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Structural and functional analysis of the N-terminal domain of the Streptococcus gordonii adhesin Sgo0707

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.

Identiferoai:union.ndltd.org:UPSALLA1/oai:DiVA.org:umu-71563
Date January 2013
CreatorsNylander, Åsa, Svensäter, Gunnel, Senadheera, Dilani B., Cvitkovitch, Dennis G., Davies, Julia R., Persson, Karina
PublisherUmeå universitet, Oral mikrobiologi, Umeå universitet, Kemiska institutionen, Malmö Högskola, University of Toronto, University of Toronto, Malmö Högskola, Public Library Science
Source SetsDiVA Archive at Upsalla University
LanguageEnglish
Detected LanguageEnglish
TypeArticle in journal, info:eu-repo/semantics/article, text
Formatapplication/pdf
Rightsinfo:eu-repo/semantics/openAccess
RelationPLoS ONE, 1932-6203, 2013, 8:5, s. e63768-

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