Asc1p, a ribosomal protein, plays a pivotal role in cellular adhesion and virulence in Candida albicans

Se Woong Kim, Yoo Jin Joo, Joon Kim

    Research output: Contribution to journalArticlepeer-review

    16 Citations (Scopus)

    Abstract

    Candida albicans, the common human fungal pathogen, can switch morphology from yeast to pseudohyphal or hyphal form upon various environmental cues. It is well-known that the ability of morphological conversion and adhesive growth renders C. albicans virulent. It is noteworthy that every factor involved in the morphogenesis is known to be important for the virulence of this pathogen. To examine a functional relevance of Asc1p, a ribosomal protein, in morphogenesis and virulence, an asc1 homozygous null mutant was generated. Although a normal morphological transition of the asc1 deletion strain in liquid media was found, it did not change its morphology on solid media. Moreover, the adhesion activity and hyphal-specific gene expression were defective due to ASC1 deletion. Finally, it was found that the asc1 null mutant was avirulent in a mouse model. These results strongly suggested that Asc1p a component of the 40S ribosomal subunit and a signal transducer, plays a pivotal role in cellular adhesion and virulence through regulation of specific gene expression in C. albicans.

    Original languageEnglish
    Pages (from-to)842-848
    Number of pages7
    JournalJournal of Microbiology
    Volume48
    Issue number6
    DOIs
    Publication statusPublished - 2010

    Bibliographical note

    Funding Information:
    This work was supported in part by FRR08131-230 and RO1-08-000-11574 grants from National Research Foundation of Korea.

    Keywords

    • Asc1p
    • C. albicans
    • adhesion
    • ribosomal protein
    • virulence

    ASJC Scopus subject areas

    • Microbiology
    • Applied Microbiology and Biotechnology

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