Suppression of Magnaporthe oryzae by culture filtrates of Streptomyces globisporus JK-1

2011 ◽  
Vol 58 (2) ◽  
pp. 139-148 ◽  
Author(s):  
Qili Li ◽  
Yinhui Jiang ◽  
Ping Ning ◽  
Lu Zheng ◽  
Junbin Huang ◽  
...  
2014 ◽  
Vol 10 ◽  
pp. 251-258 ◽  
Author(s):  
Louis P Sandjo ◽  
Eckhard Thines ◽  
Till Opatz ◽  
Anja Schüffler

Four new polyketides have been identified in culture filtrates of the fungal strain Penicillium sp. IBWF104-06 isolated from a soil sample. They are structurally based on the same trans-decalinpentanoic acid skeleton as tanzawaic acids A–H. One of the new compounds was found to inhibit the conidial germination in the rice blast fungus Magnaporthe oryzae at concentrations of 25 μg/mL.


2015 ◽  
Vol 05 (10) ◽  
pp. 686-692 ◽  
Author(s):  
Quyet Nguyen Thi ◽  
Kana Ueda ◽  
Junichi Kihara ◽  
Makoto Ueno

2017 ◽  
Vol 83 (2) ◽  
pp. 109-112 ◽  
Author(s):  
Quyet Thi Nguyen ◽  
Kana Ueda ◽  
Tomoko Tamura ◽  
Junichi Kihara ◽  
Makoto Ueno

2019 ◽  
Vol 476 (21) ◽  
pp. 3227-3240 ◽  
Author(s):  
Shanshan Wang ◽  
Yanxiang Zhao ◽  
Long Yi ◽  
Minghe Shen ◽  
Chao Wang ◽  
...  

Trehalose-6-phosphate (T6P) synthase (Tps1) catalyzes the formation of T6P from UDP-glucose (UDPG) (or GDPG, etc.) and glucose-6-phosphate (G6P), and structural basis of this process has not been well studied. MoTps1 (Magnaporthe oryzae Tps1) plays a critical role in carbon and nitrogen metabolism, but its structural information is unknown. Here we present the crystal structures of MoTps1 apo, binary (with UDPG) and ternary (with UDPG/G6P or UDP/T6P) complexes. MoTps1 consists of two modified Rossmann-fold domains and a catalytic center in-between. Unlike Escherichia coli OtsA (EcOtsA, the Tps1 of E. coli), MoTps1 exists as a mixture of monomer, dimer, and oligomer in solution. Inter-chain salt bridges, which are not fully conserved in EcOtsA, play primary roles in MoTps1 oligomerization. Binding of UDPG by MoTps1 C-terminal domain modifies the substrate pocket of MoTps1. In the MoTps1 ternary complex structure, UDP and T6P, the products of UDPG and G6P, are detected, and substantial conformational rearrangements of N-terminal domain, including structural reshuffling (β3–β4 loop to α0 helix) and movement of a ‘shift region' towards the catalytic centre, are observed. These conformational changes render MoTps1 to a ‘closed' state compared with its ‘open' state in apo or UDPG complex structures. By solving the EcOtsA apo structure, we confirmed that similar ligand binding induced conformational changes also exist in EcOtsA, although no structural reshuffling involved. Based on our research and previous studies, we present a model for the catalytic process of Tps1. Our research provides novel information on MoTps1, Tps1 family, and structure-based antifungal drug design.


2013 ◽  
Vol 38 (12) ◽  
pp. 2192-2197 ◽  
Author(s):  
Xiang-Xiao LI ◽  
Qian WANG ◽  
Sheng-Xiang LUO ◽  
Yun-Xia HE ◽  
Ling-Hua ZHU ◽  
...  

2021 ◽  
pp. 103562
Author(s):  
Alice Bisola Eseola ◽  
Lauren S. Ryder ◽  
Míriam Osés-Ruiz ◽  
Kim Findlay ◽  
Xia Yan ◽  
...  

Genes ◽  
2021 ◽  
Vol 12 (2) ◽  
pp. 301
Author(s):  
Vishesh Kumar ◽  
Priyanka Jain ◽  
Sureshkumar Venkadesan ◽  
Suhas Gorakh Karkute ◽  
Jyotika Bhati ◽  
...  

Rice blast is a global threat to food security with up to 50% yield losses. Panicle blast is a more severe form of rice blast and the response of rice plant to leaf and panicle blast is distinct in different genotypes. To understand the specific response of rice in panicle blast, transcriptome analysis of blast resistant cultivar Tetep, and susceptible cultivar HP2216 was carried out using RNA-Seq approach after 48, 72 and 96 h of infection with Magnaporthe oryzae along with mock inoculation. Transcriptome data analysis of infected panicle tissues revealed that 3553 genes differentially expressed in HP2216 and 2491 genes in Tetep, which must be the responsible factor behind the differential disease response. The defense responsive genes are involved mainly in defense pathways namely, hormonal regulation, synthesis of reactive oxygen species, secondary metabolites and cell wall modification. The common differentially expressed genes in both the cultivars were defense responsive transcription factors, NBS-LRR genes, kinases, pathogenesis related genes and peroxidases. In Tetep, cell wall strengthening pathway represented by PMR5, dirigent, tubulin, cell wall proteins, chitinases, and proteases was found to be specifically enriched. Additionally, many novel genes having DOMON, VWF, and PCaP1 domains which are specific to cell membrane were highly expressed only in Tetep post infection, suggesting their role in panicle blast resistance. Thus, our study shows that panicle blast resistance is a complex phenomenon contributed by early defense response through ROS production and detoxification, MAPK and LRR signaling, accumulation of antimicrobial compounds and secondary metabolites, and cell wall strengthening to prevent the entry and spread of the fungi. The present investigation provided valuable candidate genes that can unravel the mechanisms of panicle blast resistance and help in the rice blast breeding program.


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