scholarly journals Culture Filtrates of Trichoderma Isolate H921 Inhibit <i>Magnaporthe oryzae</i> Spore Germination and Blast Lesion Formation in Rice

2016 ◽  
Vol 06 (07) ◽  
pp. 521-527 ◽  
Author(s):  
Quyet Thi Nguyen ◽  
Kana Ueda ◽  
Junichi Kihara ◽  
Makoto Ueno
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.


1991 ◽  
Vol 69 (2) ◽  
pp. 306-310 ◽  
Author(s):  
Yves Tirilly

Fulvia fulva, the agent of leaf mould, is known to be a major parasite of tomato leaves in greenhouses. Its development is characterized by a biotrophic phase followed by a necrotrophic phase. Hansfordia pulvinata is a hyperparasite of this pathogen, but its destructive action is restricted by its inability to colonize F. fulva during the biotrophic phase, before lesion formation. An integrated system to optimize the mycoparasitic activity of H. pulvinata was studied. The hyperparasite was tolerant to fosetyl-Al in situ. At a minimal concentration of 500 mg/L, the fungicide inhibited F. fulva spore germination after spraying on tomato leaves but did not have any effect during the necrotrophic phase. Thus, fosetyl-Al, which prevented reinfection, and the destructive hyperparasite H. pulvinata had complementary effects. Key words: Hansfordia pulvinata, fosetyl-Al, Fulvia fulva, integrated control, leaf mould, tomato.


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

2011 ◽  
Vol 58 (2) ◽  
pp. 139-148 ◽  
Author(s):  
Qili Li ◽  
Yinhui Jiang ◽  
Ping Ning ◽  
Lu Zheng ◽  
Junbin Huang ◽  
...  

1974 ◽  
Vol 4 (2) ◽  
pp. 207-212 ◽  
Author(s):  
J. T. Kliejunas ◽  
J. E. Kuntz

Many species of microorganisms were associated with Eutypellaparasitica in cankers on maple. The same species of microorganisms were present in noninoculated artificial branch and trunk wounds on maple trees and in natural wounds on sugar maple and red maple seedlings. There was little antagonistic effect of the associated microorganisms on growth of E. parasitica when paired in culture. Filtrates containing extracts of sugar maple outer bark saprophytes had no effect on spore germination or mycelial growth of E. parasitica. Isolations from branch stubs associated with natural cankers and from tissues in the trunk indicated that E. parasitica invaded tissues colonized first by other microorganisms.


1989 ◽  
Vol 67 (3) ◽  
pp. 922-927 ◽  
Author(s):  
R. B. Gardiner ◽  
W. E. McKeen ◽  
T. M. Lawrence ◽  
R. J. Smith ◽  
A. W. Day

Lesion formation by spores of Botrytis cinerea on Vicia faba occurred within 15 h after inoculation. However, simultaneous application of various antisera delayed lesion formation until up to 65 h after inoculation. As the dilution of antiserum was increased, the length of the inhibitory period decreased and the fraction of the leaf surface that eventually became covered in lesions increased. Antisera of different antigen-binding specificity or different class of heavy chain (IgA, IgG, IgM) inhibited lesion formation, though IgM was the most effective. Antisera purified of other serum proteins were effective, but serum proteins such as albumins were not effective in causing inhibition of lesion formation. F(ab′)2 fragments of IgG molecules were as effective as the complete IgG molecule while Fc and light chain fragments were ineffective. Germination of B. cinerea spores on glass slides was inhibited by the same range of immunoglobulin molecules and fragments. We conclude that some constant portion of the antigen binding region of immunoglobulins inhibits lesion formation by inhibiting spore germination.


1969 ◽  
Vol 53 (2) ◽  
pp. 140-146
Author(s):  
R. Alconero ◽  
Alma G. Santiago

Filtrates of Fusarium oxysporum f. sp. vanillae (Tucker) Gordon, Schlecht. and two isolates of F. solani (Mart.) Appel & Wr., grown in nutrient and potato dextrose broth, effected spore germination, linear growth in agar, and colony development in soil plates of these and other fungi. There was not enough sign of selectivity in these filtrates to warrant their use for selective isolation of fungi from soil.


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.


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