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Mapping of the Lassa virus LAMP1 binding site reveals unique determinants not shared by other old world arenaviruses

Cell entry of many enveloped viruses occurs by engagement with cellular receptors, followed by internalization into endocytic compartments and pH-induced membrane fusion. A previously unnoticed step of receptor switching was found to be critical during cell entry of two devastating human pathogens:...

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Detalles Bibliográficos
Autores principales: Israeli, Hadar, Cohen-Dvashi, Hadas, Shulman, Anastasiya, Shimon, Amir, Diskin, Ron
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Public Library of Science 2017
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5423696/
https://www.ncbi.nlm.nih.gov/pubmed/28448640
http://dx.doi.org/10.1371/journal.ppat.1006337
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author Israeli, Hadar
Cohen-Dvashi, Hadas
Shulman, Anastasiya
Shimon, Amir
Diskin, Ron
author_facet Israeli, Hadar
Cohen-Dvashi, Hadas
Shulman, Anastasiya
Shimon, Amir
Diskin, Ron
author_sort Israeli, Hadar
collection PubMed
description Cell entry of many enveloped viruses occurs by engagement with cellular receptors, followed by internalization into endocytic compartments and pH-induced membrane fusion. A previously unnoticed step of receptor switching was found to be critical during cell entry of two devastating human pathogens: Ebola and Lassa viruses. Our recent studies revealed the functional role of receptor switching to LAMP1 for triggering membrane fusion by Lassa virus and showed the involvement of conserved histidines in this switching, suggesting that other viruses from this family may also switch to LAMP1. However, when we investigated viruses that are genetically close to Lassa virus, we discovered that they cannot bind LAMP1. A crystal structure of the receptor-binding module from Morogoro virus revealed structural differences that allowed mapping of the LAMP1 binding site to a unique set of Lassa residues not shared by other viruses in its family, illustrating a key difference in the cell-entry mechanism of Lassa virus that may contribute to its pathogenicity.
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spelling pubmed-54236962017-05-14 Mapping of the Lassa virus LAMP1 binding site reveals unique determinants not shared by other old world arenaviruses Israeli, Hadar Cohen-Dvashi, Hadas Shulman, Anastasiya Shimon, Amir Diskin, Ron PLoS Pathog Research Article Cell entry of many enveloped viruses occurs by engagement with cellular receptors, followed by internalization into endocytic compartments and pH-induced membrane fusion. A previously unnoticed step of receptor switching was found to be critical during cell entry of two devastating human pathogens: Ebola and Lassa viruses. Our recent studies revealed the functional role of receptor switching to LAMP1 for triggering membrane fusion by Lassa virus and showed the involvement of conserved histidines in this switching, suggesting that other viruses from this family may also switch to LAMP1. However, when we investigated viruses that are genetically close to Lassa virus, we discovered that they cannot bind LAMP1. A crystal structure of the receptor-binding module from Morogoro virus revealed structural differences that allowed mapping of the LAMP1 binding site to a unique set of Lassa residues not shared by other viruses in its family, illustrating a key difference in the cell-entry mechanism of Lassa virus that may contribute to its pathogenicity. Public Library of Science 2017-04-27 /pmc/articles/PMC5423696/ /pubmed/28448640 http://dx.doi.org/10.1371/journal.ppat.1006337 Text en © 2017 Israeli et al http://creativecommons.org/licenses/by/4.0/ This is an open access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/) , which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
spellingShingle Research Article
Israeli, Hadar
Cohen-Dvashi, Hadas
Shulman, Anastasiya
Shimon, Amir
Diskin, Ron
Mapping of the Lassa virus LAMP1 binding site reveals unique determinants not shared by other old world arenaviruses
title Mapping of the Lassa virus LAMP1 binding site reveals unique determinants not shared by other old world arenaviruses
title_full Mapping of the Lassa virus LAMP1 binding site reveals unique determinants not shared by other old world arenaviruses
title_fullStr Mapping of the Lassa virus LAMP1 binding site reveals unique determinants not shared by other old world arenaviruses
title_full_unstemmed Mapping of the Lassa virus LAMP1 binding site reveals unique determinants not shared by other old world arenaviruses
title_short Mapping of the Lassa virus LAMP1 binding site reveals unique determinants not shared by other old world arenaviruses
title_sort mapping of the lassa virus lamp1 binding site reveals unique determinants not shared by other old world arenaviruses
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5423696/
https://www.ncbi.nlm.nih.gov/pubmed/28448640
http://dx.doi.org/10.1371/journal.ppat.1006337
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