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Retrograde transport pathways utilised by viruses and protein toxins
A model has been presented for retrograde transport of certain toxins and viruses from the cell surface to the ER that suggests an obligatory interaction with a glycolipid receptor at the cell surface. Here we review studies on the ER trafficking cholera toxin, Shiga and Shiga-like toxins, Pseudomon...
Autores principales: | , , , , |
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Formato: | Texto |
Lenguaje: | English |
Publicado: |
BioMed Central
2006
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1524934/ https://www.ncbi.nlm.nih.gov/pubmed/16603059 http://dx.doi.org/10.1186/1743-422X-3-26 |
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author | Spooner, Robert A Smith, Daniel C Easton, Andrew J Roberts, Lynne M Lord, J Michael |
author_facet | Spooner, Robert A Smith, Daniel C Easton, Andrew J Roberts, Lynne M Lord, J Michael |
author_sort | Spooner, Robert A |
collection | PubMed |
description | A model has been presented for retrograde transport of certain toxins and viruses from the cell surface to the ER that suggests an obligatory interaction with a glycolipid receptor at the cell surface. Here we review studies on the ER trafficking cholera toxin, Shiga and Shiga-like toxins, Pseudomonas exotoxin A and ricin, and compare the retrograde routes followed by these protein toxins to those of the ER trafficking SV40 and polyoma viruses. We conclude that there is in fact no obligatory requirement for a glycolipid receptor, nor even with a protein receptor in a lipid-rich environment. Emerging data suggests instead that there is no common pathway utilised for retrograde transport by all of these pathogens, the choice of route being determined by the particular receptor utilised. |
format | Text |
id | pubmed-1524934 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2006 |
publisher | BioMed Central |
record_format | MEDLINE/PubMed |
spelling | pubmed-15249342006-08-01 Retrograde transport pathways utilised by viruses and protein toxins Spooner, Robert A Smith, Daniel C Easton, Andrew J Roberts, Lynne M Lord, J Michael Virol J Review A model has been presented for retrograde transport of certain toxins and viruses from the cell surface to the ER that suggests an obligatory interaction with a glycolipid receptor at the cell surface. Here we review studies on the ER trafficking cholera toxin, Shiga and Shiga-like toxins, Pseudomonas exotoxin A and ricin, and compare the retrograde routes followed by these protein toxins to those of the ER trafficking SV40 and polyoma viruses. We conclude that there is in fact no obligatory requirement for a glycolipid receptor, nor even with a protein receptor in a lipid-rich environment. Emerging data suggests instead that there is no common pathway utilised for retrograde transport by all of these pathogens, the choice of route being determined by the particular receptor utilised. BioMed Central 2006-04-07 /pmc/articles/PMC1524934/ /pubmed/16603059 http://dx.doi.org/10.1186/1743-422X-3-26 Text en Copyright © 2006 Spooner et al; licensee BioMed Central Ltd. http://creativecommons.org/licenses/by/2.0 This is an Open Access article distributed under the terms of the Creative Commons Attribution License ( (http://creativecommons.org/licenses/by/2.0) ), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Review Spooner, Robert A Smith, Daniel C Easton, Andrew J Roberts, Lynne M Lord, J Michael Retrograde transport pathways utilised by viruses and protein toxins |
title | Retrograde transport pathways utilised by viruses and protein toxins |
title_full | Retrograde transport pathways utilised by viruses and protein toxins |
title_fullStr | Retrograde transport pathways utilised by viruses and protein toxins |
title_full_unstemmed | Retrograde transport pathways utilised by viruses and protein toxins |
title_short | Retrograde transport pathways utilised by viruses and protein toxins |
title_sort | retrograde transport pathways utilised by viruses and protein toxins |
topic | Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1524934/ https://www.ncbi.nlm.nih.gov/pubmed/16603059 http://dx.doi.org/10.1186/1743-422X-3-26 |
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