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Reto Crameri - One of the best experts on this subject based on the ideXlab platform.

  • the vacuolar serine protease a cross reactive allergen from Cladosporium herbarum
    Molecular Immunology, 2009
    Co-Authors: Verena Poll, Reto Crameri, Ursula Denk, Horngder Shen, Raphael C Panzani, Oliver Dissertori, Peter Lackner, Wolfgang Hemmer, Adriano Mari, Friedrich Lottspeich
    Abstract:

    Subtilisin-like serine proteases make up one of the most important allergen-families regarding the number of individual allergens. Previously, fungal subtilisin-like serine proteases have been identified from Aspergillus-, Penicillium-, and Trichophyton-species having a prevalence of IgE-reactivity between 33% and 80%. Since IgE-cross-reactivity is a common phenomenon within fungal species we wanted to know whether this protein also represents an allergen in Cladosporium herbarum. Hence, a screening of a C. herbarum cDNA library was performed using the coding sequence of the Penicillium oxalicum vacuolar serine protease (Pen o 18) as hybridization probe, ending up with a full-length clone. Biochemical and immunological characterization of this clone revealed that C. herbarum vacuolar serine protease most likely is synthesized as a precursor with an N-terminal pro-enzyme sequence and represents a minor allergen (Cla h 9) with a prevalence of IgE-reactivity of 15.5%. Furthermore Cla h 9 specifically reacted with the two monoclonal antibodies FUM20 and PCM39, as do the vacuolar serine proteases from Aspergillus fumigatus and Penicillium species. Investigation of IgE-cross-reactivity between Cla h 9 and other fungal serine proteases revealed that cross-reactivity is higher between vacuolar than alkaline serine proteases. IgE-epitope mapping of Cla h 9 was done in order to test whether four Cla h 9-peptides having a high sequence homology to previously determined Pen ch 18-IgE-epitopes also harbour IgE-epitopes. Three-dimensional models of the vacuolar serine proteases from C. herbarum and Penicillium chrysogenum were generated for the three-dimensional localization of the Cla h 9- and Pen ch 18- IgE-reactive and -non-reactive peptides. Taken together a new C. herbarum allergen has been identified, which may be useful in a molecule-based approach of C. herbarum allergy-diagnosis and -therapy. Moreover, Cla h 9 represents a further member of the subtilisin-like serine protease allergen-family, which stresses the importance of these proteins with respect to fungal IgE-cross-reactivity.

  • NADP-dependent mannitol dehydrogenase, a major allergen of Cladosporium herbarum
    The Journal of biological chemistry, 2006
    Co-Authors: Birgit Simon-nobbe, Reto Crameri, Peter Schneider, Ursula Denk, Klaus Richter, Christian Radauer, Markus Teige, Thomas Hawranek, Roland Lang, Peter Schmid-grendelmeier
    Abstract:

    Abstract Cladosporium herbarum is an important allergenic fungal species that has been reported to cause allergic diseases in nearly all climatic zones. 5–30% of the allergic population displays IgE antibodies against molds. Sensitization to Cladosporium has often been associated with severe asthma and less frequently with chronic urticaria and atopic eczema. However, no dominant major allergen of this species has been found so far. We present cloning, production, and characterization of NADP-dependent mannitol dehydrogenase of C. herbarum (Cla h 8) and show that this protein is a major allergen that is recognized by IgE antibodies of ∼57% of all Cladosporium allergic patients. This is the highest percentage of patients reacting with any Cladosporium allergen characterized so far. Cla h 8 was purified to homogeneity by standard chromatographic methods, and both N-terminal and internal amino acid sequences of protein fragments were determined. Enzymatic analysis of the purified natural protein revealed that this allergen represents a NADP-dependent mannitol dehydrogenase that interconverts mannitol and d-fructose. It is a soluble, non-glycosylated cytoplasmic protein. Two-dimensional protein analysis indicated that mannitol dehydrogenase is present as a single isoform. The cDNA encoding Cla h 8 was cloned from a λ-ZAP library constructed from hyphae and spores. The recombinant non-fusion protein was expressed in Escherichia coli and purified to homogeneity. Its immunological and biochemical identity with the natural protein was shown by enzyme activity tests, CD spectroscopy, IgE immunoblots with sera of patients, and by skin prick testing of Cladosporium allergic patients. This protein therefore is a new major allergen of C. herbarum.

