FGL chaperone-assembled fimbrial polyadhesins: anti-immune armament of Gram-negative bacterial pathogens

Zavialov, Anton V.; Zav’yalova, Galina A.; Korpela, Timo; Zav’yalov, Vladimir P.

doi:10.1111/j.1574-6976.2007.00075.x

Cited by 68 publications

(106 citation statements)

References 187 publications

(556 reference statements)

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“…Members of FGL fimbriae such as Psa, F1, Saf, and Afa/Dr display either amorphous, capsule-like morphologies, or flexible polyadhesins, some consisting of a polymerized single type of adhesive subunits (4). Although sharing similar overall structures, the subunits from these fimbriae present functionally distinct characteristics.…”

Section: Discussionmentioning

confidence: 96%

“…Interestingly, many of the FGL-assembled structures are either not detectable by negative-stain electron microscopy (thus designated afimbrial or nonfimbrial adhesins) or appear as featureless electron-dense masses around the bacteria (4,7). Only in some studies were a few of these structures visualized as bacterial extensions (15,16) or as linear thin fimbriae (of ∼2-4 nm wide) that are mostly clumped together in small bundles (17,18).…”

mentioning

confidence: 99%

“…Psa belongs to the class of FGL (long F1-G1 loop) fimbriae and is a bacterial homopolymeric adhesin or polyadhesin (5). By contrast, the Afa/Dr and Saf polyadhesins of Escherichia coli and Salmonella enterica, respectively, all consist of a major multimeric adhesin and an additional tip-located invasin (4). In addition to Psa, the surface of Y. pestis also displays a homopolymeric structure known as the F1 capsule that is grouped with the FGL surface proteins and is assembled by the chaperone-usher pathway (4).…”

mentioning

confidence: 99%

“…The Psa of Y. pestis is a surface homopolymer made of the structural subunit PsaA that is assembled via the chaperoneusher pathway (4). Psa belongs to the class of FGL (long F1-G1 loop) fimbriae and is a bacterial homopolymeric adhesin or polyadhesin (5).…”

mentioning

confidence: 99%

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Structural basis for the specific recognition of dual receptors by the homopolymeric pH 6 antigen (Psa) fimbriae of Yersinia pestis

Bao

Nair

Tang

et al. 2012

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

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The pH 6 antigen (Psa) of Yersinia pestis consists of fimbriae that bind to two receptors: β1-linked galactosyl residues in glycosphingolipids and the phosphocholine group in phospholipids. Despite the ubiquitous presence of either moiety on the surface of many mammalian cells, Y. pestis appears to prefer interacting with certain types of human cells, such as macrophages and alveolar epithelial cells of the lung. The molecular mechanism of this apparent selectivity is not clear. Site-directed mutagenesis of the consensus choline-binding motif in the sequence of PsaA, the subunit of the Psa fimbrial homopolymer, identified residues that abolish galactosylceramide binding, phosphatidylcholine binding, or both. The crystal structure of PsaA in complex with both galactose and phosphocholine reveals separate receptor binding sites that share a common structural motif, thus suggesting a potential interaction between the two sites. Mutagenesis of this shared structural motif identified Tyr126, which is part of the choline-binding consensus sequence but is found in direct contact with the galactose in the structure of PsaA, important for both receptor binding. Thus, this structure depicts a fimbrial subunit that forms a polymeric adhesin with a unique arrangement of dual receptor binding sites. These findings move the field forward by providing insights into unique types of multiple receptor-ligand interactions and should steer research into the synthesis of dual receptor inhibitor molecules to slow down the rapid progression of plague.adhesin-receptor complex | adhesion | ligand binding | sugar binding | phosphocholine binding

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Section: Discussionmentioning

confidence: 96%

mentioning

confidence: 99%

mentioning

confidence: 99%

mentioning

confidence: 99%

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Structural basis for the specific recognition of dual receptors by the homopolymeric pH 6 antigen (Psa) fimbriae of Yersinia pestis

Bao

Nair

Tang

et al. 2012

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

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“…Один из них получил английское название «chaperone", которое переводится как "компаньон", "сопровождающее лицо", а в транскрипции -"шаперон", а второй ком-понент получил английское название "usher", ко-торое переводится как "швейцар", "привратник", в транскрипции -"ашер" [ [2,3,11,35], позволил нам открыть новое семейство фибриллярных адге-зинов, представляющих собой полимер одной или двух типов субъединиц, в каждой из которых рас-положен один или даже два независимых центра адгезии, специфичных к разным рецепторам клеток хозяина. Мы назвали это семейство органелл "фи-бриллярными полиадгезинами" или просто "поли-адгезинами" [49,50]. Полиадгезины собираются с помощью т. н.…”

Section: херсонский государственный университетunclassified

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2016

Ukr. ž. med. bìol. sportu

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Flow‐aligned, single‐shot fiber diffraction using a femtosecond X‐ray free‐electron laser

et al. 2017

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A major goal for X‐ray free‐electron laser (XFEL) based science is to elucidate structures of biological molecules without the need for crystals. Filament systems may provide some of the first single macromolecular structures elucidated by XFEL radiation, since they contain one‐dimensional translational symmetry and thereby occupy the diffraction intensity region between the extremes of crystals and single molecules. Here, we demonstrate flow alignment of as few as 100 filaments (Escherichia coli pili, F‐actin, and amyloid fibrils), which when intersected by femtosecond X‐ray pulses result in diffraction patterns similar to those obtained from classical fiber diffraction studies. We also determine that F‐actin can be flow‐aligned to a disorientation of approximately 5 degrees. Using this XFEL‐based technique, we determine that gelsolin amyloids are comprised of stacked β‐strands running perpendicular to the filament axis, and that a range of order from fibrillar to crystalline is discernable for individual α‐synuclein amyloids.

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FGL chaperone-assembled fimbrial polyadhesins: anti-immune armament of Gram-negative bacterial pathogens

Cited by 68 publications

References 187 publications

Structural basis for the specific recognition of dual receptors by the homopolymeric pH 6 antigen (Psa) fimbriae of Yersinia pestis

Structural basis for the specific recognition of dual receptors by the homopolymeric pH 6 antigen (Psa) fimbriae of Yersinia pestis

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Flow‐aligned, single‐shot fiber diffraction using a femtosecond X‐ray free‐electron laser

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