The commensal Streptococcus gordonii expresses numerous surface adhesins with which it interacts with other microorganisms, host cells and salivary proteins to initiate dental plaque formation. However, this Gram-positive bacterium can also spread to non-oral sites such as the heart valves and cause infective endocarditis. One of its surface adhesins, Sgo0707, is a large protein composed of a non-repetitive N-terminal region followed by several C-terminal repeat domains and a cell wall sorting motif. Here we present the crystal structure of the Sgo0707 N-terminal domains, refined to 2.1 Å resolution. The model consists of two domains, N1 and N2. The largest domain, N1, comprises a putative binding cleft with a single cysteine located in its centre and exhibits an unexpected structural similarity to the variable domains of the streptococcal Antigen I/II adhesins. The N2-domain has an IgG-like fold commonly found among Gram-positive surface adhesins. Binding studies performed on S. gordonii wild-type and a Sgo0707 deficient mutant show that the Sgo0707 adhesin is involved in binding to type-1 collagen and to oral keratinocytes.
| Identifer | oai:union.ndltd.org:UPSALLA1/oai:DiVA.org:umu-71563 |
| Date | January 2013 |
| Creators | Nylander, Åsa, Svensäter, Gunnel, Senadheera, Dilani B., Cvitkovitch, Dennis G., Davies, Julia R., Persson, Karina |
| Publisher | Umeå universitet, Oral mikrobiologi, Umeå universitet, Kemiska institutionen, Malmö Högskola, University of Toronto, University of Toronto, Malmö Högskola, Public Library Science |
| Source Sets | DiVA Archive at Upsalla University |
| Language | English |
| Detected Language | English |
| Type | Article in journal, info:eu-repo/semantics/article, text |
| Format | application/pdf |
| Rights | info:eu-repo/semantics/openAccess |
| Relation | PLoS ONE, 1932-6203, 2013, 8:5, s. e63768- |
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