title: Human ZG16p recognizes pathogenic fungi through non-self polyvalent mannose in the digestive system.
abstract: 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 glycan-binding specificity of ZG16p by recently developed glycoconjugate microarray. ZG16p appeared to exhibit selective binding to α- and β-linked mannose-polyacrylamide-biotin probes. In more quantitative analysis using frontal affinity chromatography, dissociation constants to two types of polyvalent mannose, i.e. high-density mannose and yeast mannan, were determined to be 1.3 and 1.7 µM, respectively. Mutation of the evolutionarily conserved amino acid Asp151, which is involved in sugar binding among the Jacalin-related lectins (JRLs), abolished binding activity to mannose. By immunohistochemical staining, ZG16p was specifically detected in mucus-secreting cells of the digestive system such as serosanguineous acinar cells of the parotid gland, acinar cells of the pancreas and goblet cells of the intestine. Finally, we showed that ZG16p recognizes pathogenic Candida and Malassezia species in a polyvalent mannose-dependent manner. We propose that ZG16p is a novel member of mannose-specific JRLs, which recognizes pathogenic fungi through non-self polyvalent mannose in the digestive system.
authors: Research Center for Medical Glycoscience, National Institute of Advanced Industrial Science and Technology (AIST), Central 2, 1-1-1 Umezono, Tsukuba, Ibaraki, Japan.
authors: Hiroaki
authors: H
authors: Tateno
authors: Rikio
authors: R
authors: Yabe
authors: Takashi
authors: T
authors: Sato
authors: Azusa
authors: A
authors: Shibazaki
authors: Toshihide
authors: T
authors: Shikanai
authors: Tohru
authors: T
authors: Gonoi
authors: Hisashi
authors: H
authors: Narimatsu
authors: Jun
authors: J
authors: Hirabayashi
mesh_terms: D001665:Binding Sites; D002175:Candida / Q000378:metabolism* / Q000472:pathogenicity; D002846:Chromatography, Affinity / Q000379:methods; D006801:Humans; D007413:Intestinal Mucosa / Q000378:metabolism; D007422:Intestines / Q000737:chemistry; D037102:Lectins / Q000235:genetics / Q000378:metabolism*; D008290:Malassezia / Q000378:metabolism* / Q000472:pathogenicity; D008358:Mannose / Q000737:chemistry / Q000378:metabolism*; D046228:Microarray Analysis / Q000379:methods; D009154:Mutation / Q000235:genetics; D010179:Pancreas / Q000737:chemistry / Q000378:metabolism*; D010306:Parotid Gland / Q000737:chemistry / Q000378:metabolism*; D017434:Protein Structure, Tertiary / Q000235:genetics; D011994:Recombinant Proteins / Q000235:genetics / Q000378:metabolism; D014018:Tissue Distribution
chemical_list: D037102:Lectins; D011994:Recombinant Proteins; C519401:ZG16 protein, human; D008358:Mannose