Inositol hexakisphosphate-induced autoprocessing of large bacterial protein toxins.
Large bacterial protein toxins autotranslocate functional effector domains to the eukaryotic cell cytosol, resulting in alterations to cellular functions that ultimately benefit the infecting pathogen. Among these toxins, the clostridial glucosylating toxins (CGTs) produced by Gram-positive bacteria...
| Main Authors: | , |
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| Format: | Article |
| Language: | English |
| Published: |
Public Library of Science (PLoS)
2010-07-01
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| Series: | PLoS Pathogens |
| Online Access: | http://europepmc.org/articles/PMC2900308?pdf=render |
| _version_ | 1818552974829420544 |
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| author | Martina Egerer Karla J F Satchell |
| author_facet | Martina Egerer Karla J F Satchell |
| author_sort | Martina Egerer |
| collection | DOAJ |
| description | Large bacterial protein toxins autotranslocate functional effector domains to the eukaryotic cell cytosol, resulting in alterations to cellular functions that ultimately benefit the infecting pathogen. Among these toxins, the clostridial glucosylating toxins (CGTs) produced by Gram-positive bacteria and the multifunctional-autoprocessing RTX (MARTX) toxins of Gram-negative bacteria have distinct mechanisms for effector translocation, but a shared mechanism of post-translocation autoprocessing that releases these functional domains from the large holotoxins. These toxins carry an embedded cysteine protease domain (CPD) that is activated for autoprocessing by binding inositol hexakisphosphate (InsP(6)), a molecule found exclusively in eukaryotic cells. Thus, InsP(6)-induced autoprocessing represents a unique mechanism for toxin effector delivery specifically within the target cell. This review summarizes recent studies of the structural and molecular events for activation of autoprocessing for both CGT and MARTX toxins, demonstrating both similar and potentially distinct aspects of autoprocessing among the toxins that utilize this method of activation and effector delivery. |
| first_indexed | 2024-12-12T09:20:03Z |
| format | Article |
| id | doaj.art-994b9af51dc64fcaa54b3a6689b6b962 |
| institution | Directory Open Access Journal |
| issn | 1553-7366 1553-7374 |
| language | English |
| last_indexed | 2024-12-12T09:20:03Z |
| publishDate | 2010-07-01 |
| publisher | Public Library of Science (PLoS) |
| record_format | Article |
| series | PLoS Pathogens |
| spelling | doaj.art-994b9af51dc64fcaa54b3a6689b6b9622022-12-22T00:29:16ZengPublic Library of Science (PLoS)PLoS Pathogens1553-73661553-73742010-07-0167e100094210.1371/journal.ppat.1000942Inositol hexakisphosphate-induced autoprocessing of large bacterial protein toxins.Martina EgererKarla J F SatchellLarge bacterial protein toxins autotranslocate functional effector domains to the eukaryotic cell cytosol, resulting in alterations to cellular functions that ultimately benefit the infecting pathogen. Among these toxins, the clostridial glucosylating toxins (CGTs) produced by Gram-positive bacteria and the multifunctional-autoprocessing RTX (MARTX) toxins of Gram-negative bacteria have distinct mechanisms for effector translocation, but a shared mechanism of post-translocation autoprocessing that releases these functional domains from the large holotoxins. These toxins carry an embedded cysteine protease domain (CPD) that is activated for autoprocessing by binding inositol hexakisphosphate (InsP(6)), a molecule found exclusively in eukaryotic cells. Thus, InsP(6)-induced autoprocessing represents a unique mechanism for toxin effector delivery specifically within the target cell. This review summarizes recent studies of the structural and molecular events for activation of autoprocessing for both CGT and MARTX toxins, demonstrating both similar and potentially distinct aspects of autoprocessing among the toxins that utilize this method of activation and effector delivery.http://europepmc.org/articles/PMC2900308?pdf=render |
| spellingShingle | Martina Egerer Karla J F Satchell Inositol hexakisphosphate-induced autoprocessing of large bacterial protein toxins. PLoS Pathogens |
| title | Inositol hexakisphosphate-induced autoprocessing of large bacterial protein toxins. |
| title_full | Inositol hexakisphosphate-induced autoprocessing of large bacterial protein toxins. |
| title_fullStr | Inositol hexakisphosphate-induced autoprocessing of large bacterial protein toxins. |
| title_full_unstemmed | Inositol hexakisphosphate-induced autoprocessing of large bacterial protein toxins. |
| title_short | Inositol hexakisphosphate-induced autoprocessing of large bacterial protein toxins. |
| title_sort | inositol hexakisphosphate induced autoprocessing of large bacterial protein toxins |
| url | http://europepmc.org/articles/PMC2900308?pdf=render |
| work_keys_str_mv | AT martinaegerer inositolhexakisphosphateinducedautoprocessingoflargebacterialproteintoxins AT karlajfsatchell inositolhexakisphosphateinducedautoprocessingoflargebacterialproteintoxins |