Complementary adhesin function in C-albicans biofilm formation

被引:252
作者
Nobile, Clarissa J. [1 ]
Schneider, Heather A. [2 ]
Nett, Jeniel E. [3 ]
Sheppard, Donald C. [4 ]
Filler, Scott G. [5 ]
Andes, David R. [3 ]
Mitchell, Aaron P. [1 ]
机构
[1] Columbia Univ, Dept Microbiol, New York, NY 10032 USA
[2] Columbia Univ, Dept Genet & Dev, New York, NY 10032 USA
[3] Univ Wisconsin, Dept Med, Infect Dis Sect, Madison, WI 53792 USA
[4] McGill Univ, Dept Microbiol & Immunol, Montreal, PQ H3A 2B4, Canada
[5] Harbor UCLA Med Ctr, Los Angeles Biomed Res Inst, Dept Med, Torrance, CA 90502 USA
关键词
D O I
10.1016/j.cub.2008.06.034
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Background: Biofilms are surface-associated microbial communities with significant environmental and medical impact. Here, we focus on an adherence mechanism that permits biofilm formation by Candida albicans, the major invasive fungal pathogen of humans. Results: The Als surface-protein family has been implicated in biofilm formation, and we show that Als1 and Als3 have critical but redundant roles. Overexpression of several other Als proteins permits biofilm formation in a biofilm-defective als1/als1 als3/als3 strain, thus arguing that the function of Als proteins in this process is governed by their respective expression levels. The surface protein Hwp1 is also required for biofilm formation, and we find that a mixture of biofilm-defective hwp1/hwp1 and als1/als1 als3/als3 strains can form a hybrid biofilm both in vitro and in vivo in a catheter infection model. Complementary function of Hwp1 and Als1 and 3 seems to reflect their interaction because expression of Hwp1 in the heterologous host S. cerevisiae permits adherence to wild-type C. albicans, but not to an als1/als1 als3/als3 strain. Conclusions: The complementary roles of Hwp1 and Als1 and Als3 in biofilm formation are analogous to the roles of sexual agglutinins in mating reactions. This analogy suggests that biofilm-adhesin complementarity may promote formation of monospecies biofilms.
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页码:1017 / 1024
页数:8
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