Sialic acid-dependent recognition of laminin by Penicillium marneffei conidia

Infect Immun. 1998 Dec;66(12):6024-6. doi: 10.1128/IAI.66.12.6024-6026.1998.

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Cell Adhesion
  • Laminin / metabolism*
  • N-Acetylneuraminic Acid / metabolism*
  • Penicillium / pathogenicity
  • Penicillium / physiology*
  • Protein Binding
  • Spores, Fungal / pathogenicity
  • Spores, Fungal / physiology*

Substances

  • Laminin
  • N-Acetylneuraminic Acid