TMC-69, a new antitumor antibiotic with Cdc25A inhibitory activity, produced by Chrysosporium sp. TC1068. Taxonomy, fermentation and biological activities. (1/24)

A new antibiotic designated TMC-69 has been isolated from the fermentation broth of a fungal strain Chrysosporium sp. TC 1068. TMC-69 exhibited moderate in vitro cytotoxic activity. TMC-69-6H, a derivative of TMC-69 prepared by hydrogenation, possessed more potent in vitro cytotoxicity than TMC-69, and exhibited in vivo antitumor activity against murine P388 leukemia and B16 melanoma. TMC-69-6H was found to specifically inhibit Cdc25A and B phosphatases.  (+info)

Pulmonary colonization by Chrysosporium zonatum associated with allergic inflammation in an immunocompetent subject. (2/24)

We report a case of noninvasive pulmonary disease due to Chrysosporium zonatum in an immunocompetent male. The fungus colonized an existing tuberculous cavity and was isolated from transbronchial lavage fluid and from a percutaneous aspiration specimen. The disease was accompanied by the unusual feature of an allergic reaction. The fungus ball was successfully treated by intracavitary administration of amphotericin B. C. zonatum is the anamorph of the heterothallic ascomycete Uncinocarpus orissi, and the identity of the case isolate was verified by formation of ascospores in mating tests with reference isolates.  (+info)

Non-sporulating Chrysosporium: an opportunistic fungal infection in a neutropenic patient. (3/24)

We report a case of an invasive infection with non-sporulating Chrysosporium species in a patient who was treated with chemotherapy for relapsed acute lymphoblastic leukemia. This patient presented with a persistent lobar pneumonia, skin lesions, and possible involvement of the central nervous system. The patient responded to treatment with amphotericin B and oral itraconazole.  (+info)

False identification of Coccidioides immitis: do molecular methods always get it right? (4/24)

rRNA sequence analysis of a partial region of the 18S and 5.8S-internal transcribed spacer 2 (ITS2) region of Chrysosporium keratinophilum highlights its potential molecular misidentification as Coccidioides immitis. Molecular identification of medically important fungi should not be based solely on sequence analysis of the 18S rRNA gene but should be confirmed by sequence analysis of an additional rRNA gene locus, such as the ITS region(s).  (+info)

Specific xyloglucanases as a new class of polysaccharide-degrading enzymes. (5/24)

Three specific xyloglucanases (XGs) were isolated from Aspergillus japonicus (32 kDa, pI 2.8), Chrysosporium lucknowense (78 kDa, pI 3.8) and Trichoderma reesei (75-105 kDa, pI 4.1-4.3). The characteristic feature of these enzymes was their high specific activity toward tamarind xyloglucan, whereas the activity against carboxymethylcellulose (CMC) and barley beta-glucan was absent or very low. Peptide mass fingerprinting using MALDI-TOF mass spectrometry showed that the T. reesei XG represents Cel74A, whose gene has been discovered recently (GenBank accession no. AY281371 ), but the enzyme has not been characterized and described elsewhere. Tryptic peptides from A. japonicus and C. lucknowense xyloglucanases did not show any identity to those from known glycoside hydrolases. All enzymes produced XXXG, XXLG/XLXG and XLLG oligosaccharides as the end products of xyloglucan hydrolysis. A. japonicus XG displayed an endo-type of attack on the polymeric substrate, while the mode of action of two other xyloglucanases was similar to the exo-type, when oligosaccharides containing four glucose residues in the main chain were split off the ends of xyloglucan molecules. These results together with growing literature data allow concluding that specific xyloglucanases may represent a new class of glycoside hydrolases, which are different from regular endo-1,4-beta-glucanases.  (+info)

False-positive Histoplasma capsulatum Gen-Probe chemiluminescent test result caused by a Chrysosporium species. (6/24)

We describe a case in which the Histoplasma capsulatum AccuProbe test displayed cross-reactivity with a respiratory isolate thought to be Histoplasma but not morphologically consistent with H. capsulatum. The isolate was later identified as the Chrysosporium anamorph of Nannizziopsis vriesii by sequence analysis and phenotypic data.  (+info)

Overproduction of lignin-degrading enzymes by an isolate of Phanerochaete chrysosporium. (7/24)

Phanerochaete chrysosporium is a white rot fungus which secretes a family of lignin-degrading enzymes under nutrient limitation. PSBL-1 is a mutant of this organism that generates the ligninolytic system under nonlimiting conditions during primary metabolism. Lignin peroxidase, manganese peroxidase, and glyoxal oxidase activities for PSBL-1 under nonlimiting conditions were 4- to 10-fold higher than those of the wild type (WT) under nitrogen-limiting conditions. PSBL-1 was still in the log phase of growth while secreting the enzymes, whereas the WT had ceased to grow by this time. As in the WT, manganese(II) increased manganese peroxidase activity in the mutant. However, manganese also caused an increase in lignin peroxidase and glyoxal oxidase activities in PSBL-1. Addition of veratryl alcohol to the culture medium stimulated lignin peroxidase activity, inhibited glyoxal oxidase activity, and had little effect on manganese peroxidase activity in PSBL-1, as in the WT. Fast protein liquid chromatography (FPLC) analysis shows production of larger amounts of isozyme H2 in PSBL-1 than in the WT. These properties make PSBL-1 very useful for isolation of large amounts of all ligninolytic enzymes for biochemical study, and they open the possibility of scale-up production for pratical use.  (+info)

Pannorin, a new 3-hydroxy-3-methylglutaryl coenzyme A reductase inhibitor produced by Chrysosporium pannorum. (8/24)

Pannorin, a naphthopyrone that inhibits 3-hydroxy-3-methylglutaryl coenzyme A (HMG-CoA) reductase, the rate-limiting enzyme in cholesterol synthesis, was isolated from a culture broth of Chrysosporium pannorum M10539 by solvent extraction, Bio-Gel P-6 column chromatography and reverse phase HPLC (Silica ODS). Spectroscopic analyses of the compound yielded 4,8,10-trihydroxy-5-methyl-2H-naphtho[1,2-b]pyran-2-one as the proposed structure. Pannorin inhibited HMG-CoA reductase and in vitro sterol synthesis 50% at a concentration of 160 microM.  (+info)

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