Structure of the membrane anchor of pestivirus glycoprotein E(rns), a long tilted amphipathic helix.

E(rns) is an essential virion glycoprotein with RNase activity that suppresses host cellular innate immune responses upon being partially secreted from the infected cells. Its unusual C-terminus plays multiple roles, as the amphiphilic helix acts as a membrane anchor, as a signal peptidase cleavage...

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Autores principales:	Daniel Aberle, Claudia Muhle-Goll, Jochen Bürck, Moritz Wolf, Sabine Reißer, Burkhard Luy, Wolfgang Wenzel, Anne S Ulrich, Gregor Meyers
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2014
Materias:	Immunologic diseases. Allergy RC581-607 Biology (General) QH301-705.5
Acceso en línea:	https://doaj.org/article/d8c7c5b4135d46a0b110c9e0d75db212
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spelling	oai:doaj.org-article:d8c7c5b4135d46a0b110c9e0d75db2122021-11-18T06:06:55ZStructure of the membrane anchor of pestivirus glycoprotein E(rns), a long tilted amphipathic helix.1553-73661553-737410.1371/journal.ppat.1003973https://doaj.org/article/d8c7c5b4135d46a0b110c9e0d75db2122014-02-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/24586172/?tool=EBIhttps://doaj.org/toc/1553-7366https://doaj.org/toc/1553-7374E(rns) is an essential virion glycoprotein with RNase activity that suppresses host cellular innate immune responses upon being partially secreted from the infected cells. Its unusual C-terminus plays multiple roles, as the amphiphilic helix acts as a membrane anchor, as a signal peptidase cleavage site, and as a retention/secretion signal. We analyzed the structure and membrane binding properties of this sequence to gain a better understanding of the underlying mechanisms. CD spectroscopy in different setups, as well as Monte Carlo and molecular dynamics simulations confirmed the helical folding and showed that the helix is accommodated in the amphiphilic region of the lipid bilayer with a slight tilt rather than lying parallel to the surface. This model was confirmed by NMR analyses that also identified a central stretch of 15 residues within the helix that is fully shielded from the aqueous layer, which is C-terminally followed by a putative hairpin structure. These findings explain the strong membrane binding of the protein and provide clues to establishing the E(rns) membrane contact, processing and secretion.Daniel AberleClaudia Muhle-GollJochen BürckMoritz WolfSabine ReißerBurkhard LuyWolfgang WenzelAnne S UlrichGregor MeyersPublic Library of Science (PLoS)articleImmunologic diseases. AllergyRC581-607Biology (General)QH301-705.5ENPLoS Pathogens, Vol 10, Iss 2, p e1003973 (2014)
institution	DOAJ
collection	DOAJ
language	EN
topic	Immunologic diseases. Allergy RC581-607 Biology (General) QH301-705.5
spellingShingle	Immunologic diseases. Allergy RC581-607 Biology (General) QH301-705.5 Daniel Aberle Claudia Muhle-Goll Jochen Bürck Moritz Wolf Sabine Reißer Burkhard Luy Wolfgang Wenzel Anne S Ulrich Gregor Meyers Structure of the membrane anchor of pestivirus glycoprotein E(rns), a long tilted amphipathic helix.
description	E(rns) is an essential virion glycoprotein with RNase activity that suppresses host cellular innate immune responses upon being partially secreted from the infected cells. Its unusual C-terminus plays multiple roles, as the amphiphilic helix acts as a membrane anchor, as a signal peptidase cleavage site, and as a retention/secretion signal. We analyzed the structure and membrane binding properties of this sequence to gain a better understanding of the underlying mechanisms. CD spectroscopy in different setups, as well as Monte Carlo and molecular dynamics simulations confirmed the helical folding and showed that the helix is accommodated in the amphiphilic region of the lipid bilayer with a slight tilt rather than lying parallel to the surface. This model was confirmed by NMR analyses that also identified a central stretch of 15 residues within the helix that is fully shielded from the aqueous layer, which is C-terminally followed by a putative hairpin structure. These findings explain the strong membrane binding of the protein and provide clues to establishing the E(rns) membrane contact, processing and secretion.
format	article
author	Daniel Aberle Claudia Muhle-Goll Jochen Bürck Moritz Wolf Sabine Reißer Burkhard Luy Wolfgang Wenzel Anne S Ulrich Gregor Meyers
author_facet	Daniel Aberle Claudia Muhle-Goll Jochen Bürck Moritz Wolf Sabine Reißer Burkhard Luy Wolfgang Wenzel Anne S Ulrich Gregor Meyers
author_sort	Daniel Aberle
title	Structure of the membrane anchor of pestivirus glycoprotein E(rns), a long tilted amphipathic helix.
title_short	Structure of the membrane anchor of pestivirus glycoprotein E(rns), a long tilted amphipathic helix.
title_full	Structure of the membrane anchor of pestivirus glycoprotein E(rns), a long tilted amphipathic helix.
title_fullStr	Structure of the membrane anchor of pestivirus glycoprotein E(rns), a long tilted amphipathic helix.
title_full_unstemmed	Structure of the membrane anchor of pestivirus glycoprotein E(rns), a long tilted amphipathic helix.
title_sort	structure of the membrane anchor of pestivirus glycoprotein e(rns), a long tilted amphipathic helix.
publisher	Public Library of Science (PLoS)
publishDate	2014
url	https://doaj.org/article/d8c7c5b4135d46a0b110c9e0d75db212
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Structure of the membrane anchor of pestivirus glycoprotein E(rns), a long tilted amphipathic helix.

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