
β‐Galactofuranoside glycoconjugates on conidia and conidiophores of Aspergillus niger
Author(s) -
Wallis Gregg L.F.,
Hemming Frank W.,
Peberdy John F.
Publication year - 2001
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.2001.tb10727.x
Subject(s) - glycoconjugate , epitope , conidium , microbiology and biotechnology , monoclonal antibody , biology , aspergillus niger , aspergillus fumigatus , galactose , blot , biochemistry , immunofluorescence , antigen , chemistry , antibody , botany , immunology , gene
Galactose in the furanoic conformation appears to be limited to bacteria and lower eukaryotes. Galactofuranoic (Gal f )‐containing glycoconjugates that occur in organisms pathogenic or allergenic to man are frequently antigenic and immunodominant. We have used an immunochemical approach, employing a monoclonal antibody that recognises Gal f epitopes, to investigate the presence of Gal f ‐containing glycoconjugates within conidia and conidiophores of Aspergillus niger . ELISA and immunofluorescence microscopy indicated that specific and saturable binding sites were found on both. Inhibition studies confirmed that this binding was to Gal f ‐containing glycoconjugates. Interestingly, the conidiophore heads were particularly rich in these glycoconjugates. Western blotting identified a Gal f glycoprotein of 150–200 kDa from disrupted conidia.