A novel mannose‐containing sialoprotein adhesin involved in the binding of Candida albicans cells to DMBT1

Candida albicans colonizes the oral cavity and causes oral candidiasis and early childhood caries synergistically with cariogenic Streptococcus mutans. Colonization of oral tissues with C. albicans is an essential step in the initiation of these infectious diseases. Deleted in malignant brain tumors...

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Bibliographic Details
Published in:Molecular oral microbiology 2022-08, Vol.37 (4), p.154-163
Main Authors: Setoguchi, Daisuke, Nagata, Emi, Oho, Takahiko
Format: Article
Language:English
Subjects:
adhesin
Adhesion
Binding
Brain tumors
Candida albicans
Candidiasis
Cell walls
Children
Dental caries
Dental enamel
DMBT1
DMBT1 protein
Enzyme-linked immunosorbent assay
Infectious diseases
Innate immunity
Lectins
Localization
Mannose
Microorganisms
Oral cavity
Proteins
Residues
Scavenger receptors
sialic acid
Sugar
surface localization
Teeth
Western blotting
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Summary:Candida albicans colonizes the oral cavity and causes oral candidiasis and early childhood caries synergistically with cariogenic Streptococcus mutans. Colonization of oral tissues with C. albicans is an essential step in the initiation of these infectious diseases. Deleted in malignant brain tumors 1 (DMBT1), also known as salivary agglutinin or gp‐340, belongs to the scavenger receptor cysteine‐rich (SRCR) superfamily and has important functions in innate immunity. In the oral cavity, DMBT1 causes microbial adherence to tooth enamel and oral mucosa surfaces, but the adherence of C. albicans to DMBT1 has not been examined. In this study, we investigated the binding of C. albicans to DMBT1 and isolated the fungal components responsible for the binding. Candida albicans specifically bound to DMBT1 and strongly bound to the peptide domain SRCRP2. Binding to SRCRP2 was inhibited by N‐acetylneuraminic acid and mannose and by lectins recognizing these sugars. The isolated component had a molecular mass of 25 kDa, contained sialic acid and mannose residues, and inhibited C. albicans binding to SRCRP2. The localization of the 25‐kDa protein on the surface of C. albicans cell walls was confirmed by immunostaining and a cell ELISA using an antiserum to the protein, and Western blotting revealed the presence of the 25‐kDa protein in the cell wall fraction of C. albicans. These results suggest that the isolated adhesin is localized on the surface of C. albicans cell walls and that sialic acid and mannose residues in the adhesin play a significant role in the binding reaction.
ISSN:2041-1006
2041-1014
DOI:10.1111/omi.12374