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Structural basis for receptor recognition by New World hemorrhagic fever arenaviruses
New World hemorrhagic fever arenaviruses are rodent-borne agents that cause severe human disease. The GP1 subunit of the surface glycoprotein mediates cell attachment through transferrin receptor 1 (TfR1). We report the structure of Machupo virus (MACV) GP1 bound with human TfR1. Atomic details of t...
Autores principales: | , , , , |
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Formato: | Texto |
Lenguaje: | English |
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Nature Publishing Group US
2010
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2920743/ https://www.ncbi.nlm.nih.gov/pubmed/20208545 http://dx.doi.org/10.1038/nsmb.1772 |
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author | Abraham, Jonathan Corbett, Kevin D Farzan, Michael Choe, Hyeryun Harrison, Stephen C |
author_facet | Abraham, Jonathan Corbett, Kevin D Farzan, Michael Choe, Hyeryun Harrison, Stephen C |
author_sort | Abraham, Jonathan |
collection | PubMed |
description | New World hemorrhagic fever arenaviruses are rodent-borne agents that cause severe human disease. The GP1 subunit of the surface glycoprotein mediates cell attachment through transferrin receptor 1 (TfR1). We report the structure of Machupo virus (MACV) GP1 bound with human TfR1. Atomic details of the GP1-TfR1 interface clarify the importance of TfR1 residues implicated in New World arenavirus host specificity. Analysis of sequence variation among New World arenavirus GP1s and their host-species receptors, in light of the molecular structure, indicates determinants of viral zoonotic transmission. Infectivities of pseudoviruses in cells expressing mutated TfR1 confirm that contacts at the tip of the TfR1 apical domain determine the capacity of human TfR1 to mediate infection by particular New World arenaviruses. We propose that New World arenaviruses that are pathogenic to humans fortuitously acquired affinity for human TfR1 during adaptation to TfR1 of their natural hosts. SUPPLEMENTARY INFORMATION: The online version of this article (doi:10.1038/nsmb.1772) contains supplementary material, which is available to authorized users. |
format | Text |
id | pubmed-2920743 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2010 |
publisher | Nature Publishing Group US |
record_format | MEDLINE/PubMed |
spelling | pubmed-29207432010-10-01 Structural basis for receptor recognition by New World hemorrhagic fever arenaviruses Abraham, Jonathan Corbett, Kevin D Farzan, Michael Choe, Hyeryun Harrison, Stephen C Nat Struct Mol Biol Article New World hemorrhagic fever arenaviruses are rodent-borne agents that cause severe human disease. The GP1 subunit of the surface glycoprotein mediates cell attachment through transferrin receptor 1 (TfR1). We report the structure of Machupo virus (MACV) GP1 bound with human TfR1. Atomic details of the GP1-TfR1 interface clarify the importance of TfR1 residues implicated in New World arenavirus host specificity. Analysis of sequence variation among New World arenavirus GP1s and their host-species receptors, in light of the molecular structure, indicates determinants of viral zoonotic transmission. Infectivities of pseudoviruses in cells expressing mutated TfR1 confirm that contacts at the tip of the TfR1 apical domain determine the capacity of human TfR1 to mediate infection by particular New World arenaviruses. We propose that New World arenaviruses that are pathogenic to humans fortuitously acquired affinity for human TfR1 during adaptation to TfR1 of their natural hosts. SUPPLEMENTARY INFORMATION: The online version of this article (doi:10.1038/nsmb.1772) contains supplementary material, which is available to authorized users. Nature Publishing Group US 2010-03-07 2010 /pmc/articles/PMC2920743/ /pubmed/20208545 http://dx.doi.org/10.1038/nsmb.1772 Text en © Nature Publishing Group 2010 This article is made available via the PMC Open Access Subset for unrestricted research re-use and secondary analysis in any form or by any means with acknowledgement of the original source. These permissions are granted for the duration of the World Health Organization (WHO) declaration of COVID-19 as a global pandemic. |
spellingShingle | Article Abraham, Jonathan Corbett, Kevin D Farzan, Michael Choe, Hyeryun Harrison, Stephen C Structural basis for receptor recognition by New World hemorrhagic fever arenaviruses |
title | Structural basis for receptor recognition by New World hemorrhagic fever arenaviruses |
title_full | Structural basis for receptor recognition by New World hemorrhagic fever arenaviruses |
title_fullStr | Structural basis for receptor recognition by New World hemorrhagic fever arenaviruses |
title_full_unstemmed | Structural basis for receptor recognition by New World hemorrhagic fever arenaviruses |
title_short | Structural basis for receptor recognition by New World hemorrhagic fever arenaviruses |
title_sort | structural basis for receptor recognition by new world hemorrhagic fever arenaviruses |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2920743/ https://www.ncbi.nlm.nih.gov/pubmed/20208545 http://dx.doi.org/10.1038/nsmb.1772 |
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