Open AccessExpression, crystallization and preliminary X‐ray data analysis of NT‐Als9‐2, a fungal adhesin from Candida albicans
Author(s) -
Salgado Paula S.,
Yan Robert,
Rowan Fiona,
Cota Ernesto
Publication year - 2011
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309111003460
Subject(s) - bacterial adhesin , candida albicans , microbiology and biotechnology , systemic candidiasis , escherichia coli , corpus albicans , recombinant dna , biology , chemistry , gene , biochemistry
Candida albicans is a common human fungal commensal that can also cause a range of infections from skin/mucosal `thrush' to severe systemic candidiasis. Adherence to host cells is one of the key determinants of Candida pathogenesis. The Als family of surface proteins has been implicated in adhesion of C. albicans , yet limited information has been published on the structure and mechanism of these fungal adhesins. The N‐terminal region of these proteins has been shown to possess adhesive properties, making it a possible target for new therapeutic strategies. Recombinant NT‐Als9‐2 from C. albicans (residues 18–329) was overexpressed in Escherichia coli , purified and crystallized. Diffraction data were collected to 2.0 Å resolution. The crystals belonged to space group P 2 1 2 1 2 1 , with unit‐cell parameters a = 34.73, b = 68.71, c = 120.03 Å, α = β = γ = 90° and one molecule in the asymmetric unit. Platinum‐derivatized crystals belonged to the same space group, with similar unit‐cell parameters, although they were not completely isomorphous.