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Productive Entry Pathways of Human Rhinoviruses
Currently, complete or partial genome sequences of more than 150 human rhinovirus (HRV) isolates are known. Twelve species A use members of the low-density lipoprotein receptor family for cell entry, whereas the remaining HRV-A and all HRV-B bind ICAM-1. HRV-Cs exploit an unknown receptor. At least...
Autores principales: | , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Hindawi Publishing Corporation
2012
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3513715/ https://www.ncbi.nlm.nih.gov/pubmed/23227049 http://dx.doi.org/10.1155/2012/826301 |
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author | Fuchs, Renate Blaas, Dieter |
author_facet | Fuchs, Renate Blaas, Dieter |
author_sort | Fuchs, Renate |
collection | PubMed |
description | Currently, complete or partial genome sequences of more than 150 human rhinovirus (HRV) isolates are known. Twelve species A use members of the low-density lipoprotein receptor family for cell entry, whereas the remaining HRV-A and all HRV-B bind ICAM-1. HRV-Cs exploit an unknown receptor. At least all A and B type viruses depend on receptor-mediated endocytosis for infection. In HeLa cells, they are internalized mainly by a clathrin- and dynamin-dependent mechanism. Upon uptake into acidic compartments, the icosahedral HRV capsid expands by ~4% and holes open at the 2-fold axes, close to the pseudo-3-fold axes and at the base of the star-shaped dome protruding at the vertices. RNA-protein interactions are broken and new ones are established, the small internal myristoylated capsid protein VP4 is expelled, and amphipathic N-terminal sequences of VP1 become exposed. The now hydrophobic subviral particle attaches to the inner surface of endosomes and transfers its genomic (+) ssRNA into the cytosol. The RNA leaves the virus starting with the poly(A) tail at its 3′-end and passes through a membrane pore contiguous with one of the holes in the capsid wall. Alternatively, the endosome is disrupted and the RNA freely diffuses into the cytoplasm. |
format | Online Article Text |
id | pubmed-3513715 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2012 |
publisher | Hindawi Publishing Corporation |
record_format | MEDLINE/PubMed |
spelling | pubmed-35137152012-12-07 Productive Entry Pathways of Human Rhinoviruses Fuchs, Renate Blaas, Dieter Adv Virol Review Article Currently, complete or partial genome sequences of more than 150 human rhinovirus (HRV) isolates are known. Twelve species A use members of the low-density lipoprotein receptor family for cell entry, whereas the remaining HRV-A and all HRV-B bind ICAM-1. HRV-Cs exploit an unknown receptor. At least all A and B type viruses depend on receptor-mediated endocytosis for infection. In HeLa cells, they are internalized mainly by a clathrin- and dynamin-dependent mechanism. Upon uptake into acidic compartments, the icosahedral HRV capsid expands by ~4% and holes open at the 2-fold axes, close to the pseudo-3-fold axes and at the base of the star-shaped dome protruding at the vertices. RNA-protein interactions are broken and new ones are established, the small internal myristoylated capsid protein VP4 is expelled, and amphipathic N-terminal sequences of VP1 become exposed. The now hydrophobic subviral particle attaches to the inner surface of endosomes and transfers its genomic (+) ssRNA into the cytosol. The RNA leaves the virus starting with the poly(A) tail at its 3′-end and passes through a membrane pore contiguous with one of the holes in the capsid wall. Alternatively, the endosome is disrupted and the RNA freely diffuses into the cytoplasm. Hindawi Publishing Corporation 2012 2012-11-26 /pmc/articles/PMC3513715/ /pubmed/23227049 http://dx.doi.org/10.1155/2012/826301 Text en Copyright © 2012 R. Fuchs and D. Blaas. https://creativecommons.org/licenses/by/3.0/ This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Review Article Fuchs, Renate Blaas, Dieter Productive Entry Pathways of Human Rhinoviruses |
title | Productive Entry Pathways of Human Rhinoviruses |
title_full | Productive Entry Pathways of Human Rhinoviruses |
title_fullStr | Productive Entry Pathways of Human Rhinoviruses |
title_full_unstemmed | Productive Entry Pathways of Human Rhinoviruses |
title_short | Productive Entry Pathways of Human Rhinoviruses |
title_sort | productive entry pathways of human rhinoviruses |
topic | Review Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3513715/ https://www.ncbi.nlm.nih.gov/pubmed/23227049 http://dx.doi.org/10.1155/2012/826301 |
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