Refined Mechanism of <named-content content-type="genus-species">Mycoplasma mobile</named-content> Gliding Based on Structure, ATPase Activity, and Sialic Acid Binding of Machinery

ABSTRACT Mycoplasma mobile, a fish pathogen, glides on solid surfaces by repeated catch, pull, and release of sialylated oligosaccharides by a unique mechanism based on ATP energy. The gliding machinery is composed of huge surface proteins and an internal “jellyfish”-like structure. Here, we elucida...

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Autores principales:	Miyuki S. Nishikawa, Daisuke Nakane, Takuma Toyonaga, Akihiro Kawamoto, Takayuki Kato, Keiichi Namba, Makoto Miyata
Formato:	article
Lenguaje:	EN
Publicado:	American Society for Microbiology 2019
Materias:	electron microscopy electron cryotomography F-type ATPase/synthase image averaging sialylated oligosaccharide Microbiology QR1-502
Acceso en línea:	https://doaj.org/article/2ab87fabd6244236bae0cbad6a4621f0
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spelling	oai:doaj.org-article:2ab87fabd6244236bae0cbad6a4621f02021-11-15T15:54:45ZRefined Mechanism of <named-content content-type="genus-species">Mycoplasma mobile</named-content> Gliding Based on Structure, ATPase Activity, and Sialic Acid Binding of Machinery10.1128/mBio.02846-192150-7511https://doaj.org/article/2ab87fabd6244236bae0cbad6a4621f02019-12-01T00:00:00Zhttps://journals.asm.org/doi/10.1128/mBio.02846-19https://doaj.org/toc/2150-7511ABSTRACT Mycoplasma mobile, a fish pathogen, glides on solid surfaces by repeated catch, pull, and release of sialylated oligosaccharides by a unique mechanism based on ATP energy. The gliding machinery is composed of huge surface proteins and an internal “jellyfish”-like structure. Here, we elucidated the detailed three-dimensional structures of the machinery by electron cryotomography. The internal “tentacle”-like structure hydrolyzed ATP, which was consistent with the fact that the paralogs of the α- and β-subunits of F1-ATPase are at the tentacle structure. The electron microscopy suggested conformational changes of the tentacle structure depending on the presence of ATP analogs. The gliding machinery was isolated and showed that the binding activity to sialylated oligosaccharide was higher in the presence of ADP than in the presence of ATP. Based on these results, we proposed a model to explain the mechanism of M. mobile gliding. IMPORTANCE The genus Mycoplasma is made up of the smallest parasitic and sometimes commensal bacteria; Mycoplasma pneumoniae, which causes human “walking pneumonia,” is representative. More than ten Mycoplasma species glide on host tissues by novel mechanisms, always in the direction of the distal side of the machinery. Mycoplasma mobile, the fastest species in the genus, catches, pulls, and releases sialylated oligosaccharides (SOs), the carbohydrate molecules also targeted by influenza viruses, by means of a specific receptor and using ATP hydrolysis for energy. Here, the architecture of the gliding machinery was visualized three dimensionally by electron cryotomography (ECT), and changes in the structure and binding activity coupled to ATP hydrolysis were discovered. Based on the results, a refined mechanism was proposed for this unique motility.Miyuki S. NishikawaDaisuke NakaneTakuma ToyonagaAkihiro KawamotoTakayuki KatoKeiichi NambaMakoto MiyataAmerican Society for Microbiologyarticleelectron microscopyelectron cryotomographyF-type ATPase/synthaseimage averagingsialylated oligosaccharideMicrobiologyQR1-502ENmBio, Vol 10, Iss 6 (2019)
institution	DOAJ
collection	DOAJ
language	EN
topic	electron microscopy electron cryotomography F-type ATPase/synthase image averaging sialylated oligosaccharide Microbiology QR1-502
