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The N‐terminal part of Als1 protein from Candida albicans specifically binds fucose‐containing glycans
Author(s) -
Donohue Dagmara S.,
Ielasi Francesco S.,
Goossens Katty V. Y.,
Willaert Ronnie G.
Publication year - 2011
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1111/j.1365-2958.2011.07676.x
Subject(s) - biology , fucose , glycan , biochemistry , glycoconjugate , candida albicans , fibronectin , surface plasmon resonance , lectin , plasma protein binding , fungal protein , binding protein , microbiology and biotechnology , glycoprotein , peptide sequence , extracellular matrix , materials science , nanoparticle , gene , nanotechnology
Summary The opportunistic pathogen Candida albicans expresses on its surface Als (Agglutinin like sequence) proteins, which play an important role in the adhesion to host cells and in the development of candidiasis. The binding specificity of these proteins is broad, as they can bind to various mammalian proteins, such as extracellular matrix proteins, and N‐ and E‐cadherins. The N‐terminal part of Als proteins constitutes the substrate‐specific binding domain and is responsible for attachment to epithelial and endothelial cells. We have used glycan array screening to identify possible glycan receptors for the binding domain of Als1p‐N. Under those conditions, Als1p‐N binds specifically to fucose‐containing glycans, which adds a lectin function to the functional diversity of the Als1 protein. The binding between Als1p‐N and BSA‐fucose glycoconjugate was quantitatively characterized using surface plasmon resonance, which demonstrated a weak millimolar affinity between Als1p‐N and fucose. Furthermore, we have also quantified the affinity of Als1p‐N to the extracellular matrix proteins proteins fibronectin and laminin, which is situated in the micromolar range. Surface plasmon resonance characterization of Als1p‐N–Als1p‐N interaction was in the micromolar affinity range.