Sortase A-Mediated N-Terminal Modification of Cowpea Chlorotic Mottle Virus for Highly Efficient Cargo Loading

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• 作者：Lise Schoonen ; Jan Pille ; Annika Borrmann ; Roeland J. M. Nolte ; Jan C. M. van Hest
• 刊名：Bioconjugate Chemistry
• 出版年：2015
• 出版时间：December 16, 2015
• 年：2015
• 卷：26
• 期：12
• 页码：2429-2434
• 全文大小：395K
• ISSN：1520-4812

文摘

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.