Human ZG16p recognizes pathogenic fungi through non-self polyvalent mannose in the digestive system

作者: Hiroaki Tateno , Rikio Yabe , Takashi Sato , Azusa Shibazaki , Toshihide Shikanai

DOI: 10.1093/GLYCOB/CWR130

关键词:

摘要: Human zymogen granule protein 16 (ZG16p) contains a Jacalin-like lectin domain, although its glycan-binding properties are not fully understood. Here, we screened the specificity of ZG16p by recently developed glycoconjugate microarray. appeared to exhibit selective binding α- and β-linked mannose-polyacrylamide-biotin probes. In more quantitative analysis using frontal affinity chromatography, dissociation constants two types polyvalent mannose, i.e. high-density mannose yeast mannan, were determined be 1.3 1.7 µM, respectively. Mutation evolutionarily conserved amino acid Asp151, which is involved in sugar among Jacalin-related lectins (JRLs), abolished activity mannose. By immunohistochemical staining, was specifically detected mucus-secreting cells digestive system such as serosanguineous acinar parotid gland, pancreas goblet intestine. Finally, showed that recognizes pathogenic Candida Malassezia species mannose-dependent manner. We propose novel member mannose-specific JRLs, fungi through non-self system.

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