spellingShingle	electron microscopy electron cryotomography F-type ATPase/synthase image averaging sialylated oligosaccharide Microbiology QR1-502 Miyuki S. Nishikawa Daisuke Nakane Takuma Toyonaga Akihiro Kawamoto Takayuki Kato Keiichi Namba Makoto Miyata Refined Mechanism of <named-content content-type="genus-species">Mycoplasma mobile</named-content> Gliding Based on Structure, ATPase Activity, and Sialic Acid Binding of Machinery
description	ABSTRACT Mycoplasma mobile, a fish pathogen, glides on solid surfaces by repeated catch, pull, and release of sialylated oligosaccharides by a unique mechanism based on ATP energy. The gliding machinery is composed of huge surface proteins and an internal “jellyfish”-like structure. Here, we elucidated the detailed three-dimensional structures of the machinery by electron cryotomography. The internal “tentacle”-like structure hydrolyzed ATP, which was consistent with the fact that the paralogs of the α- and β-subunits of F1-ATPase are at the tentacle structure. The electron microscopy suggested conformational changes of the tentacle structure depending on the presence of ATP analogs. The gliding machinery was isolated and showed that the binding activity to sialylated oligosaccharide was higher in the presence of ADP than in the presence of ATP. Based on these results, we proposed a model to explain the mechanism of M. mobile gliding. IMPORTANCE The genus Mycoplasma is made up of the smallest parasitic and sometimes commensal bacteria; Mycoplasma pneumoniae, which causes human “walking pneumonia,” is representative. More than ten Mycoplasma species glide on host tissues by novel mechanisms, always in the direction of the distal side of the machinery. Mycoplasma mobile, the fastest species in the genus, catches, pulls, and releases sialylated oligosaccharides (SOs), the carbohydrate molecules also targeted by influenza viruses, by means of a specific receptor and using ATP hydrolysis for energy. Here, the architecture of the gliding machinery was visualized three dimensionally by electron cryotomography (ECT), and changes in the structure and binding activity coupled to ATP hydrolysis were discovered. Based on the results, a refined mechanism was proposed for this unique motility.
format	article
author	Miyuki S. Nishikawa Daisuke Nakane Takuma Toyonaga Akihiro Kawamoto Takayuki Kato Keiichi Namba Makoto Miyata
author_facet	Miyuki S. Nishikawa Daisuke Nakane Takuma Toyonaga Akihiro Kawamoto Takayuki Kato Keiichi Namba Makoto Miyata
author_sort	Miyuki S. Nishikawa
title	Refined Mechanism of <named-content content-type="genus-species">Mycoplasma mobile</named-content> Gliding Based on Structure, ATPase Activity, and Sialic Acid Binding of Machinery
title_short	Refined Mechanism of <named-content content-type="genus-species">Mycoplasma mobile</named-content> Gliding Based on Structure, ATPase Activity, and Sialic Acid Binding of Machinery
title_full	Refined Mechanism of <named-content content-type="genus-species">Mycoplasma mobile</named-content> Gliding Based on Structure, ATPase Activity, and Sialic Acid Binding of Machinery
title_fullStr	Refined Mechanism of <named-content content-type="genus-species">Mycoplasma mobile</named-content> Gliding Based on Structure, ATPase Activity, and Sialic Acid Binding of Machinery
title_full_unstemmed	Refined Mechanism of <named-content content-type="genus-species">Mycoplasma mobile</named-content> Gliding Based on Structure, ATPase Activity, and Sialic Acid Binding of Machinery
title_sort	refined mechanism of <named-content content-type="genus-species">mycoplasma mobile</named-content> gliding based on structure, atpase activity, and sialic acid binding of machinery
publisher	American Society for Microbiology
publishDate	2019
url	https://doaj.org/article/2ab87fabd6244236bae0cbad6a4621f0
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Refined Mechanism of <named-content content-type="genus-species">Mycoplasma mobile</named-content> Gliding Based on Structure, ATPase Activity, and Sialic Acid Binding of Machinery

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