometry; Plant proteomics; Plant-virus interaction; ToBMV
Mesh:
Substances:
Year: 2018 PMID: 29802510 DOI: 10.1007/s10930-018-9775-9
Source DB: PubMed Journal: Protein J ISSN: 1572-3887 Impact factor: 2.371