  • Histamine releasing factor (TCTP) is an auto-reactive IgE-binding antigen in patients allergic to Cladosporium herbarum☆
    Journal of Allergy and Clinical Immunology, 2004
    Co-Authors: Claudia Holler, Reto Crameri, Klaus Richter, Birgit Simon-nobbe, Verena Wally, Arnulf Josef Hartl, J. Thalhamer, C. Ebner
    Abstract:

    Abstract Rationale Cladosporium herbarum ( C. herbarum ) is one of the most important and world wide occurring allergenic fungal species. Sensitization to C. herbarum (and fungi in general) has often been associated with asthma, chronic idiopathic urticaria, and allergic dermatitis. It is therefore interesting to define the allergen repertoire of C. herbarum . We have undertaken here to characterize a new Cladosporium allergen, which was isolated from a cDNA library of C. herbarum spores and mycelia and to compare it with its human homologue. Methods A C. herbarum cDNA library constructed in the lambda-ZAP vector was screened with sera of patients allergic to Cladosporium . The newly isolated cDNA clone and its human homolog were expressed in E. coli , purified to homogeneity and immunologically analyzed by IgE blots. Results The characterized allergen is a close homolog of the human histamine releasing factor (TCTP). IgE antibodies of three of five patients, which recognize the Cladosporium allergen, also recognize the human protein in immune blots. Conclusion The new allergen will not only contribute to define more comprehensively the allergen repertoire of C. herbarum , it also allows us to test the role of a new auto-antigen with a possible role in certain severe forms of allergic disease.

  • Immunoglobulin E‐binding and skin test reactivity to hydrophobin HCh‐1 from Cladosporium herbarum, the first allergenic cell wall component of fungi
    Clinical and experimental allergy : journal of the British Society for Allergy and Clinical Immunology, 2003
    Co-Authors: Michael Weichel, Claudio Rhyner, Gernot Achatz, Kurt Blaser, Peter Schmid-grendelmeier, Reto Crameri
    Abstract:

    Summary Background For many years, fungal spores have been recognized as potential causes of respiratory allergies. All fungal allergens cloned so far represent either secreted or cytoplasmatic proteins, but nothing is known about the involvement of fungal surface proteins in allergic diseases. Methods A phage surface displayed cDNA-library from the mould Cladosporium herbarum was constructed and phage displaying IgE-binding proteins were selectively enriched with immobilized serum IgE from C. herbarum-sensitized individuals. Inserts encoding putative allergens were sequenced, subcloned and used to produce recombinant proteins. Allergenicity of the proteins was evaluated by IgE binding in Western blots, enzyme-linked immunosorbent assay (ELISA) and skin prick test in a total of 84 patients sensitized to either C. herbarum or Aspergillus fumigatus and three healthy controls. Results After four rounds of affinity selection, the cDNA-library was enriched for clones displaying IgE-binding molecules. Sequencing of inserts showed that one clone contained an open reading frame predicting a protein of 105 amino acids and a calculated molecular weight of 10.5 kDa showing the classical signature of members of the hydrophobin family. The recombinant protein, termed HCh-1, was able to bind IgE from six patients sensitized to fungi in vitro. Two of those patients were also included in a skin prick test survey and showed strong type I skin reactions to HCh-1, demonstrating the allergenic nature of C. herbarum hydrophobin and indicating a prevalence of sensitization in the range of 8–9%. In contrast, the hydrophobin HYP1 from Aspergillus fumigatus was not recognized by the sera of the same patients and controls investigated with HCh-1. ConclusionC. herbarum hydrophobin represents the first component of the cell wall of fungi demonstrated to act as a rare but clinically relevant allergen in vitro and in vivo.

