Expression of the biofilm-associated protein interferes with host protein receptors of Staphylococcus aureus and alters the infective process

The adherence of Staphylococcus aureus to soluble proteins and extracellular-matrix components of the host is one of the key steps in the pathogenesis of staphylococcal infections. S. aureus presents a family of adhesins called MSCRAMMs (microbial surface components recognizing adhesive matrix molec...

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Detalles Bibliográficos
Autores: Cucarella, Carme, Tormo Más, María Ángeles, Knecht, Erwin, Amorena Zabalza, Beatriz, Lasa Uzcudun, Íñigo, Foster, Timothy J., Penadés, José R.
Tipo de recurso: artículo
Estado:Versión publicada
Fecha de publicación:2002
País:España
Institución:Universidad Pública de Navarra
Repositorio:Academica-e. Repositorio Institucional de la Universidad Pública de Navarra
OAI Identifier:oai:academica-e.unavarra.es:2454/32082
Acceso en línea:https://hdl.handle.net/2454/32082
Access Level:acceso abierto
Palabra clave:Biofilms
Staphylococcus aureus
Carrier Proteins
Descripción
Sumario:The adherence of Staphylococcus aureus to soluble proteins and extracellular-matrix components of the host is one of the key steps in the pathogenesis of staphylococcal infections. S. aureus presents a family of adhesins called MSCRAMMs (microbial surface components recognizing adhesive matrix molecules) that specifically recognize host matrix components. We examined the influence of biofilm-associated protein (Bap) expression on S. aureus adherence to host proteins, epithelial cell cultures, and mammary gland sections and on colonization of the mammary gland in an in vivo infection model. Bap-positive strain V329 showed lower adherence to immobilized fibrinogen and fibronectin than isogenic Bap-deficient strain m556. Bacterial adherence to histological sections of mammary gland and bacterial internalization into 293 cells were significantly lower in the Bap-positive strains. In addition, the Bap-negative strain showed significantly higher colonization in vivo of sheep mammary glands than the Bap-positive strain. Taken together, these results strongly suggest that the expression of the Bap protein interferes with functional properties of the MSCRAMM proteins, preventing initial bacterial attachment to host tissues and cellular internalization.