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Structural basis for promiscuity and specificity during Candida glabrata invasion of host epithelia.


ABSTRACT: The human pathogenic yeast Candida glabrata harbors more than 20 surface-exposed, epithelial adhesins (Epas) for host cell adhesion. The Epa family recognizes host glycans and discriminates between target tissues by their adhesin (A) domains, but a detailed structural basis for ligand-binding specificity of Epa proteins has been lacking so far. In this study, we provide high-resolution crystal structures of the Epa1A domain in complex with different carbohydrate ligands that reveal how host cell mucin-type O-glycans are recognized and allow a structure-guided classification of the Epa family into specific subtypes. Further detailed structural and functional characterization of subtype-switched Epa1 variants shows that specificity is governed by two inner loops, CBL1 and CBL2, involved in calcium binding as well as by three outer loops, L1, L2, and L3. In summary, our study provides the structural basis for promiscuity and specificity of Epa adhesins, which might further contribute to developing anti-adhesive antimycotics and combating Candida colonization.

SUBMITTER: Maestre-Reyna M 

PROVIDER: S-EPMC3479469 | biostudies-literature | 2012 Oct

REPOSITORIES: biostudies-literature

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Structural basis for promiscuity and specificity during Candida glabrata invasion of host epithelia.

Maestre-Reyna Manuel M   Diderrich Rike R   Veelders Maik Stefan MS   Eulenburg Georg G   Kalugin Vitali V   Brückner Stefan S   Keller Petra P   Rupp Steffen S   Mösch Hans-Ulrich HU   Essen Lars-Oliver LO  

Proceedings of the National Academy of Sciences of the United States of America 20121003 42


The human pathogenic yeast Candida glabrata harbors more than 20 surface-exposed, epithelial adhesins (Epas) for host cell adhesion. The Epa family recognizes host glycans and discriminates between target tissues by their adhesin (A) domains, but a detailed structural basis for ligand-binding specificity of Epa proteins has been lacking so far. In this study, we provide high-resolution crystal structures of the Epa1A domain in complex with different carbohydrate ligands that reveal how host cell  ...[more]

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