  • immunoglobulin e binding and skin test reactivity to hydrophobin hch 1 from Cladosporium herbarum the first allergenic cell wall component of fungi
    Clinical & Experimental Allergy, 2003
    Co-Authors: Michael Weichel, Peter Schmidgrendelmeier, Claudio Rhyner, Gernot Achatz, Kurt Blaser, Reto Crameri
    Abstract:

    Summary Background For many years, fungal spores have been recognized as potential causes of respiratory allergies. All fungal allergens cloned so far represent either secreted or cytoplasmatic proteins, but nothing is known about the involvement of fungal surface proteins in allergic diseases. Methods A phage surface displayed cDNA-library from the mould Cladosporium herbarum was constructed and phage displaying IgE-binding proteins were selectively enriched with immobilized serum IgE from C. herbarum-sensitized individuals. Inserts encoding putative allergens were sequenced, subcloned and used to produce recombinant proteins. Allergenicity of the proteins was evaluated by IgE binding in Western blots, enzyme-linked immunosorbent assay (ELISA) and skin prick test in a total of 84 patients sensitized to either C. herbarum or Aspergillus fumigatus and three healthy controls. Results After four rounds of affinity selection, the cDNA-library was enriched for clones displaying IgE-binding molecules. Sequencing of inserts showed that one clone contained an open reading frame predicting a protein of 105 amino acids and a calculated molecular weight of 10.5 kDa showing the classical signature of members of the hydrophobin family. The recombinant protein, termed HCh-1, was able to bind IgE from six patients sensitized to fungi in vitro. Two of those patients were also included in a skin prick test survey and showed strong type I skin reactions to HCh-1, demonstrating the allergenic nature of C. herbarum hydrophobin and indicating a prevalence of sensitization in the range of 8–9%. In contrast, the hydrophobin HYP1 from Aspergillus fumigatus was not recognized by the sera of the same patients and controls investigated with HCh-1. ConclusionC. herbarum hydrophobin represents the first component of the cell wall of fungi demonstrated to act as a rare but clinically relevant allergen in vitro and in vivo.

Peter Proksch - One of the best experts on this subject based on the ideXlab platform.

  • new metabolites from sponge derived fungi curvularia lunata and Cladosporium herbarum
    Journal of Natural Products, 2002
    Co-Authors: Raquel Jadulco, Rainer Ebel, Gernot Brauers, Ruangelie Edradaebel, Victor Wray, Peter Proksch
    Abstract:

    The fungus Curvularia lunata, isolated from the marine sponge Niphates olemda, yielded the new 1,3,8-trihydroxy-6-methoxyanthraquinone, which we named lunatin (1), the known modified bisanthraquinone cytoskyrin A (2), and the known plant hormone (+)-abscisic acid (3). Both anthraquinones were found to be active against Bacillus subtilis, Staphylococcus aureus, and Escherichia coli. Two strains of the fungus Cladosporium herbarum, isolated from the sponges Aplysina aerophoba and Callyspongia aerizusa, respectively, yielded two new α-pyrones, herbarin A (4) and herbarin B (5), the known compound citreoviridin A (6), and the new phthalide herbaric acid (7). All structures were unambiguously established by 1D and 2D NMR and MS data.

  • new macrolides and furan carboxylic acid derivative from the sponge derived fungus Cladosporium herbarum
    Journal of Natural Products, 2001
    Co-Authors: Raquel Jadulco, And Albrecht Berg, Peter Proksch, Victor Wray, Udo Gräfe
    Abstract:

    Bioassay-guided fractionation of organic extracts of Cladosporium herbarum, isolated from the marine sponge Callyspongia aerizusa, yielded two new macrolide metabolites:  pandangolide 3 and 4 (1 and 2) and the known fungal metabolites pandangolide 2 (3), cladospolide B (4), and iso-cladospolide B (5). Also isolated were the antimicrobially active (against Bacillus subtilis and Staphylococcus aureus) furan carboxylic acids:  Sumiki's acid (6) and its new derivative, acetyl Sumiki's acid (7). All structures were elucidated by spectroscopic methods.

