期刊
BIOCONJUGATE CHEMISTRY
卷 26, 期 12, 页码 2429-2434出版社
AMER CHEMICAL SOC
DOI: 10.1021/acs.bioconjchem.5b00485
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资金
- Ministry of Education, Culture and Science [024.001.035]
A new strategy is described for the modification of CCMV for loading of cargoes inside the viral capsid. Sortase A, an enzyme which is present in Gram-positive bacteria, was used to attach cargo to the glycine-tagged N-termini of several CCMV variants. We show that small molecules and proteins bearing a C-terminal LPETG-motif can be attached in this way. This method allows for the site-specific, covalent, and orthogonal modification of CCMV capsids in a mild fashion, leading to high encapsulation efficiencies. This strategy can easily be expanded to other types of cargoes, labeled with an LPETG-tag without altering protein function.
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