ena-STUDY-UNIVERSITY OF TROMSO-12-06-2017-11:43:22:440-1133
Studies of SdrD proteins of Staphylococcus  aureus
Staphylococcus aureus cell surface anchored Serine Aspartate repeat containing protein D (SdrD) is an essential virulence factor. Thus, polymorphisms within its sequences could influence its function.  The sdrD A region from 48 S. aureus isolates from healthy carriers were analysed and classified into seven variants. Variations in the sdrD A region were concentrated in the N2 and N3 subdomains. Sequence analysis of the entire sdrD gene of representative isolates revealed variations in the SD repeat and the EF motifs of the B repeat. Structural modelling indicates that there are no differences in the SdrD structure of the sdrD variants. Variable amino acid residues mapped onto the 3D structure revealed that the variations are surface located exist within the groove between the N2-N3 subdomains and distributed mainly on the N3 subdomain. However, the variation within SdrD showed no major differences in the adhesion to keratinocytes, aside from a significant difference between two variants. Our results provide evidence of variations across the different domains of SdrD from S. aureus strains isolated from healthy carriers.
Staphylococcus aureus cell surface anchored Serine Aspartate repeat containing protein D (SdrD) is an essential virulence factor. Thus, polymorphisms within its sequences could influence its function.  The sdrD A region from 48 S. aureus isolates from healthy carriers were analysed and classified into seven variants. Variations in the sdrD A region were concentrated in the N2 and N3 subdomains. Sequence analysis of the entire sdrD gene of representative isolates revealed variations in the SD repeat and the EF motifs of the B repeat. Structural modelling indicates that there are no differences in the SdrD structure of the sdrD variants. Variable amino acid residues mapped onto the 3D structure revealed that the variations are surface located exist within the groove between the N2-N3 subdomains and distributed mainly on the N3 subdomain. However, the variation within SdrD showed no major differences in the adhesion to keratinocytes, aside from a significant difference between two variants. Our results provide evidence of variations across the different domains of SdrD from S. aureus strains isolated from healthy carriers.