Gernot Achatz - One of the best experts on this subject based on the ideXlab platform.

  • Immunoglobulin E‐binding and skin test reactivity to hydrophobin HCh‐1 from Cladosporium herbarum, the first allergenic cell wall component of fungi
    Clinical and experimental allergy : journal of the British Society for Allergy and Clinical Immunology, 2003
    Co-Authors: Michael Weichel, Claudio Rhyner, Gernot Achatz, Kurt Blaser, Peter Schmid-grendelmeier, Reto Crameri
    Abstract:

    Summary Background For many years, fungal spores have been recognized as potential causes of respiratory allergies. All fungal allergens cloned so far represent either secreted or cytoplasmatic proteins, but nothing is known about the involvement of fungal surface proteins in allergic diseases. Methods A phage surface displayed cDNA-library from the mould Cladosporium herbarum was constructed and phage displaying IgE-binding proteins were selectively enriched with immobilized serum IgE from C. herbarum-sensitized individuals. Inserts encoding putative allergens were sequenced, subcloned and used to produce recombinant proteins. Allergenicity of the proteins was evaluated by IgE binding in Western blots, enzyme-linked immunosorbent assay (ELISA) and skin prick test in a total of 84 patients sensitized to either C. herbarum or Aspergillus fumigatus and three healthy controls. Results After four rounds of affinity selection, the cDNA-library was enriched for clones displaying IgE-binding molecules. Sequencing of inserts showed that one clone contained an open reading frame predicting a protein of 105 amino acids and a calculated molecular weight of 10.5 kDa showing the classical signature of members of the hydrophobin family. The recombinant protein, termed HCh-1, was able to bind IgE from six patients sensitized to fungi in vitro. Two of those patients were also included in a skin prick test survey and showed strong type I skin reactions to HCh-1, demonstrating the allergenic nature of C. herbarum hydrophobin and indicating a prevalence of sensitization in the range of 8–9%. In contrast, the hydrophobin HYP1 from Aspergillus fumigatus was not recognized by the sera of the same patients and controls investigated with HCh-1. ConclusionC. herbarum hydrophobin represents the first component of the cell wall of fungi demonstrated to act as a rare but clinically relevant allergen in vitro and in vivo.

  • immunoglobulin e binding and skin test reactivity to hydrophobin hch 1 from Cladosporium herbarum the first allergenic cell wall component of fungi
    Clinical & Experimental Allergy, 2003
    Co-Authors: Michael Weichel, Peter Schmidgrendelmeier, Claudio Rhyner, Gernot Achatz, Kurt Blaser, Reto Crameri
    Abstract:

    Summary Background For many years, fungal spores have been recognized as potential causes of respiratory allergies. All fungal allergens cloned so far represent either secreted or cytoplasmatic proteins, but nothing is known about the involvement of fungal surface proteins in allergic diseases. Methods A phage surface displayed cDNA-library from the mould Cladosporium herbarum was constructed and phage displaying IgE-binding proteins were selectively enriched with immobilized serum IgE from C. herbarum-sensitized individuals. Inserts encoding putative allergens were sequenced, subcloned and used to produce recombinant proteins. Allergenicity of the proteins was evaluated by IgE binding in Western blots, enzyme-linked immunosorbent assay (ELISA) and skin prick test in a total of 84 patients sensitized to either C. herbarum or Aspergillus fumigatus and three healthy controls. Results After four rounds of affinity selection, the cDNA-library was enriched for clones displaying IgE-binding molecules. Sequencing of inserts showed that one clone contained an open reading frame predicting a protein of 105 amino acids and a calculated molecular weight of 10.5 kDa showing the classical signature of members of the hydrophobin family. The recombinant protein, termed HCh-1, was able to bind IgE from six patients sensitized to fungi in vitro. Two of those patients were also included in a skin prick test survey and showed strong type I skin reactions to HCh-1, demonstrating the allergenic nature of C. herbarum hydrophobin and indicating a prevalence of sensitization in the range of 8–9%. In contrast, the hydrophobin HYP1 from Aspergillus fumigatus was not recognized by the sera of the same patients and controls investigated with HCh-1. ConclusionC. herbarum hydrophobin represents the first component of the cell wall of fungi demonstrated to act as a rare but clinically relevant allergen in vitro and in vivo.

