Nucleotide sequence of the gene for a fibronectin-binding protein from Staphylococcus aureus: use of this peptide sequence in the synthesis of biologically active peptides.

• DOI: 10.1073/pnas.86.2.699
• Publication Date: 2006-05-31T11:05:40Z
• Authors: C Signäs; G Raucci; K Jönsson; P E Lindgren; G M Anantharamaiah; M Höök; M Lindberg
• Keywords: DNA, Bacterial; Staphylococcus aureus; 0303 health sciences; Base Sequence; Transcription, Genetic; Molecular Sequence Data; Bacterial Adhesion; Fibronectins; 3. Good health; 03 medical and health sciences; Receptors, Fibronectin; Amino Acid Sequence; Cloning, Molecular; Receptors, Immunologic; Peptides

Binding of cells Staphylococcus aureus to fibronectin, which may represent a mechanism host tissue adherence, involves fibronectin-receptor protein present on the bacterial surface. Cloning gene coding for staphylococcal fibronectin-binding and construction fusion with properties was previously reported from our laboratory. We have now sequenced deduced primary sequence protein. The resembles other cell-wall-associated proteins Gram-positive bacteria in that it (i) appears be anchored cell membrane via its C-terminal end, (ii) contains proline-rich repeating unit outside anchor, (iii) long (36-amino acid) signal at N terminus. activity has been localized domain composed 38-amino acid repeated completely three times partially fourth time; identity between sequences varies 42 87%. Three synthetic peptides mimicking structure each were constructed. All interacted as indicated by their ability inhibit binding fibronectin cells, whereas an unrelated 37-amino peptide showed no inhibitory activity.