title: Beta 1,4-oligoglucosides inhibit the binding of Aspergillus fumigatus conidia to human monocytes.
abstract: The binding of Aspergillus fumigatus conidia to human monocytes is mediated by a barley beta-glucan-inhibitable receptor. The simplest linkages in this glucan are present in the disaccharides laminaribiose (beta 1,3) and cellobiose (beta 1,4). Although laminaribiose gave strong inhibition of conidial binding to monocytes, cellobiose and oligosaccharides with beta 1,4-linked glucose residues were more potent as specific inhibitors of this binding over similar concentrations. Increasing the number of beta 1,4-linked glucose residues led to greater inhibition of conidial binding by human monocytes.
authors.affiliation: Clinical Mycology Section, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892.
authors.forename: V L
authors.initials: VL
authors.lastname: Kan
authors.forename: J E
authors.initials: JE
authors.lastname: Bennett
mesh_terms: D001232:Aspergillus fumigatus / Q000187:drug effects / Q000378:metabolism*; D002475:Cellobiose / Q000494:pharmacology; D004187:Disaccharides; D005936:Glucans / Q000494:pharmacology*; D005947:Glucose / Q000494:pharmacology; D005960:Glucosides / Q000494:pharmacology*; D006801:Humans; D008757:Methylglucosides / Q000494:pharmacology; D009000:Monocytes / Q000187:drug effects / Q000378:metabolism*
chemical_list: D004187:Disaccharides; D005936:Glucans; D005960:Glucosides; D008757:Methylglucosides; C014637:laminaribiose; D002475:Cellobiose; C027020:methylglucoside; D005947:Glucose