Journal of Bacteriology, May 2001, p. 2888-2896, Vol. 183, No. 9
0021-9193/01/$04.00+0 DOI: 10.1128/JB.183.9.2888-2896.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.
Unit of Biochemistry, Department of Basic Biomedical Sciences, Cardenal Herrera-CEU University, 46113 Moncada, Valencia,1 and Instituto de Agrobiotecnología y Recursos Naturales and Departamento de Producción Agraria, Universidad Pública de Navarra-Consejo Superior de Investigaciones Científicas, Campus de Arrosadía, 31006 Pamplona,2 Spain
Received 20 October 2000/Accepted 7 February 2001
Identification of new genes involved in biofilm formation is needed to understand the molecular basis of strain variation and the pathogenic mechanisms implicated in chronic staphylococcal infections. A biofilm-producing Staphylococcus aureus isolate was used to generate biofilm-negative transposon (Tn917) insertion mutants. Two mutants were found with a significant decrease in attachment to inert surfaces (early adherence), intercellular adhesion, and biofilm formation. The transposon was inserted at the same locus in both mutants. This locus (bap [for biofilm associated protein]) encodes a novel cell wall associated protein of 2,276 amino acids (Bap), which shows global organizational similarities to surface proteins of gram-negative (Pseudomonas aeruginosa and Salmonella enterica serovar Typhi) and gram-positive (Enteroccocus faecalis) microorganisms. Bap's core region represents 52% of the protein and consists of 13 successive nearly identical repeats, each containing 86 amino acids. bap was present in a small fraction of bovine mastitis isolates (5% of the 350 S. aureus isolates tested), but it was absent from the 75 clinical human S. aureus isolates analyzed. All staphylococcal isolates harboring bap were highly adherent and strong biofilm producers. In a mouse infection model bap was involved in pathogenesis, causing a persistent infection.
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