The role of Staphylococcus aureus surface protein SasG in adherence and biofilm formation

Corrigan, Rebecca M.; Rigby, David L.; Handley, Pauline S.; Foster, Timothy J.

doi:10.1099/mic.0.2007/006676-0

Cited by 299 publications

(299 citation statements)

References 38 publications

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“…The formation of Aapmediated biofilm requires proteolytic cleavage of the N-terminal A domain (11). A similar processing pathway was proposed for SasG (9). However, recent findings indicated that the full-length protein exposed on the bacterial surface undergoes limited processing within B repeats (12).…”

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confidence: 99%

“…SasG variants with more than four repeats blocked the binding of S. aureus surface adhesins to their ligands; for example, the clumping factor B binding to cytokeratin and fibrinogen (9). It is therefore possible that a minimum number of repeats is required for projection of the biofilm forming domains beyond other surface proteins.…”

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confidence: 99%

“…Polysaccharide intercellular adhesin is also known as poly-N-acetyl-glucosamine and is synthesized by enzymes encoded on the icaADBC operon (7). Accumulation can occur independently of ica, instead relying on the expression of surface proteins such as accumulation-associated protein (Aap) (8) in S. epidermidis and S. aureus surface protein G (SasG) (9) in S. aureus.…”

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confidence: 99%

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Staphylococcal biofilm-forming protein has a contiguous rod-like structure

Gruszka

Wojdyla

Bingham

et al. 2012

Proc. Natl. Acad. Sci. U.S.A.

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Staphylococcus aureus and Staphylococcus epidermidis form communities (called biofilms) on inserted medical devices, leading to infections that affect many millions of patients worldwide and cause substantial morbidity and mortality. As biofilms are resistant to antibiotics, device removal is often required to resolve the infection. Thus, there is a need for new therapeutic strategies and molecular data that might assist their development. Surface proteins S. aureus surface protein G (SasG) and accumulation-associated protein ( S. epidermidis ) promote biofilm formation through their “B” regions. B regions contain tandemly arrayed G5 domains interspersed with approximately 50 residue sequences (herein called E) and have been proposed to mediate intercellular accumulation through Zn 2+ -mediated homodimerization. Although E regions are predicted to be unstructured, SasG and accumulation-associated protein form extended fibrils on the bacterial surface. Here we report structures of E–G5 and G5–E–G5 from SasG and biophysical characteristics of single and multidomain fragments. E sequences fold cooperatively and form interlocking interfaces with G5 domains in a head-to-tail fashion, resulting in a contiguous, elongated, monomeric structure. E and G5 domains lack a compact hydrophobic core, and yet G5 domain and multidomain constructs have thermodynamic stabilities only slightly lower than globular proteins of similar size. Zn 2+ does not cause SasG domains to form dimers. The work reveals a paradigm for formation of fibrils on the 100-nm scale and suggests that biofilm accumulation occurs through a mechanism distinct from the “zinc zipper.” Finally, formation of two domains by each repeat (as in SasG) might reduce misfolding in proteins when the tandem arrangement of highly similar sequences is advantageous.

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confidence: 99%

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confidence: 99%

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Staphylococcal biofilm-forming protein has a contiguous rod-like structure

Gruszka

Wojdyla

Bingham

et al. 2012

Proc. Natl. Acad. Sci. U.S.A.

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“…In general, pathogenicity and persistence of these infections are associated with biofilm forming capability. Many surface proteins are reported to be involved in biofilm formation such as SasG [14], FnBPA and FnBPB [15], and the biofilm-associated protein Bap [3]. The Bap protein is encoded by a 6831 bp long bap gene.…”

Section: Discussionmentioning

confidence: 99%

“…Spreading of Bap among staphylococci and the presence of homologous proteins among other pathogens suggest the urgent need of complete characterisation of such proteins. Apart from this, studying functioning and biophysical characterisation of Bap is warranted as various other surface proteins exhibit similar structural similarity, such as SasG [14], SasC [21] and accumulation-associated protein (Aap) [22,23] Bap is homologous to the accumulation-associated protein Aap, which mediates biofilm accumulation in S. epidermidis [23].…”

Section: Discussionmentioning

confidence: 99%