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Inhibition of yeast-to-hypha transition in Candida albicans by phorbasin H isolated from Phorbas sp.

Abstract

Phorbasin H is a diterpene acid of a bisabolane-related skeletal class isolated from the marine sponge Phorbas sp. In this study, we examined whether phorbasin H acted as a yeast-to-hypha transition inhibitor of Candida albicans. Growth experiments suggest that this compound does not inhibit yeast cell growth but inhibits filamentous growth in C. albicans. Northern blot analysis of signaling pathway components indicated that phorbasin H inhibited the expression of mRNAs related to cAMP-Efg1 pathway. The exogenous addition of db-cAMP to C. albicans cells had no influence on the frequency of hyphal formation. The expression of hypha-specific HWP1 and ALS3 mRNAs, both of which are positively regulated by the important regulator of cell wall dynamics Efg1, was significantly inhibited by the addition of phorbasin H. This compound also reduced the ability of C. albicans cells to adhere in a dose-dependent manner. Our findings suggest that phorbasin H impacts the activity of the cAMP-Efg1 pathway, thus leading to an alteration of C. albicans morphology.

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    MeSH

    Candida albicans
    Diterpenes
    Fungal Proteins
    Gene Expression
    Growth Inhibitors
    Hyphae
    Membrane Glycoproteins
    RNA, Messenger
    Signal Transduction

    Pub Type(s)

    Journal Article
    Research Support, Non-U.S. Gov't

    Language

    eng

    PubMed ID

    23229567

    Citation

    TY - JOUR T1 - Inhibition of yeast-to-hypha transition in Candida albicans by phorbasin H isolated from Phorbas sp. AU - Lee,So-Hyoung, AU - Jeon,Ju-eun, AU - Ahn,Chan-Hong, AU - Chung,Soon-Chun, AU - Shin,Jongheon, AU - Oh,Ki-Bong, Y1 - 2012/11/16/ PY - 2012/8/11/received PY - 2012/10/24/accepted PY - 2012/10/23/revised PY - 2012/11/16/aheadofprint PY - 2012/12/12/entrez PY - 2012/12/12/pubmed PY - 2013/9/3/medline SP - 3141 EP - 8 JF - Applied microbiology and biotechnology JO - Appl. Microbiol. Biotechnol. VL - 97 IS - 7 N2 - Phorbasin H is a diterpene acid of a bisabolane-related skeletal class isolated from the marine sponge Phorbas sp. In this study, we examined whether phorbasin H acted as a yeast-to-hypha transition inhibitor of Candida albicans. Growth experiments suggest that this compound does not inhibit yeast cell growth but inhibits filamentous growth in C. albicans. Northern blot analysis of signaling pathway components indicated that phorbasin H inhibited the expression of mRNAs related to cAMP-Efg1 pathway. The exogenous addition of db-cAMP to C. albicans cells had no influence on the frequency of hyphal formation. The expression of hypha-specific HWP1 and ALS3 mRNAs, both of which are positively regulated by the important regulator of cell wall dynamics Efg1, was significantly inhibited by the addition of phorbasin H. This compound also reduced the ability of C. albicans cells to adhere in a dose-dependent manner. Our findings suggest that phorbasin H impacts the activity of the cAMP-Efg1 pathway, thus leading to an alteration of C. albicans morphology. SN - 1432-0614 UR - https://www.unboundmedicine.com/medline/citation/23229567/Inhibition_of_yeast_to_hypha_transition_in_Candida_albicans_by_phorbasin_H_isolated_from_Phorbas_sp_ L2 - http://dx.doi.org/10.1007/s00253-012-4549-3 ER -