title: Sialic acid-dependent recognition of laminin by Penicillium marneffei conidia.
abstract: Immunofluorescence microscopy demonstrated that laminin bound to the surface of Penicillium marneffei conidia. Attachment of P. marneffei conidia in an adherence assay was inhibited by soluble laminin and anti-laminin antibody. N-Acetylneuraminic acid abolished adherence, indicating an interaction mediated by a sialic acid-specific lectin.
authors.affiliation: Dunhill Dermatology Unit, St John's Institute of Dermatology, Guy's Hospital, London, United Kingdom. a.hamilton@umds.ac.uk
authors.forename: A J
authors.initials: AJ
authors.lastname: Hamilton
authors.forename: L
authors.initials: L
authors.lastname: Jeavons
authors.forename: S
authors.initials: S
authors.lastname: Youngchim
authors.forename: N
authors.initials: N
authors.lastname: Vanittanakom
authors.forename: R J
authors.initials: RJ
authors.lastname: Hay
mesh_terms: D002448:Cell Adhesion; D007797:Laminin / Q000378:metabolism*; D019158:N-Acetylneuraminic Acid / Q000378:metabolism*; D010407:Penicillium / Q000472:pathogenicity / Q000502:physiology*; D011485:Protein Binding; D013172:Spores, Fungal / Q000472:pathogenicity / Q000502:physiology*
chemical_list: D007797:Laminin; D019158:N-Acetylneuraminic Acid