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1.
Nat Commun ; 9(1): 31, 2018 01 02.
Article in English | MEDLINE | ID: mdl-29295978

ABSTRACT

Bacterial-fungal interactions are widely found in distinct environments and contribute to ecosystem processes. Previous studies of these interactions have mostly been performed in soil, and only limited studies of aerial plant tissues have been conducted. Here we show that a seed-borne plant pathogenic bacterium, Burkholderia glumae (Bg), and an air-borne plant pathogenic fungus, Fusarium graminearum (Fg), interact to promote bacterial survival, bacterial and fungal dispersal, and disease progression on rice plants, despite the production of antifungal toxoflavin by Bg. We perform assays of toxoflavin sensitivity, RNA-seq analyses, lipid staining and measures of triacylglyceride content to show that triacylglycerides containing linolenic acid mediate resistance to reactive oxygen species that are generated in response to toxoflavin in Fg. As a result, Bg is able to physically attach to Fg to achieve rapid and expansive dispersal to enhance disease severity.


Subject(s)
Air Microbiology , Burkholderia/physiology , Fusarium/physiology , Oryza/microbiology , Seeds/microbiology , Burkholderia/metabolism , Drug Resistance, Fungal/drug effects , Fusarium/classification , Fusarium/genetics , Gene Expression Profiling , Gene Expression Regulation, Fungal , Host-Pathogen Interactions , Microbial Interactions , Mutation , Phylogeny , Plant Diseases/microbiology , Pyrimidinones/metabolism , Pyrimidinones/pharmacology , Triazines/metabolism , Triazines/pharmacology
2.
Oncol Lett ; 5(1): 201-207, 2013 Jan.
Article in English | MEDLINE | ID: mdl-23255920

ABSTRACT

Osteosarcoma is the most common primary malignant bone tumor in children and adolescents. Recent studies have shown that extracellular matrix metalloproteinase inducer (EMMPRIN/CD147) promotes adhesion, invasion and metastasis of malignant tumor cells. The aim of this study was to investigate the impact of EMMPRIN/CD147 expression on prognosis and its correlation with clinicopathological characteristics in patients with osteosarcoma. The expression of EMMPRIN/CD147 in 55 surgical specimens from patients with osteosarcoma at stage IIA or above, 15 non-tumor rib bone tissues, three human osteosarcoma cell lines (Saos-2, U-2OS and MG-63), the human osteoblast cell line HOB and the malignant melanoma cell line A375 were examined by immunohistochemistry, western blot analysis and ELISA, respectively. The potential association of the levels of EMMPRIN/CD147 expression in osteosarcoma specimens with the overall survival of patients was statistically analyzed. We found that the EMMPRIN/CD147 was expressed in 45 out of 55 osteosarcomas, with immunoreactivity primarily within the membrane and cytoplasm of tumor cells, but not in the non-tumor bone tissues. We also observed that EMMPRIN/CD147 was expressed in Saos-2, U-2OS, MG-63 and A375, but not in HOB cells. The levels of EMMPRIN/CD147 expression correlated positively with the pathological degree of osteosarcoma and negatively with the survival period of patients with osteosarcoma. The expression of EMMPRIN/CD147 is a potential factor in the development and prognosis of osteosarcoma and may be a novel therapeutic target of human osteosarcoma.

3.
Biotechnol Lett ; 32(7): 943-9, 2010 Jul.
Article in English | MEDLINE | ID: mdl-20213521

ABSTRACT

Random mutagenesis was performed on beta-agarase, AgaB, from Zobellia galactanivorans to improve its catalytic activity and thermostability. The activities of three mutants E99K, T307I and E99K-T307I were approx. 140, 190 and 200%, respectively, of wild type beta-agarase (661 U/mg) at 40 degrees C. All three mutant enzymes were stable up to 50 degrees C and E99K-T307I had the highest thermostability. The melting temperature (Tm) of E99K-T307I, determined by CD spectra, was increased by 5.2 degrees C over that of the wild-type enzyme (54.6 degrees C). Activities of both the wild-type and E99K-T307I enzymes, as well as their overall thermostabilities, increased in 1 mM CaCl2. The E99K-T307I enzyme was stable at 55 degrees C with 1 mM CaCl2, reaching 260% of the activity the wild-type enzyme held at 40 degrees C without CaCl2.


Subject(s)
Bacterial Proteins/chemistry , Flavobacteriaceae/enzymology , Glycoside Hydrolases/chemistry , Hot Temperature , Mutagenesis , Amino Acid Substitution/genetics , Bacterial Proteins/genetics , Calcium Chloride/metabolism , Circular Dichroism , DNA Mutational Analysis , Enzyme Stability , Flavobacteriaceae/genetics , Glycoside Hydrolases/genetics , Mutant Proteins/chemistry , Mutant Proteins/genetics , Mutation, Missense , Protein Stability , Transition Temperature
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