Cas9 degradation in human cells using phage anti-CRISPR proteins
Zuriah Meacham, Luisa Arake de Tacca, Joseph Bondy-Denomy, David Rabuka, Michael Schelle · 2023
Read Cas9 degradation in human cells using phage anti-CRISPR proteins by Zuriah Meacham, Luisa Arake de Tacca, Joseph Bondy-Denomy, David Rabuka, Michael Schelle (2023) in the Tower of Babel, a free online library of public-domain works preserved in clean, searchable text. No sign-up. The full text is served as a plain-text file at a predictable URL, where text is present: https://antarctic-labs.com/tower-of-babel/pmc-10732428.txt.
Description
Zuriah Meacham and colleagues borrow a virus weapon to make the gene-editing enzyme Cas9 destroy itself in human cells, in this study from twenty twenty-three. Bacteria use CRISPR-Cas as immunity; the phages that hunt them answer with anti-CRISPR proteins. One of them, AcrIIA1, latches onto Cas9's cutting domain.
The surprise was what happened next in human cell culture: Cas9 vanished. The anti-CRISPR did not merely block the enzyme, it triggered its degradation, for both the common Streptococcus and Staphylococcus versions. Mutations that broke the physical grip between the two proteins abolished the effect, proving contact is required. A built-in self-destruct could one day limit how long Cas9 lingers in a patient, trimming off-target risk. The authors also sketch using the small, specific protein as the targeting half of designer protein-degradation drugs.
Catalog record
| CREATOR | Zuriah Meacham, Luisa Arake de Tacca, Joseph Bondy-Denomy, David Rabuka, Michael Schelle |
|---|---|
| YEAR | 2023 |
| COLLECTION | PAPERS |
| FORMAT | TXT |
| FILE SIZE | 21 KB |
| VERSION | 1.0 |
| LICENSE | CC BY 4.0 |
| RIGHTS | CC BY |
| SOURCE | Europe PMC |