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Description of a new group of variants of the Staphylococcus aureus elastin-binding protein that lacks an entire DNA segment of 180 bp

Autor: Campoccia D, Cangini I, Speziale P, MONTANARO, LUCIO, RAVAIOLI, STEFANO, ARCIOLA, CARLA RENATA

The elastin-binding protein (EbpS) is a microbial surface component recognizing adhesive matrix molecule (MSCRAM) found in Staphylococcus aureus that mediates bacterial cell binding to soluble elastin and tropoelastin. In scientific literature it is

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=od______4094::04c644d1c58554d9b95aec69a4f45b37
http://hdl.handle.net/11585/78286

Antibiotic multi-resistance strictly associated with IS256 and ica genes in Staphylococcus epidermidis strains from implant orthopedic infections

Autor: MONTANARO, LUCIO, RAVAIOLI, STEFANO, ARCIOLA, CARLA RENATA, Campoccia D, Pirini V, Otto M

In this study the presence both of the ica genes, encoding for biofilm exopolysaccharide production, and the insertion sequence IS256, a mobile element frequently associated to transposons, was investigated in relationship with the prevalence of anti

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=od______4094::fe06d5b073d703b4c9463ddc4f1d9c30
http://hdl.handle.net/11585/45583

Bacteria study of staphylococcus aureus adhesion on a novel nanostructured surface

Autor: Campoccia, D., Montanaro, L., Agheli, H., Sutherland, Duncan, Pirini, V., Giardino, R., Arciola, C.R.

Publikováno v: Campoccia, D, Montanaro, L, Agheli, H, Sutherland, D, Pirini, V, Giardino, R & Arciola, C R 2006, ' Bacteria study of staphylococcus aureus adhesion on a novel nanostructured surface ', International Journal of Artificial Organs, vol. 29, no. 6, pp. 622-629 .

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pure_au_____::f9f9284d20b82ad5e35894559958ece0
https://pure.au.dk/portal/da/publications/bacteria-study-of-staphylococcus-aureus-adhesion-on-a-novel-nanostructured-surface(07bbfc40-ba72-11db-bee9-02004c4f4f50).html