Journal article
Redirecting pore assembly of staphylococcal α-hemolysin by protein engineering
- Abstract:
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α-Hemolysin (αHL), a β-barrel pore-forming toxin (βPFT), is secreted as a water-soluble monomer by Staphylococcus aureus. Upon binding to receptors on target cell membranes, αHL assembles to form heptameric membrane-spanning pores. We have previously engineered αHL to create a protease-activatable toxin that is activated by site-specific proteolysis including by tumor proteases. In this study, we redesigned αHL so that it requires 2-fold activation on target cells through (i) binding to speci...
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- Publication status:
- Published
- Peer review status:
- Peer reviewed
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(Preview, Version of record, pdf, 6.0MB, Terms of use)
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- Publisher copy:
- 10.1021/acscentsci.8b00910
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Bibliographic Details
- Publisher:
- American Chemical Society
- Journal:
- ACS Central Science More from this journal
- Volume:
- 5
- Issue:
- 4
- Pages:
- 629-639
- Publication date:
- 2019-03-25
- DOI:
- EISSN:
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2374-7951
- ISSN:
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2374-7943
- Pmid:
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31041382
Item Description
- Language:
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English
- Keywords:
- Pubs id:
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pubs:995499
- UUID:
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uuid:7e1af29e-a741-475f-84ae-7723047e26fe
- Local pid:
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pubs:995499
- Source identifiers:
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995499
- Deposit date:
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2020-01-15
Terms of use
- Copyright holder:
- American Chemical Society
- Copyright date:
- 2019
- Notes:
- © 2019 American Chemical Society. This is an open access article published under an ACS AuthorChoice License, which permits copying and redistribution of the article or any adaptations for non-commercial purposes.
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