  • Molecular characterization of Alternaria alternata and Cladosporium herbarum allergens
    Advances in experimental medicine and biology, 1996
    Co-Authors: Gernot Achatz, Hannes Oberkofler, Erich Lechenauer, Birgit Simon, Andrea Unger, Doris Kandler, C. Ebner, Hansjörg Prillinger, Dietrich Kraft, Michael Breitenbach
    Abstract:

    Investigations of fungal air spora have demonstrated that conidium-forming fungi usually predominate over other fungal groups. Cladosporium herbarum, Alternaria alternata, Penicillium sp. and Aspergillus sp., listed in decreasing frequency of occurrence, are most consistently associated with the highest mean percentages of total fungal spore catches. In addition to daily variations in meteorologie conditions and seasonal changes, both of which have enormous impact on the concentration of air spora, the amount and type of vegetation of a region or microenvironment may be important factors in determining the composition of the airborne fungal population. Over the past two decades most allergologists have recognized a need for more information on fungal allergy because of increased awareness of the problem and the greater number of patients suffering from asthma and rhinitis due to fungi. Seasonal variation in regard to fungi in the air or to those in homes, and their detection and monitoring but also the biological relevance of the allergenic protein in the fungal organism are new fields of studies (1, 2). In the environment, Cladosporium herbarum is the most frequently encountered mould in the air. The dry conidia are carried easily through the air and can be detected in extremely large numbers e.g. a concentration of 35000 conidia/cubic meter can often be measured. The indoor counts to a large extent reflect the outdoor concentration. Depending on climate conditions the conidia may begin to appear in the atmosphere in spring and rise to a peak in either late summer or early autumn. Cladosporium herbarum is one of the most common colonizer of dying and dead plants and also occurs in various soil types and on food. It can frequently be found in uncleaned refrigerators, foodstuff, on wet window frames, in houses with poor ventilation and houses with straw roofs (3, 4, 5).

  • molecular cloning of major and minor allergens of alternaria alternata and Cladosporium herbarum
    Molecular Immunology, 1995
    Co-Authors: Gernot Achatz, Hannes Oberkofler, Erich Lechenauer, Birgit Simon, Andrea Unger, Doris Kandler, C. Ebner, Hansjörg Prillinger, Dietrich Kraft, Michael Breitenbach
    Abstract:

    The two moulds, Alternaria alternata and Cladosporium herbarum, are recognized as major causes of fungal allergies. Cloning, sequencing and heterologous expression of the allergens of the two moulds is a necessary step in understanding fungal allergy and in the development of new and improved methods of diagnosis and therapy. The seven new mould allergens presented here represent four new allergen proteins: aldehyde dehydrogenase (ALDH), enolase, YCP4 (previously found as a Saccharomyces cerevisiae protein of unknown function), and the acidic ribosomal protein, P2. Three of them (ALDH, YCP4 and P2) were found to be allergens in both fungi, Alternaria and Cladosporium. All allergens found so far are cytoplasmic proteins and are rather well conserved in evolution even when comparing distant species. Most of the allergens have "household" functions (ALDH, enolase). One allergen (P2) is a homolog of a very highly conserved human lupus erythematodes (LE) antigen. None of the fungal allergens is clearly related to other known non-fungal allergens.

