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Asc1p, a Ribosomal Protein, Plays a Pivotal Role in Cellular Adhesion and Virulence in Candida albicans

Authors
Kim, Se WoongJoo, Yoo JinKim, Joon
Issue Date
Dec-2010
Publisher
MICROBIOLOGICAL SOCIETY KOREA
Keywords
C. albicans; Asc1p; ribosomal protein; virulence; adhesion
Citation
JOURNAL OF MICROBIOLOGY, v.48, no.6, pp.842 - 848
Indexed
SCIE
SCOPUS
KCI
Journal Title
JOURNAL OF MICROBIOLOGY
Volume
48
Number
6
Start Page
842
End Page
848
URI
https://scholar.korea.ac.kr/handle/2021.sw.korea/115225
DOI
10.1007/s12275-010-0422-1
ISSN
1225-8873
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.
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