Covalently linked cell wall proteins of Candida albicans and their role in fitness and virulence

被引:131
作者
Klis, Frans M. [1 ]
Sosinska, Grazyna J. [1 ]
de Groot, Piet W. J. [1 ]
Brul, Stanley [1 ]
机构
[1] Univ Amsterdam, Swammerdam Inst Life Sci, NL-1018 WV Amsterdam, Netherlands
关键词
adhesion; amyloid; biofilm; cell wall model; GPI proteins; proteomics; GLYCOSYLPHOSPHATIDYLINOSITOL-ANCHORED PROTEINS; RECOMBINANT N-TERMINUS; BIOFILM FORMATION; SACCHAROMYCES-CEREVISIAE; TRANSCRIPTIONAL RESPONSE; IN-VIVO; SUPEROXIDE DISMUTASES; CICLOPIROX OLAMINE; HYPHAL DEVELOPMENT; ANTIFUNGAL AGENTS;
D O I
10.1111/j.1567-1364.2009.00541.x
中图分类号
Q81 [生物工程学(生物技术)]; Q93 [微生物学];
学科分类号
071005 ; 0836 ; 090102 ; 100705 ;
摘要
The cell wall of Candida albicans consists of an internal skeletal layer and an external protein coat. This coat has a mosaic-like nature, containing c. 20 different protein species covalently linked to the skeletal layer. Most of them are GPI proteins. Coat proteins vary widely in function. Many of them are involved in the primary interactions between C. albicans and the host and mediate adhesive steps or invasion of host cells. Others are involved in biofilm formation and cell-cell aggregation. They further include iron acquisition proteins, superoxide dismutases, and yapsin-like aspartic proteases. In addition, several covalently linked carbohydrate-active enzymes are present, whose precise functions remain hitherto largely elusive. The expression levels of the genes that encode covalently linked cell wall proteins (CWPs) can vary enormously. They depend on the mode of growth and the combined inputs of several signaling pathways that sense environmental conditions. This is reflected in the unusually long intergenic regions of most of these genes. Finally, the precise location of several covalently linked CWPs is temporally and spatially regulated. We conclude that covalently linked CWPs of C. albicans play a crucial role in fitness and virulence and that their expression is tightly controlled.
引用
收藏
页码:1013 / 1028
页数:16
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