Periodicity in Attachment Organelle Revealed by Electron Cryotomography Suggests Conformational Changes in Gliding Mechanism of <named-content content-type="genus-species">Mycoplasma pneumoniae</named-content>

ABSTRACT Mycoplasma pneumoniae, a pathogenic bacterium, glides on host surfaces using a unique mechanism. It forms an attachment organelle at a cell pole as a protrusion comprised of knoblike surface structures and an internal core. Here, we analyzed the three-dimensional structure of the organelle...

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Autores principales:	Akihiro Kawamoto, Lisa Matsuo, Takayuki Kato, Hiroki Yamamoto, Keiichi Namba, Makoto Miyata
Formato:	article
Lenguaje:	EN
Publicado:	American Society for Microbiology 2016
Materias:	Microbiology QR1-502
Acceso en línea:	https://doaj.org/article/926e29bf2dba469292cd7cdc5e12b4cb
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spelling	oai:doaj.org-article:926e29bf2dba469292cd7cdc5e12b4cb2021-11-15T15:41:41ZPeriodicity in Attachment Organelle Revealed by Electron Cryotomography Suggests Conformational Changes in Gliding Mechanism of <named-content content-type="genus-species">Mycoplasma pneumoniae</named-content>10.1128/mBio.00243-162150-7511https://doaj.org/article/926e29bf2dba469292cd7cdc5e12b4cb2016-05-01T00:00:00Zhttps://journals.asm.org/doi/10.1128/mBio.00243-16https://doaj.org/toc/2150-7511ABSTRACT Mycoplasma pneumoniae, a pathogenic bacterium, glides on host surfaces using a unique mechanism. It forms an attachment organelle at a cell pole as a protrusion comprised of knoblike surface structures and an internal core. Here, we analyzed the three-dimensional structure of the organelle in detail by electron cryotomography. On the surface, knoblike particles formed a two-dimensional array, albeit with limited regularity. Analyses using a nonbinding mutant and an antibody showed that the knoblike particles correspond to a naplike structure that has been observed by negative-staining electron microscopy and is likely to be formed as a complex of P1 adhesin, the key protein for binding and gliding. The paired thin and thick plates feature a rigid hexagonal lattice and striations with highly variable repeat distances, respectively. The combination of variable and invariant structures in the internal core and the P1 adhesin array on the surface suggest a model in which axial extension and compression of the thick plate along a rigid thin plate is coupled with attachment to and detachment from the substrate during gliding. IMPORTANCE Human mycoplasma pneumonia, epidemic all over the world in recent years, is caused by a pathogenic bacterium, Mycoplasma pneumoniae. This tiny bacterium, about 2 µm in cell body length, glides on the surface of the human trachea to infect the host by binding to sialylated oligosaccharides, which are also the binding targets of influenza viruses. The mechanism of mycoplasmal gliding motility is not related to any other well-studied motility systems, such as bacterial flagella and cytoplasmic motor proteins. Here, we visualized the attachment organelle, a cellular architecture for gliding, three dimensionally by using electron cryotomography and other conventional methods. A possible gliding mechanism has been suggested based on the architectural images.Akihiro KawamotoLisa MatsuoTakayuki KatoHiroki YamamotoKeiichi NambaMakoto MiyataAmerican Society for MicrobiologyarticleMicrobiologyQR1-502ENmBio, Vol 7, Iss 2 (2016)
institution	DOAJ
collection	DOAJ
language	EN
topic	Microbiology QR1-502
spellingShingle	Microbiology QR1-502 Akihiro Kawamoto Lisa Matsuo Takayuki Kato Hiroki Yamamoto Keiichi Namba Makoto Miyata Periodicity in Attachment Organelle Revealed by Electron Cryotomography Suggests Conformational Changes in Gliding Mechanism of <named-content content-type="genus-species">Mycoplasma pneumoniae</named-content>
description	ABSTRACT Mycoplasma pneumoniae, a pathogenic bacterium, glides on host surfaces using a unique mechanism. It forms an attachment organelle at a cell pole as a protrusion comprised of knoblike surface structures and an internal core. Here, we analyzed the three-dimensional structure of the organelle in detail by electron cryotomography. On the surface, knoblike particles formed a two-dimensional array, albeit with limited regularity. Analyses using a nonbinding mutant and an antibody showed that the knoblike particles correspond to a naplike structure that has been observed by negative-staining electron microscopy and is likely to be formed as a complex of P1 adhesin, the key protein for binding and gliding. The paired thin and thick plates feature a rigid hexagonal lattice and striations with highly variable repeat distances, respectively. The combination of variable and invariant structures in the internal core and the P1 adhesin array on the surface suggest a model in which axial extension and compression of the thick plate along a rigid thin plate is coupled with attachment to and detachment from the substrate during gliding. IMPORTANCE Human mycoplasma pneumonia, epidemic all over the world in recent years, is caused by a pathogenic bacterium, Mycoplasma pneumoniae. This tiny bacterium, about 2 µm in cell body length, glides on the surface of the human trachea to infect the host by binding to sialylated oligosaccharides, which are also the binding targets of influenza viruses. The mechanism of mycoplasmal gliding motility is not related to any other well-studied motility systems, such as bacterial flagella and cytoplasmic motor proteins. Here, we visualized the attachment organelle, a cellular architecture for gliding, three dimensionally by using electron cryotomography and other conventional methods. A possible gliding mechanism has been suggested based on the architectural images.
format	article
author	Akihiro Kawamoto Lisa Matsuo Takayuki Kato Hiroki Yamamoto Keiichi Namba Makoto Miyata
author_facet	Akihiro Kawamoto Lisa Matsuo Takayuki Kato Hiroki Yamamoto Keiichi Namba Makoto Miyata
author_sort	Akihiro Kawamoto
title	Periodicity in Attachment Organelle Revealed by Electron Cryotomography Suggests Conformational Changes in Gliding Mechanism of <named-content content-type="genus-species">Mycoplasma pneumoniae</named-content>
title_short	Periodicity in Attachment Organelle Revealed by Electron Cryotomography Suggests Conformational Changes in Gliding Mechanism of <named-content content-type="genus-species">Mycoplasma pneumoniae</named-content>
title_full	Periodicity in Attachment Organelle Revealed by Electron Cryotomography Suggests Conformational Changes in Gliding Mechanism of <named-content content-type="genus-species">Mycoplasma pneumoniae</named-content>
title_fullStr	Periodicity in Attachment Organelle Revealed by Electron Cryotomography Suggests Conformational Changes in Gliding Mechanism of <named-content content-type="genus-species">Mycoplasma pneumoniae</named-content>
title_full_unstemmed	Periodicity in Attachment Organelle Revealed by Electron Cryotomography Suggests Conformational Changes in Gliding Mechanism of <named-content content-type="genus-species">Mycoplasma pneumoniae</named-content>
title_sort	periodicity in attachment organelle revealed by electron cryotomography suggests conformational changes in gliding mechanism of <named-content content-type="genus-species">mycoplasma pneumoniae</named-content>
publisher	American Society for Microbiology
publishDate	2016
url	https://doaj.org/article/926e29bf2dba469292cd7cdc5e12b4cb
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Periodicity in Attachment Organelle Revealed by Electron Cryotomography Suggests Conformational Changes in Gliding Mechanism of <named-content content-type="genus-species">Mycoplasma pneumoniae</named-content>

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