Structure of the collagen-binding domain from a Staphylococcus aureus adhesin

Symerský, J.; Patti, Joseph M.; Carson, M.; House-Pompeo, Karen; Teale, Michael; Moore, Dwight; Jin, Lei; Schneider, Amy; DeLucas, Lawrence J.; Höök, Magnus; Narayana, S.V.L.

doi:10.1038/nsb1097-833

Cited by 140 publications

(155 citation statements)

References 21 publications

Supporting

Mentioning

151

Contrasting

Order By: Relevance

“…A distinctive feature of the N-domain is the presence of 2 helices between strands B and C that partially cover one side of the core, whereas the C-domain uniquely contains an elongated ␤-ribbon, formed by strands S and T, running toward the M-domain. In contrast, the M-domain of SpaA has the CnaA fold, first seen in the N2 domain of S. aureus CnaA (14). This comprises 9 ␤-strands that form a partially open ␤-barrel.…”

Section: Resultsmentioning

confidence: 99%

The Corynebacterium diphtheriae shaft pilin SpaA is built of tandem Ig-like modules with stabilizing isopeptide and disulfide bonds

Kang

Paterson

Gaspar

et al. 2009

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

104

166

View full text Add to dashboard Cite

Cell-surface pili are important virulence factors that enable bacterial pathogens to adhere to specific host tissues and modulate host immune response. Relatively little is known about the structure of Gram-positive bacterial pili, which are built by the sortase-catalyzed covalent crosslinking of individual pilin proteins. Here we report the 1.6-Å resolution crystal structure of the shaft pilin component SpaA from Corynebacterium diphtheriae , revealing both common and unique features. The SpaA pilin comprises 3 tandem Ig-like domains, with characteristic folds related to those typically found in non-pilus adhesins. Whereas both the middle and the C-terminal domains contain an intramolecular Lys–Asn isopeptide bond, previously detected in the shaft pilins of Streptococcus pyogenes and Bacillus cereus , the middle Ig-like domain also harbors a calcium ion, and the C-terminal domain contains a disulfide bond. By mass spectrometry, we show that the SpaA monomers are cross-linked in the assembled pili by a Lys–Thr isopeptide bond, as predicted by previous genetic studies. Together, our results reveal that despite profound dissimilarities in primary sequences, the shaft pilins of Gram-positive pathogens have strikingly similar tertiary structures, suggesting a modular backbone construction, including stabilizing intermolecular and intramolecular isopeptide bonds.

show abstract

Section: Resultsmentioning

confidence: 99%

The Corynebacterium diphtheriae shaft pilin SpaA is built of tandem Ig-like modules with stabilizing isopeptide and disulfide bonds

Kang

Paterson

Gaspar

et al. 2009

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

104

166

View full text Add to dashboard Cite

show abstract

“…Further computational analyses were carried out to investigate the possible function of this domain using the Profunc server, also available at the European Bioinformatics Institute; this is a program developed to help assign a likely biochemical function of a protein based on its 3D structure. Interestingly, the highest score was observed for a collagen binding domain from a Staphylococcus aureus adhesin (PDB code 1amx) (33), with which the N2 domain exhibits 26.4% primary sequence identity; structure superimposition gave an RMSD of 1.7 Å (covering 55 out of the 84 residues). Such structural identity occurs between four ␤-strands of the N2 domain (␤1, ␤2, ␤4, and ␤5) that together comprise one ␤-sheet of the ␤-barrel (see Fig.…”

Section: Resultsmentioning

confidence: 99%

Group BStreptococcusPullulanase Crystal Structures in the Context of a Novel Strategy for Vaccine Development

et al. 2009

View full text Add to dashboard Cite

The group B streptococcus type I pullulanase (SAP) is a class 13 glycoside hydrolase that is anchored to the bacterial cell surface via a conserved C-terminal anchoring motif and involved in ␣-glucan degradation. Recent in vitro functional studies have shown that SAP is immunogenic in humans and that anti-SAP sera derived from immunized animals impair both group A and group B streptococcus pullulanase activities, suggesting that in vivo immunization with this antigen could prevent streptococcal colonization. To further investigate the putative role of SAP in bacterial pathogenesis, we carried out functional studies and found that recombinant SAP binds to human cervical epithelial cells. Furthermore, with a view of using SAP as a vaccine candidate, we present high-resolution crystal structure analyses of an N-terminally truncated form of SAP lacking the carbohydrate binding module but containing the catalytic domain and displaying glycosidase hydrolase activity, both in its apo form and in complex with maltotetraose, at resolutions of 2.1 and 2.4 Å, respectively.

show abstract

“…1). Recently, we determined the crystal structure of CBD19, which represents the smallest sub-fragment of the A domain with measurable collagenbinding activity (Symersky et al, 1997). Biochemical studies of the repeats of the B domain are in progress.…”

Section: Introductionmentioning

confidence: 99%

Crystallization and preliminary X-ray analysis of B-domain fragments of a Staphylococcus aureus collagen-binding protein

Deivanayagam

Rich

Danthuluri

et al. 1999

Acta Crystallogr D Biol Cryst

Self Cite

View full text Add to dashboard Cite

Structure of the collagen-binding domain from a Staphylococcus aureus adhesin

Cited by 140 publications

References 21 publications

The Corynebacterium diphtheriae shaft pilin SpaA is built of tandem Ig-like modules with stabilizing isopeptide and disulfide bonds

The Corynebacterium diphtheriae shaft pilin SpaA is built of tandem Ig-like modules with stabilizing isopeptide and disulfide bonds

Group BStreptococcusPullulanase Crystal Structures in the Context of a Novel Strategy for Vaccine Development

Crystallization and preliminary X-ray analysis of B-domain fragments of a Staphylococcus aureus collagen-binding protein

Contact Info

Product

Resources

About