A novel mannose-containing sialoprotein adhesin involved in the binding of Candida albicans cells to DMBT1
A novel mannose-containing sialoprotein adhesin involved in the binding of Candida albicans cells to DMBT1
复制标题
一种新型含甘露糖唾液蛋白粘附素参与白色念珠菌细胞与 DMBT1 的结合
DOI:
10.1111/omi.12374
复制
发表时间:
2022
影响因子:
3.7
通讯作者:
Oho T
中科院分区:
文献类型:
--
作者:
Setoguchi D;Nagata E;Oho T
Candida albicanscolonizes the oral cavity and causes oral candidiasis and early childhood caries synergistically with cariogenicStreptococcus mutans. Colonization of oral tissues withC. albicansis 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 ofC. albicansto DMBT1 has not been examined. In this study, we investigated the binding ofC. albicansto DMBT1 and isolated the fungal components responsible for the binding.Candida albicansspecifically bound to DMBT1 and strongly bound to the peptide domain SRCRP2. Binding to SRCRP2 was inhibited byN‐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 inhibitedC. albicansbinding to SRCRP2. The localization of the 25‐kDa protein on the surface ofC. albicanscell 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 ofC. albicans. These results suggest that the isolated adhesin is localized on the surface ofC. albicanscell walls and that sialic acid and mannose residues in the adhesin play a significant role in the binding reaction.