Michael Weichel - One of the best experts on this subject based on the ideXlab platform.

  • Immunoglobulin E‐binding and skin test reactivity to hydrophobin HCh‐1 from Cladosporium herbarum, the first allergenic cell wall component of fungi
    Clinical and experimental allergy : journal of the British Society for Allergy and Clinical Immunology, 2003
    Co-Authors: Michael Weichel, Claudio Rhyner, Gernot Achatz, Kurt Blaser, Peter Schmid-grendelmeier, Reto Crameri
    Abstract:

    Summary Background For many years, fungal spores have been recognized as potential causes of respiratory allergies. All fungal allergens cloned so far represent either secreted or cytoplasmatic proteins, but nothing is known about the involvement of fungal surface proteins in allergic diseases. Methods A phage surface displayed cDNA-library from the mould Cladosporium herbarum was constructed and phage displaying IgE-binding proteins were selectively enriched with immobilized serum IgE from C. herbarum-sensitized individuals. Inserts encoding putative allergens were sequenced, subcloned and used to produce recombinant proteins. Allergenicity of the proteins was evaluated by IgE binding in Western blots, enzyme-linked immunosorbent assay (ELISA) and skin prick test in a total of 84 patients sensitized to either C. herbarum or Aspergillus fumigatus and three healthy controls. Results After four rounds of affinity selection, the cDNA-library was enriched for clones displaying IgE-binding molecules. Sequencing of inserts showed that one clone contained an open reading frame predicting a protein of 105 amino acids and a calculated molecular weight of 10.5 kDa showing the classical signature of members of the hydrophobin family. The recombinant protein, termed HCh-1, was able to bind IgE from six patients sensitized to fungi in vitro. Two of those patients were also included in a skin prick test survey and showed strong type I skin reactions to HCh-1, demonstrating the allergenic nature of C. herbarum hydrophobin and indicating a prevalence of sensitization in the range of 8–9%. In contrast, the hydrophobin HYP1 from Aspergillus fumigatus was not recognized by the sera of the same patients and controls investigated with HCh-1. ConclusionC. herbarum hydrophobin represents the first component of the cell wall of fungi demonstrated to act as a rare but clinically relevant allergen in vitro and in vivo.

  • immunoglobulin e binding and skin test reactivity to hydrophobin hch 1 from Cladosporium herbarum the first allergenic cell wall component of fungi
    Clinical & Experimental Allergy, 2003
    Co-Authors: Michael Weichel, Peter Schmidgrendelmeier, Claudio Rhyner, Gernot Achatz, Kurt Blaser, Reto Crameri
    Abstract:

    Summary Background For many years, fungal spores have been recognized as potential causes of respiratory allergies. All fungal allergens cloned so far represent either secreted or cytoplasmatic proteins, but nothing is known about the involvement of fungal surface proteins in allergic diseases. Methods A phage surface displayed cDNA-library from the mould Cladosporium herbarum was constructed and phage displaying IgE-binding proteins were selectively enriched with immobilized serum IgE from C. herbarum-sensitized individuals. Inserts encoding putative allergens were sequenced, subcloned and used to produce recombinant proteins. Allergenicity of the proteins was evaluated by IgE binding in Western blots, enzyme-linked immunosorbent assay (ELISA) and skin prick test in a total of 84 patients sensitized to either C. herbarum or Aspergillus fumigatus and three healthy controls. Results After four rounds of affinity selection, the cDNA-library was enriched for clones displaying IgE-binding molecules. Sequencing of inserts showed that one clone contained an open reading frame predicting a protein of 105 amino acids and a calculated molecular weight of 10.5 kDa showing the classical signature of members of the hydrophobin family. The recombinant protein, termed HCh-1, was able to bind IgE from six patients sensitized to fungi in vitro. Two of those patients were also included in a skin prick test survey and showed strong type I skin reactions to HCh-1, demonstrating the allergenic nature of C. herbarum hydrophobin and indicating a prevalence of sensitization in the range of 8–9%. In contrast, the hydrophobin HYP1 from Aspergillus fumigatus was not recognized by the sera of the same patients and controls investigated with HCh-1. ConclusionC. herbarum hydrophobin represents the first component of the cell wall of fungi demonstrated to act as a rare but clinically relevant allergen in vitro and in vivo.

