A bacterial ABC transporter enables import of mammalian host glycosaminoglycans

Abstract Glycosaminoglycans (GAGs), such as hyaluronan, chondroitin sulfate, and heparin, constitute mammalian extracellular matrices. The uronate and amino sugar residues in hyaluronan and chondroitin sulfate are linked by 1,3-glycoside bond, while heparin contains 1,4-glycoside bond. Some bacteria...

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Autores principales:	Sayoko Oiki, Bunzo Mikami, Yukie Maruyama, Kousaku Murata, Wataru Hashimoto
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2017
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/d0a201178fa540b4a7f653193036d871
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spelling	oai:doaj.org-article:d0a201178fa540b4a7f653193036d8712021-12-02T12:32:15ZA bacterial ABC transporter enables import of mammalian host glycosaminoglycans10.1038/s41598-017-00917-y2045-2322https://doaj.org/article/d0a201178fa540b4a7f653193036d8712017-04-01T00:00:00Zhttps://doi.org/10.1038/s41598-017-00917-yhttps://doaj.org/toc/2045-2322Abstract Glycosaminoglycans (GAGs), such as hyaluronan, chondroitin sulfate, and heparin, constitute mammalian extracellular matrices. The uronate and amino sugar residues in hyaluronan and chondroitin sulfate are linked by 1,3-glycoside bond, while heparin contains 1,4-glycoside bond. Some bacteria target GAGs as means of establishing colonization and/or infection, and bacterial degradation mechanisms of GAGs have been well characterized. However, little is known about the bacterial import of GAGs. Here, we show a GAG import system, comprised of a solute-binding protein (Smon0123)-dependent ATP-binding cassette (ABC) transporter, in the pathogenic Streptobacillus moniliformis. A genetic cluster responsible for depolymerization, degradation, and metabolism of GAGs as well as the ABC transporter system was found in the S. moniliformis genome. This bacterium degraded hyaluronan and chondroitin sulfate with an expression of the genetic cluster, while heparin repressed the bacterial growth. The purified recombinant Smon0123 exhibited an affinity with disaccharides generated from hyaluronan and chondroitin sulfate. X-ray crystallography indicated binding mode of Smon0123 to GAG disaccharides. The purified recombinant ABC transporter as a tetramer (Smon0121-Smon0122/Smon0120-Smon0120) reconstructed in liposomes enhanced its ATPase activity in the presence of Smon0123 and GAG disaccharides. This is the first report that has molecularly depicted a bacterial import system of both sulfated and non-sulfated GAGs.Sayoko OikiBunzo MikamiYukie MaruyamaKousaku MurataWataru HashimotoNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 7, Iss 1, Pp 1-16 (2017)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Sayoko Oiki Bunzo Mikami Yukie Maruyama Kousaku Murata Wataru Hashimoto A bacterial ABC transporter enables import of mammalian host glycosaminoglycans
description	Abstract Glycosaminoglycans (GAGs), such as hyaluronan, chondroitin sulfate, and heparin, constitute mammalian extracellular matrices. The uronate and amino sugar residues in hyaluronan and chondroitin sulfate are linked by 1,3-glycoside bond, while heparin contains 1,4-glycoside bond. Some bacteria target GAGs as means of establishing colonization and/or infection, and bacterial degradation mechanisms of GAGs have been well characterized. However, little is known about the bacterial import of GAGs. Here, we show a GAG import system, comprised of a solute-binding protein (Smon0123)-dependent ATP-binding cassette (ABC) transporter, in the pathogenic Streptobacillus moniliformis. A genetic cluster responsible for depolymerization, degradation, and metabolism of GAGs as well as the ABC transporter system was found in the S. moniliformis genome. This bacterium degraded hyaluronan and chondroitin sulfate with an expression of the genetic cluster, while heparin repressed the bacterial growth. The purified recombinant Smon0123 exhibited an affinity with disaccharides generated from hyaluronan and chondroitin sulfate. X-ray crystallography indicated binding mode of Smon0123 to GAG disaccharides. The purified recombinant ABC transporter as a tetramer (Smon0121-Smon0122/Smon0120-Smon0120) reconstructed in liposomes enhanced its ATPase activity in the presence of Smon0123 and GAG disaccharides. This is the first report that has molecularly depicted a bacterial import system of both sulfated and non-sulfated GAGs.
format	article
author	Sayoko Oiki Bunzo Mikami Yukie Maruyama Kousaku Murata Wataru Hashimoto
author_facet	Sayoko Oiki Bunzo Mikami Yukie Maruyama Kousaku Murata Wataru Hashimoto
author_sort	Sayoko Oiki
title	A bacterial ABC transporter enables import of mammalian host glycosaminoglycans
title_short	A bacterial ABC transporter enables import of mammalian host glycosaminoglycans
title_full	A bacterial ABC transporter enables import of mammalian host glycosaminoglycans
title_fullStr	A bacterial ABC transporter enables import of mammalian host glycosaminoglycans
title_full_unstemmed	A bacterial ABC transporter enables import of mammalian host glycosaminoglycans
title_sort	bacterial abc transporter enables import of mammalian host glycosaminoglycans
publisher	Nature Portfolio
publishDate	2017
url	https://doaj.org/article/d0a201178fa540b4a7f653193036d871
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_version_	1718394122764550144

A bacterial ABC transporter enables import of mammalian host glycosaminoglycans

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