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Adhesion of the human pathogen Sporothrix schenckii to several extracellular matrix proteins

O C Lima1, C C Figueiredo, B A Pereira

  • 1Departamento de Biologia Celular e Genética, Instituto de Biologia Roberto Alcântara Gomes, Universidade do Estado do Rio de Janeiro, Brasil.

Brazilian Journal of Medical and Biological Research = Revista Brasileira De Pesquisas Medicas E Biologicas
|July 21, 1999
PubMed

Insights

Sporothrix schenckii, a fungus causing sporotrichosis, adheres to host extracellular matrix proteins like collagen, fibronectin, and laminin. This fungal adhesion varies between its yeast and conidia forms, impacting disease dissemination.

Area of Science:

  • Medical Mycology
  • Pathogen-Host Interactions
  • Biochemistry

Background:

  • Sporothrix schenckii causes sporotrichosis, a mycosis that can disseminate to internal organs, particularly in immunocompromised individuals.
  • Fungal adhesion to host tissues is a critical initial step in pathogen dissemination.
  • Understanding the interaction between S. schenckii and host extracellular matrix (ECM) proteins is crucial for elucidating disease mechanisms.

Purpose of the Study:

  • To investigate the binding capabilities of S. schenckii to various ECM proteins.
  • To compare the adhesion of different morphological phases of S. schenckii (yeast and conidia) to ECM components.
  • To identify specific ECM targets involved in S. schenckii adhesion and potential dissemination.

Main Methods:

  • Enzyme-Linked Immunosorbent Assay (ELISA) was employed to quantify the binding of S. schenckii yeast cells and conidia.
  • Immobilized ECM proteins including type II collagen, laminin, fibronectin, fibrinogen, and thrombospondin were used as substrates.
  • Poly (2-hydroxyethyl methacrylate) (poly-HEMA) served as a negative control, and Bovine Serum Albumin (BSA) as a blocking agent.

Main Results:

  • Both yeast cells and conidia of S. schenckii demonstrated significant binding to type II collagen, fibronectin, and laminin compared to BSA.
  • A statistically significant (P < 0.05) adhesion rate was observed for these ECM proteins.
  • While conidia showed no significant binding to fibrinogen or thrombospondin, yeast cells exhibited binding to fibrinogen.

Conclusions:

  • Sporothrix schenckii exhibits adhesive properties to key ECM proteins: fibronectin, laminin, and type II collagen.
  • The fungus displays differential binding affinities depending on its morphological form (yeast vs. conidia).
  • These findings highlight specific molecular interactions that likely contribute to the initial stages of sporotrichosis pathogenesis and dissemination.

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