<I>Candida albicans</I> Adheres to Chitin by Recognizing <I>N</I>-acetylglucosamine (GlcNAc)
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- Ishijima Sanae A.
- Teikyo University Institute of Medical Mycology
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- Yamada Tsuyoshi
- Teikyo University Institute of Medical Mycology
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- Maruyama Naho
- Teikyo University Institute of Medical Mycology Faculty of Health and Medical Science, Teikyo Heisei University
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- Abe Shigeru
- Teikyo University Institute of Medical Mycology
Bibliographic Information
- Other Title
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- Candida albicans Adheres to Chitin by Recognizing N-acetylglucosamine (GlcNAc)
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Description
The binding of Candida albicans cells to chitin was examined in a cell-binding assay. Microscopic observations indicated that both living and heat-killed Candida cells bound to chitin-coated substrates. C. albicans preferentially bound to chitin-coated plastic plates over chitosan-coated and uncoated plates. We prepared 125I-labeled Candida cells for quantitative analysis of their binding to chitin. Heat-killed 125I-labeled Candida cells bound to chitin-coated plates in a time-dependent manner until 1.5 hours after start of incubation at 4℃. The binding of 125I-labeled Candida cells to chitin-coated plates was inhibited by adding unlabeled living or unlabeled heat-killed Candida cells. The binding of Candida to chitin was also reduced by addition of 25 mg/ml chitin or chitosan up to 10%. N-acetylglucosamine (GlcNAc), which is a constituent of chitin, inhibited binding of Candida to chitin in a dose-dependent manner between 12.5 and 200 mM. Glucosamine, which is a constituent of chitosan, showed no such inhibitory effect. These findings suggest that the binding of Candida to chitin may be mediated by recognition of GlcNAc.
Journal
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- Medical Mycology Journal
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Medical Mycology Journal 58 (1), E15-E21, 2017
The Japanese Society for Medical Mycology
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Details 詳細情報について
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- CRID
- 1390001205398286208
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- NII Article ID
- 130005401911
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- NII Book ID
- AA12518136
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- ISSN
- 2186165X
- 18820476
- 21856486
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- NDL BIB ID
- 027969713
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- PubMed
- 28250359
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- Text Lang
- ja
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- Data Source
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- JaLC
- NDL
- Crossref
- PubMed
- CiNii Articles
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- Abstract License Flag
- Disallowed