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Eukaryotic Cell, May 2008, p. 776-782, Vol. 7, No. 5
1535-9778/08/$08.00+0     doi:10.1128/EC.00309-07
Copyright © 2008, American Society for Microbiology. All Rights Reserved.

Candida albicans Als Adhesins Have Conserved Amyloid-Forming Sequences{triangledown}

Henry N. Otoo,1 Kyeng Gea Lee,2 Weigang Qiu,3 and Peter N. Lipke1*

Department of Biology, Brooklyn College of City University of New York, New York, New York 11210,1 Department of Biology and Medical Laboratory Technology, Bronx Community College of City University of New York, Bronx, New York 10453,2 Department of Biology and the Center for Gene Structure and Function, Hunter College of City University of New York, New York, New York 100213

Received 22 August 2007/ Accepted 3 December 2007

The cell wall-bound Als adhesins of Candida albicans mediate both yeast-to-host tissue adherence and yeast aggregation. This aggregation is amyloid-like, with self-propagating secondary-structure changes, amyloid-characteristic dye binding, and induced birefringence (J. M. Rauceo, N. K. Gaur, K. G. Lee, J. E. Edwards, S. A. Klotz, and P. N. Lipke, Infect. Immun. 72:4948-4955, 2004). Therefore, we determined whether Als proteins could form amyloid fibers with properties like those in cellular aggregation. The β-aggregation predictor TANGO identified a heptapeptide sequence present in a highly conserved sequence with amyloid-forming potential in Als1p, Als3p, and Als5p. A tridecapeptide containing this sequence formed fibers that bound Congo red and thioflavin T and had characteristic amyloid morphology. Als5p20-431 and Als5p20-664, large fragments of Als5p containing the amyloid sequence, also formed amyloid-like fibers and bound Congo red under native conditions. Ka/Ks analysis showed that the amyloid-forming sequences are highly conserved in Als proteins and evolve more slowly than other regions of the proteins. Therefore, amyloid-forming ability itself is conserved in these proteins.

* Corresponding author. Mailing address: Department of Biology, Brooklyn College, 2900 Bedford Avenue, Brooklyn, NY 11210. Phone: (718) 951-5000, ext. 1949. Fax: (718) 951-4659. E-mail: plipke{at}brooklyn.cuny.edu

{triangledown} Published ahead of print on 14 December 2007.

Eukaryotic Cell, May 2008, p. 776-782, Vol. 7, No. 5
1535-9778/08/$08.00+0     doi:10.1128/EC.00309-07
Copyright © 2008, American Society for Microbiology. All Rights Reserved.



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