Identification of Biomarkers for Resistance to Fusarium oxysporum f. sp. cubense Infection and in Silico Studies in Musa paradisiaca Cultivar Puttabale through Proteomic Approach

Autor:	Anup Chandra Pal, Venkatesh Ramu, Kukkundoor Ramachandra Kini, Pradeepa Krishnappa, Nagaraja Deeplanaik, Santosh Kumar Shimoga Rajanna, Krishna Venkatarangaiah
Rok vydání:	2016
Předmět:	panama wilt 0301 basic medicine Musa paradisiaca cv. puttabale two dimensional gel electrophoresis Clinical Biochemistry lcsh:QR1-502 Musa × paradisiaca Plant disease resistance protein-protein docking PR proteins Biochemistry lcsh:Microbiology Article 03 medical and health sciences Structural Biology Botany Fusarium oxysporum Molecular Biology Gel electrophoresis Fungal protein biology Binding protein Fusarium oxysporum f.sp. cubense biology.organism_classification 030104 developmental biology Docking (molecular)
Zdroj:	Proteomes Proteomes; Volume 4; Issue 1; Pages: 9 Proteomes, Vol 4, Iss 1, p 9 (2016)
ISSN:	2227-7382
DOI:	10.3390/proteomes4010009
Popis:	Panama wilt caused by Fusarium oxysporum f. sp. cubense (Foc) is one of the major disease constraints of banana production. Previously, we reported the disease resistance Musa paradisiaca cv. puttabale clones developed from Ethylmethanesulfonate and Foc culture filtrate against Foc inoculation. Here, the same resistant clones and susceptible clones were used for the study of protein accumulation against Foc inoculation by two-dimensional gel electrophoresis (2-DE), their expression pattern and an in silico approach. The present investigation revealed mass-spectrometry identified 16 proteins that were over accumulated and 5 proteins that were under accumulated as compared to the control. The polyphosphoinositide binding protein ssh2p (PBPssh2p) and Indoleacetic acid-induced-like (IAA) protein showed significant up-regulation and down-regulation. The docking of the pathogenesis-related protein (PR) with the fungal protein endopolygalacturonase (PG) exemplify the three ionic interactions and seven hydrophobic residues that tends to good interaction at the active site of PG with free energy of assembly dissociation (1.5 kcal/mol). The protein-ligand docking of the Peptide methionine sulfoxide reductase chloroplastic-like protein (PMSRc) with the ligand β-1,3 glucan showed minimum binding energy (−6.48 kcal/mol) and docking energy (−8.2 kcal/mol) with an interaction of nine amino-acid residues. These explorations accelerate the research in designing the host pathogen interaction studies for the better management of diseases.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_dedup___::94733a223d56093534b7271e9264655a https://doi.org/10.3390/proteomes4010009 Zobrazit plný text záznamu Plný text ve formátu PDF Plný text ve formátu HTML
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