Making Contact: VAP Targeting by Intracellular Pathogens
In naïve cells, the endoplasmic reticulum (ER) and the ER-resident V esicle-associated membrane protein- A ssociated P roteins (VAP) are common components of sites of membrane contacts that mediate the nonvesicular transfer of lipids between organelles. There is increasing recognition that the hijac...
| Main Authors: | , |
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| Format: | Article |
| Language: | English |
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SAGE Publishing
2018-05-01
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| Series: | Contact |
| Online Access: | https://doi.org/10.1177/2515256418775512 |
| _version_ | 1797679710650499072 |
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| author | Rebecca Murray Isabelle Derré |
| author_facet | Rebecca Murray Isabelle Derré |
| author_sort | Rebecca Murray |
| collection | DOAJ |
| description | In naïve cells, the endoplasmic reticulum (ER) and the ER-resident V esicle-associated membrane protein- A ssociated P roteins (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. |
| first_indexed | 2024-03-11T23:18:50Z |
| format | Article |
| id | doaj.art-ac9e9bb444424ee4b23367c3d95a1548 |
| institution | Directory Open Access Journal |
| issn | 2515-2564 |
| language | English |
| last_indexed | 2024-03-11T23:18:50Z |
| publishDate | 2018-05-01 |
| publisher | SAGE Publishing |
| record_format | Article |
| series | Contact |
| spelling | doaj.art-ac9e9bb444424ee4b23367c3d95a15482023-09-20T17:03:21ZengSAGE PublishingContact2515-25642018-05-01110.1177/2515256418775512Making Contact: VAP Targeting by Intracellular PathogensRebecca MurrayIsabelle DerréIn naïve cells, the endoplasmic reticulum (ER) and the ER-resident V esicle-associated membrane protein- A ssociated P roteins (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.https://doi.org/10.1177/2515256418775512 |
| spellingShingle | Rebecca Murray Isabelle Derré Making Contact: VAP Targeting by Intracellular Pathogens Contact |
| 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 |
| url | https://doi.org/10.1177/2515256418775512 |
| work_keys_str_mv | AT rebeccamurray makingcontactvaptargetingbyintracellularpathogens AT isabellederre makingcontactvaptargetingbyintracellularpathogens |