Anthrax Research Today is a free monthly online journal that collates and summarizes the latest research about Anthrax, including details on bacillus anthracis, contagiousness, exposure, effects.

The conserved PA14 domain of cell wall-associated fungal adhesins governs their glycan-binding specificity.

de Groot PW, Klis FM

Swammerdam Institute for Life Sciences, University of Amsterdam, Nieuwe Achtergracht 166, 1018 WV, Amsterdam, The Netherlands.

Yeast cell wall-associated, lectin-like adhesins form large families that mediate flocculation and host cell recognition. The glycan specificity of individual adhesins is largely unknown. Zupancic et al. (this issue of Molecular Microbiology) used glycan microarrays to compare the glycan-binding characteristics of individual adhesins (Epa proteins) of the pathogenic yeast Candida glabrata produced in the non-adherent yeast Saccharomyces cerevisiae. By sequence swapping between the conserved PA14 domains of two related Epa proteins, they identified a pentapeptide that determines binding specificity and cell adherence and is located on a surface loop of the known crystal structure of the anthrax toxin PA14 domain.

Published 8 April 2008 in Mol Microbiol, 68(3): 535-7.
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