Sialic acid-dependent recognition of laminin by Penicillium marneffei conidia.
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.
Hamilton
A J
AJ
Dunhill Dermatology Unit, St John's Institute of Dermatology, Guy's Hospital, London, United Kingdom. a.hamilton@umds.ac.uk
Jeavons
L
L
Youngchim
S
S
Vanittanakom
N
N
Hay
R J
RJ
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*
D007797:Laminin; D019158:N-Acetylneuraminic Acid