Adhesion of the human pathogen Sporothrix schenckii to several extracellular matrix proteins
The pathogenic fungus Sporothrix schenckii is the causative agent of sporotrichosis. This subcutaneous mycosis may disseminate in immunocompromised individuals and also affect several internal organs and tissues, most commonly the bone, joints and lung. Since adhesion is the first step involved with...
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Associação Brasileira de Divulgação Científica
1999-05-01
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Series: | Brazilian Journal of Medical and Biological Research |
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Online Access: | http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X1999000500020 |
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author | O.C. Lima C.C. Figueiredo B.A.S. Pereira M.G.P. Coelho V. Morandi L.M. Lopes-Bezerra |
author_facet | O.C. Lima C.C. Figueiredo B.A.S. Pereira M.G.P. Coelho V. Morandi L.M. Lopes-Bezerra |
author_sort | O.C. Lima |
collection | DOAJ |
description | The pathogenic fungus Sporothrix schenckii is the causative agent of sporotrichosis. This subcutaneous mycosis may disseminate in immunocompromised individuals and also affect several internal organs and tissues, most commonly the bone, joints and lung. Since adhesion is the first step involved with the dissemination of pathogens in the host, we have studied the interaction between S. schenckii and several extracellular matrix (ECM) proteins. The binding of two morphological phases of S. schenckii, yeast cells and conidia, to immobilized type II collagen, laminin, fibronectin, fibrinogen and thrombospondin was investigated. Poly (2-hydroxyethyl methacrylate) (poly-HEMA) was used as the negative control. Cell adhesion was assessed by ELISA with a rabbit anti-S. schenckii antiserum. The results indicate that both morphological phases of this fungus can bind significantly to type II collagen, fibronectin and laminin in comparison to the binding observed with BSA (used as blocking agent). The adhesion rate observed with the ECM proteins (type II collagen, fibronectin and laminin) was statistically significant (P<0.05) when compared to the adhesion obtained with BSA. No significant binding of conidia was observed to either fibrinogen or thrombospondin, but yeast cells did bind to the fibrinogen. Our results indicate that S. schenckii can bind to fibronectin, laminin and type II collagen and also show differences in binding capacity according to the morphological form of the fungus. |
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id | doaj.art-c55d72a7518145b7a9ef3363ca8c6382 |
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issn | 0100-879X 1414-431X |
language | English |
last_indexed | 2024-12-16T08:34:39Z |
publishDate | 1999-05-01 |
publisher | Associação Brasileira de Divulgação Científica |
record_format | Article |
series | Brazilian Journal of Medical and Biological Research |
spelling | doaj.art-c55d72a7518145b7a9ef3363ca8c63822022-12-21T22:37:47ZengAssociação Brasileira de Divulgação CientíficaBrazilian Journal of Medical and Biological Research0100-879X1414-431X1999-05-0132565110.1590/S0100-879X1999000500020Adhesion of the human pathogen Sporothrix schenckii to several extracellular matrix proteinsO.C. LimaC.C. FigueiredoB.A.S. PereiraM.G.P. CoelhoV. MorandiL.M. Lopes-BezerraThe pathogenic fungus Sporothrix schenckii is the causative agent of sporotrichosis. This subcutaneous mycosis may disseminate in immunocompromised individuals and also affect several internal organs and tissues, most commonly the bone, joints and lung. Since adhesion is the first step involved with the dissemination of pathogens in the host, we have studied the interaction between S. schenckii and several extracellular matrix (ECM) proteins. The binding of two morphological phases of S. schenckii, yeast cells and conidia, to immobilized type II collagen, laminin, fibronectin, fibrinogen and thrombospondin was investigated. Poly (2-hydroxyethyl methacrylate) (poly-HEMA) was used as the negative control. Cell adhesion was assessed by ELISA with a rabbit anti-S. schenckii antiserum. The results indicate that both morphological phases of this fungus can bind significantly to type II collagen, fibronectin and laminin in comparison to the binding observed with BSA (used as blocking agent). The adhesion rate observed with the ECM proteins (type II collagen, fibronectin and laminin) was statistically significant (P<0.05) when compared to the adhesion obtained with BSA. No significant binding of conidia was observed to either fibrinogen or thrombospondin, but yeast cells did bind to the fibrinogen. Our results indicate that S. schenckii can bind to fibronectin, laminin and type II collagen and also show differences in binding capacity according to the morphological form of the fungus.http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X1999000500020Sporothrix schenckiifibronectinlaminintype II collagenadhesion |
spellingShingle | O.C. Lima C.C. Figueiredo B.A.S. Pereira M.G.P. Coelho V. Morandi L.M. Lopes-Bezerra Adhesion of the human pathogen Sporothrix schenckii to several extracellular matrix proteins Brazilian Journal of Medical and Biological Research Sporothrix schenckii fibronectin laminin type II collagen adhesion |
title | Adhesion of the human pathogen Sporothrix schenckii to several extracellular matrix proteins |
title_full | Adhesion of the human pathogen Sporothrix schenckii to several extracellular matrix proteins |
title_fullStr | Adhesion of the human pathogen Sporothrix schenckii to several extracellular matrix proteins |
title_full_unstemmed | Adhesion of the human pathogen Sporothrix schenckii to several extracellular matrix proteins |
title_short | Adhesion of the human pathogen Sporothrix schenckii to several extracellular matrix proteins |
title_sort | adhesion of the human pathogen sporothrix schenckii to several extracellular matrix proteins |
topic | Sporothrix schenckii fibronectin laminin type II collagen adhesion |
url | http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X1999000500020 |
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