  • Unfolding and Double-stranded DNA Binding of the Cold Shock Protein Homologue Cla h 8 from Cladosporium herbarum
    The Journal of biological chemistry, 2002
    Co-Authors: S. Fabio Falsone, Michael Weichel, Reto Crameri, Michael Breitenbach, Andreas J. Kungl
    Abstract:

    Abstract The cloning, purification, and biophysical characterization of the first eukaryotic cold shock protein homologue, Cla h 8, expressed as single functional polypeptide is reported here. It was discovered as a minor allergen of the mold Cladosporium herbarum by phage display using a library selectively enriched for IgE-binding proteins. Based on the sequence homology of Cla h 8 with bacterial cold shock proteins (CSPs), a homology-based computer model of the allergen was computed indicating an all-β structure of Cla h 8. This major structural feature was confirmed by CD spectroscopy. Despite the structural similarities with bacterial CSPs, the DNA-binding and unfolding behavior of Cla h 8 exhibited unique and previously undescribed characteristics. High affinities of Cla h 8 for single-stranded DNA as well as for double-stranded DNA corresponding to the human Y-box were detected. The affinity for double-stranded DNA increased significantly with decreasing temperature, which was paralleled by an increase in the β sheet content of the protein. Temperature-dependent fluorescence anisotropy and far-UV CD measurements revealed different unfolding transitions at 28 and at 35.7 °C, respectively, indicating a multistate transition, which is uncommon for CSPs. The enhanced affinity for DNA at low temperatures together with the low unfolding transition refer to the functional significance of Cla h 8 at reduced temperatures.

Raquel Jadulco - One of the best experts on this subject based on the ideXlab platform.

  • new metabolites from sponge derived fungi curvularia lunata and Cladosporium herbarum
    Journal of Natural Products, 2002
    Co-Authors: Raquel Jadulco, Rainer Ebel, Gernot Brauers, Ruangelie Edradaebel, Victor Wray, Peter Proksch
    Abstract:

    The fungus Curvularia lunata, isolated from the marine sponge Niphates olemda, yielded the new 1,3,8-trihydroxy-6-methoxyanthraquinone, which we named lunatin (1), the known modified bisanthraquinone cytoskyrin A (2), and the known plant hormone (+)-abscisic acid (3). Both anthraquinones were found to be active against Bacillus subtilis, Staphylococcus aureus, and Escherichia coli. Two strains of the fungus Cladosporium herbarum, isolated from the sponges Aplysina aerophoba and Callyspongia aerizusa, respectively, yielded two new α-pyrones, herbarin A (4) and herbarin B (5), the known compound citreoviridin A (6), and the new phthalide herbaric acid (7). All structures were unambiguously established by 1D and 2D NMR and MS data.

  • new macrolides and furan carboxylic acid derivative from the sponge derived fungus Cladosporium herbarum
    Journal of Natural Products, 2001
    Co-Authors: Raquel Jadulco, And Albrecht Berg, Peter Proksch, Victor Wray, Udo Gräfe
    Abstract:

    Bioassay-guided fractionation of organic extracts of Cladosporium herbarum, isolated from the marine sponge Callyspongia aerizusa, yielded two new macrolide metabolites:  pandangolide 3 and 4 (1 and 2) and the known fungal metabolites pandangolide 2 (3), cladospolide B (4), and iso-cladospolide B (5). Also isolated were the antimicrobially active (against Bacillus subtilis and Staphylococcus aureus) furan carboxylic acids:  Sumiki's acid (6) and its new derivative, acetyl Sumiki's acid (7). All structures were elucidated by spectroscopic methods.