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Making Contact: VAP Targeting by Intracellular Pathogens
In naïve cells, the endoplasmic reticulum (ER) and the ER-resident Vesicle-associated membrane protein-Associated Proteins (VAP) are common components of sites of membrane contacts that mediate the nonvesicular transfer of lipids between organelles. There is increasing recognition that the hijacking...
Autores principales: | , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
SAGE Publications
2018
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6083021/ https://www.ncbi.nlm.nih.gov/pubmed/30101212 http://dx.doi.org/10.1177/2515256418775512 |
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author | Murray, Rebecca Derré, Isabelle |
author_facet | Murray, Rebecca Derré, Isabelle |
author_sort | Murray, Rebecca |
collection | PubMed |
description | In naïve cells, the endoplasmic reticulum (ER) and the ER-resident Vesicle-associated membrane protein-Associated Proteins (VAP) are common components of sites of membrane contacts that mediate the nonvesicular transfer of lipids between organelles. There is increasing recognition that the hijacking of VAP by intracellular pathogens is a novel mechanism of host–pathogen interaction. Here, we summarize our recent findings showing that the Chlamydia inclusion membrane protein IncV tethers the ER to the inclusion membrane by binding to VAP via the molecular mimicry of two eukaryotic FFAT motifs. We extend the discussion to other microorganisms that have evolved similar mechanisms. |
format | Online Article Text |
id | pubmed-6083021 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2018 |
publisher | SAGE Publications |
record_format | MEDLINE/PubMed |
spelling | pubmed-60830212018-08-09 Making Contact: VAP Targeting by Intracellular Pathogens Murray, Rebecca Derré, Isabelle Contact (Thousand Oaks) News and Views In naïve cells, the endoplasmic reticulum (ER) and the ER-resident Vesicle-associated membrane protein-Associated Proteins (VAP) are common components of sites of membrane contacts that mediate the nonvesicular transfer of lipids between organelles. There is increasing recognition that the hijacking of VAP by intracellular pathogens is a novel mechanism of host–pathogen interaction. Here, we summarize our recent findings showing that the Chlamydia inclusion membrane protein IncV tethers the ER to the inclusion membrane by binding to VAP via the molecular mimicry of two eukaryotic FFAT motifs. We extend the discussion to other microorganisms that have evolved similar mechanisms. SAGE Publications 2018-05-17 /pmc/articles/PMC6083021/ /pubmed/30101212 http://dx.doi.org/10.1177/2515256418775512 Text en © The Author(s) 2018 https://creativecommons.org/licenses/by-nc/4.0/Creative Commons Non Commercial CC BY-NC: This article is distributed under the terms of the Creative Commons Attribution-NonCommercial 4.0 License (https://creativecommons.org/licenses/by-nc/4.0/) which permits non-commercial use, reproduction and distribution of the work without further permission provided the original work is attributed as specified on the SAGE and Open Access pages (https://us.sagepub.com/en-us/nam/open-access-at-sage). |
spellingShingle | News and Views Murray, Rebecca Derré, Isabelle Making Contact: VAP Targeting by Intracellular Pathogens |
title | Making Contact: VAP Targeting by Intracellular Pathogens |
title_full | Making Contact: VAP Targeting by Intracellular Pathogens |
title_fullStr | Making Contact: VAP Targeting by Intracellular Pathogens |
title_full_unstemmed | Making Contact: VAP Targeting by Intracellular Pathogens |
title_short | Making Contact: VAP Targeting by Intracellular Pathogens |
title_sort | making contact: vap targeting by intracellular pathogens |
topic | News and Views |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6083021/ https://www.ncbi.nlm.nih.gov/pubmed/30101212 http://dx.doi.org/10.1177/2515256418775512 |
work_keys_str_mv | AT murrayrebecca makingcontactvaptargetingbyintracellularpathogens AT derreisabelle makingcontactvaptargetingbyintracellularpathogens |