The Yersinia adhesin YadA collagen-binding domain structure is a novel left-handed parallel β-roll

Nummelin, Heli; Merckel, Michael C.; Leo, Jack C.; Lankinen, Hilkka; Skurnik, Mikael; Goldman, Adrian

doi:10.1038/sj.emboj.7600100

Cited by 172 publications

(223 citation statements)

References 67 publications

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“…Like YadA, the C-terminal region of all four Vomp is predicted to consist of a membrane anchor of four transmembrane ␤-strands and an ␣-helical internal region with a propensity to form coiled-coils (20). Most importantly, four repeats of the NSVAIG-S collagenbinding motifs in YadA (28,29) are found within the N-terminal half in VompA, VompB, and VompC (Figs. 3A and 7), followed by a conserved neck and stalk region.…”

Section: Vomp Family Members Have Conserved Motifs and Domains Presentmentioning

confidence: 99%

A family of variably expressed outer-membrane proteins (Vomp) mediates adhesion and autoaggregation in Bartonella quintana

Zhang

Chomel

Schau

et al. 2004

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

139

194

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Section: Vomp Family Members Have Conserved Motifs and Domains Presentmentioning

confidence: 99%

A family of variably expressed outer-membrane proteins (Vomp) mediates adhesion and autoaggregation in Bartonella quintana

Zhang

Chomel

Schau

et al. 2004

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

139

194

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“…The general repeat length is 14 residues, and each repeat consists of an outer and an inner β-strand, running perpendicularly to the fiber axis. The repeats stack to form continuous β-sheets running along the inner and outer faces of the β-helices (15). Like the heptads of coiled coils, individual repeats have a structure that is independent of their sequence, but short insertions and deletions of one or two residues are common and, in contrast to coiled coils, do not affect the overall structure.…”

Section: Structure Determination Of Sada Fragments and Reconstruction Ofmentioning

confidence: 99%

Complete fiber structures of complex trimeric autotransporter adhesins conserved in enterobacteria

Hartmann

Grin

Dunin-Horkawicz

et al. 2012

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

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Trimeric autotransporter adhesins (TAAs) are modular, highly repetitive surface proteins that mediate adhesion to host cells in a broad range of Gram-negative pathogens. Although their sizes may differ by more than one order of magnitude, they all follow the same basic head-stalk-anchor architecture, where the head mediates adhesion and autoagglutination, the stalk projects the head from the bacterial surface, and the anchor provides the export function and attaches the adhesin to the bacterial outer membrane after export is complete. In complex adhesins, head and stalk domains may alternate several times before the anchor is reached. Despite extensive sequence divergence, the structures of TAA domains are highly constrained, due to the tight interleaving of their constituent polypeptide chains. We have therefore taken a "domain dictionary" approach to characterize representatives for each domain type by X-ray crystallography and use these structures to reconstruct complete TAA fibers. With SadA from Salmonella enterica, EhaG from enteropathogenic Escherichia coli (EHEC), and UpaG from uropathogenic E. coli (UPEC), we present three representative structures of a complex adhesin that occur in a conserved genomic context in Enterobacteria and is essential in the infection process of uropathogenic E. coli. Our work proves the applicability of the dictionary approach to understanding the structure of a class of proteins that are otherwise poorly tractable by high-resolution methods and provides a basis for the rapid and detailed annotation of newly identified TAAs.coiled coil | β-layer

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“…It is not a trimeric straight fiber like protein, rather a folded and twisted molecule at the bacterial surface. A prototypical autotransporter such as Yersinia adhesion (YadA) and ubiquitous surface proteins (Usp) A1/A2 of M. catarrhalis appear as straight "lollipop" like structures consisting of a membrane-anchoring domain, a stalk and finally a head (Nummelin et al, 2004). On the other hand, some of the autotransporters may appear like a fibril, and thus may not be similar to a prototypical TAA (Cotter et al, 2005a).…”

Section: Discussionmentioning

confidence: 99%

Haemophilus influenzae surface fibril (Hsf) is a unique twisted hairpin-like trimeric autotransporter

Singh

Jubair

Mörgelin

et al. 2015

International Journal of Medical Microbiology

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The Haemophilus surface fibril (Hsf) is an extraordinary large (2413 amino acids) trimeric autotransporter, present in all encapsulated Haemophilus influenzae. It contributes to virulence by directly functioning as an adhesin. Furthermore, Hsf recruits the host factor vitronectin thereby inhibiting the host innate immune response resulting in enhanced survival in serum. Here we observed by electron microscopy that Hsf appears as an 100 nm long fibril at the bacterial surface albeit the length is approximately 200 nm according to a bioinformatics based model. To unveil this discrepancy, we denaturated Hsf at the surface of Hib by using guanidine hydrochloride (GuHCl). Partial denaturation induced in the presence of GuHCl unfolded the Hsf molecules, and resulted in an increased length of fibres in comparison to the native trimeric form. Importantly, our findings were also verified by E. coli expressing Hsf at its surface. In addition, a set of Hsf-specific peptide antibodies also indicated that the N-terminal of Hsf is located near the C-terminal at the base of the fibril. Taken together, our results demonstrated that Hsf is not a straight molecule but is folded and doubled over. This is the first report that provides the unique structural features of the trimeric autotransporter Hsf. Highlights Trimeric autotransporters are important virulence factors of Gram negative bacteria, and have a "lollipop-shape" structure or straight trimeric strand.  Haemophilus surface fibril is involved in adherence to host epithelium and for recruitment of vitronectin.  Here we show for the first time that Haemophilus surface fibril has a twisted hairpin-like structure.

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The Yersinia adhesin YadA collagen-binding domain structure is a novel left-handed parallel β-roll

Cited by 172 publications

References 67 publications

A family of variably expressed outer-membrane proteins (Vomp) mediates adhesion and autoaggregation in Bartonella quintana

A family of variably expressed outer-membrane proteins (Vomp) mediates adhesion and autoaggregation in Bartonella quintana

Complete fiber structures of complex trimeric autotransporter adhesins conserved in enterobacteria

Haemophilus influenzae surface fibril (Hsf) is a unique twisted hairpin-like trimeric autotransporter

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