Recognition of extracellular matrix proteins by Paracoccidioides brasiliensis yeast cells

Angel Gonzalez, Beatriz L. Gomez, Angela Restrepo, Andrew John Hamilton, Luz Elena Cano

    Research output: Contribution to journalArticlepeer-review

    12 Scopus citations

    Abstract

    The adhesion of microorganism to host cells or extracellular matrix (ECM) proteins is the first step in the establishment of an infectious process. Interaction between Paracoccidioides brasiliensis yeast cells and ECM proteins has been previously noted. In vivo, in the chronic phase of experimental paracoccidioidomycosis (PCM), laminin and fibronectin have been detected on the surface of yeast cells located inside granulomatous lesions. The aim of the present study was to examine the ability of P. brasiliensis yeast cells to interact with extracellular matrix proteins (laminin, fibrinogen and fibronectin) and to establish which molecules were involved in this interaction. Immunofluorescence microscopy and flow cytometry demonstrated that all three ECM proteins tested were able to bind to the surface of P. brasiliensis yeast cells. Treatment with trypsin, chymotrypsin, chitinase, proteinase K or different sugars resulted in no change in laminin binding. In addition, ligand affinity assays were performed using different yeast extracts (total homogenates, β-mercaptoethanol, SDS extracts). These assays demonstrated the presence of 19 and 32-kDa proteins in the cell wall with the ability to bind to laminin, fibrinogen and fibronectin. This interaction could be important in mediating attachment of the fungus to host tissues and may consequently play a role in the pathogenesis of PCM.

    Original languageEnglish (US)
    Pages (from-to)637-645
    Number of pages9
    JournalMedical Mycology
    Volume43
    Issue number7
    DOIs
    StatePublished - Nov 2005

    All Science Journal Classification (ASJC) codes

    • Infectious Diseases

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