Cryo-EM reveals new species-specific proteins and symmetry elements in the Legionella pneumophila Dot/Icm T4SS

Legionella pneumophila is an opportunistic pathogen that causes the potentially fatal pneumonia known as Legionnaires’ disease. The pathology associated with infection depends on bacterial delivery of effector proteins into the host via the membrane spanning Dot/Icm type IV secretion system (T4SS)....

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Autores principales:	Michael J Sheedlo, Clarissa L Durie, Jeong Min Chung, Louise Chang, Jacquelyn Roberts, Michele Swanson, Dana Borden Lacy, Melanie D Ohi
Formato:	article
Lenguaje:	EN
Publicado:	eLife Sciences Publications Ltd 2021
Materias:	Legionella pneumophila cryo-electron microscopy type IV secretion system Medicine R Science Q Biology (General) QH301-705.5
Acceso en línea:	https://doaj.org/article/769fbc40a033482aa6d6f369888cccee
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spelling	oai:doaj.org-article:769fbc40a033482aa6d6f369888cccee2021-12-01T10:57:16ZCryo-EM reveals new species-specific proteins and symmetry elements in the Legionella pneumophila Dot/Icm T4SS10.7554/eLife.704272050-084Xe70427https://doaj.org/article/769fbc40a033482aa6d6f369888cccee2021-09-01T00:00:00Zhttps://elifesciences.org/articles/70427https://doaj.org/toc/2050-084XLegionella pneumophila is an opportunistic pathogen that causes the potentially fatal pneumonia known as Legionnaires’ disease. The pathology associated with infection depends on bacterial delivery of effector proteins into the host via the membrane spanning Dot/Icm type IV secretion system (T4SS). We have determined sub-3.0 Å resolution maps of the Dot/Icm T4SS core complex by single particle cryo-EM. The high-resolution structural analysis has allowed us to identify proteins encoded outside the Dot/Icm genetic locus that contribute to the core T4SS structure. We can also now define two distinct areas of symmetry mismatch, one that connects the C18 periplasmic ring (PR) and the C13 outer membrane cap (OMC) and one that connects the C13 OMC with a 16-fold symmetric dome. Unexpectedly, the connection between the PR and OMC is DotH, with five copies sandwiched between the OMC and PR to accommodate the symmetry mismatch. Finally, we observe multiple conformations in the reconstructions that indicate flexibility within the structure.Michael J SheedloClarissa L DurieJeong Min ChungLouise ChangJacquelyn RobertsMichele SwansonDana Borden LacyMelanie D OhieLife Sciences Publications LtdarticleLegionella pneumophilacryo-electron microscopytype IV secretion systemMedicineRScienceQBiology (General)QH301-705.5ENeLife, Vol 10 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Legionella pneumophila cryo-electron microscopy type IV secretion system Medicine R Science Q Biology (General) QH301-705.5
spellingShingle	Legionella pneumophila cryo-electron microscopy type IV secretion system Medicine R Science Q Biology (General) QH301-705.5 Michael J Sheedlo Clarissa L Durie Jeong Min Chung Louise Chang Jacquelyn Roberts Michele Swanson Dana Borden Lacy Melanie D Ohi Cryo-EM reveals new species-specific proteins and symmetry elements in the Legionella pneumophila Dot/Icm T4SS
description	Legionella pneumophila is an opportunistic pathogen that causes the potentially fatal pneumonia known as Legionnaires’ disease. The pathology associated with infection depends on bacterial delivery of effector proteins into the host via the membrane spanning Dot/Icm type IV secretion system (T4SS). We have determined sub-3.0 Å resolution maps of the Dot/Icm T4SS core complex by single particle cryo-EM. The high-resolution structural analysis has allowed us to identify proteins encoded outside the Dot/Icm genetic locus that contribute to the core T4SS structure. We can also now define two distinct areas of symmetry mismatch, one that connects the C18 periplasmic ring (PR) and the C13 outer membrane cap (OMC) and one that connects the C13 OMC with a 16-fold symmetric dome. Unexpectedly, the connection between the PR and OMC is DotH, with five copies sandwiched between the OMC and PR to accommodate the symmetry mismatch. Finally, we observe multiple conformations in the reconstructions that indicate flexibility within the structure.
format	article
author	Michael J Sheedlo Clarissa L Durie Jeong Min Chung Louise Chang Jacquelyn Roberts Michele Swanson Dana Borden Lacy Melanie D Ohi
author_facet	Michael J Sheedlo Clarissa L Durie Jeong Min Chung Louise Chang Jacquelyn Roberts Michele Swanson Dana Borden Lacy Melanie D Ohi
author_sort	Michael J Sheedlo
title	Cryo-EM reveals new species-specific proteins and symmetry elements in the Legionella pneumophila Dot/Icm T4SS
title_short	Cryo-EM reveals new species-specific proteins and symmetry elements in the Legionella pneumophila Dot/Icm T4SS
title_full	Cryo-EM reveals new species-specific proteins and symmetry elements in the Legionella pneumophila Dot/Icm T4SS
title_fullStr	Cryo-EM reveals new species-specific proteins and symmetry elements in the Legionella pneumophila Dot/Icm T4SS
title_full_unstemmed	Cryo-EM reveals new species-specific proteins and symmetry elements in the Legionella pneumophila Dot/Icm T4SS
title_sort	cryo-em reveals new species-specific proteins and symmetry elements in the legionella pneumophila dot/icm t4ss
publisher	eLife Sciences Publications Ltd
publishDate	2021
url	https://doaj.org/article/769fbc40a033482aa6d6f369888cccee
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Cryo-EM reveals new species-specific proteins and symmetry elements in the Legionella pneumophila Dot/Icm T4SS

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