Metal-Ion-Induced Formation and Stabilization of Protein Cages Based on the Cowpea Chlorotic Mottle Virus

The cowpea chlorotic mottle virus (CCMV) is a versatile building block for the construction of nanoreactors and functional materials. Upon RNA removal, the capsid can be reversibly assembled and disassembed by adjusting the pH. At pH 5.0 the capsid is in the native assembled conformation, while at p...

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Bibliographic Details
Published in:	Small (Weinheim an der Bergstrasse, Germany) Vol. 7; no. 7; pp. 911 - 919
Main Authors:	Minten, Inge J., Wilke, Koos D. M., Hendriks, Linda J. A., van Hest, Jan C. M., Nolte, Roeland J. M., Cornelissen, Jeroen J. L. M.
Format:	Journal Article
Language:	English
Published:	Weinheim WILEY-VCH Verlag 04-04-2011 WILEY‐VCH Verlag
Subjects:	Bromovirus - chemistry Bromovirus - metabolism Capsid - chemistry Capsid - metabolism Capsid Proteins - chemistry CCMV Cowpea chlorotic mottle virus Hydrogen-Ion Concentration Metals - chemistry Models, Molecular nickel Nickel - chemistry protein engineering Protein Multimerization self-assembly supramolecular chemistry
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Summary:	The cowpea chlorotic mottle virus (CCMV) is a versatile building block for the construction of nanoreactors and functional materials. Upon RNA removal, the capsid can be reversibly assembled and disassembed by adjusting the pH. At pH 5.0 the capsid is in the native assembled conformation, while at pH 7.5 it disassembles into 90 capsid protein dimers. This special property enables the encapsulation of various molecules, such as protein and enzymes, but only at low pH. It is possible to stabilize the capsid at pH 7.5 by addition of negatively charged polyelectrolytes or negatively charged particles, but these methods all fill the interior of the capsid, leaving little or no space for other cargo molecules. This pH restriction therefore severely limits the range of enzymes that can be encapsulated, and hampers the investigation of the CCMV capsid as a nanoreactor for the study of enzymes in confined spaces. Herein, the interaction of N‐terminal histidine‐tag‐modified capsid proteins with several metal ions is reported. Depending on the conditions used, nanometer‐sized protein particles or capsidlike architectures are formed that are stable at pH 7.5. This metal‐mediated stabilization methodology is employed to form stable capsids containing multiple proteins at pH 7.5, thereby greatly expanding the scope of the CCMV capsid as a nanoreactor. The cowpea chlorotic mottle virus capsid, devoid of RNA, is stable at pH 5.0 but disassembles into dimers at pH 7.5. Capsid proteins modified with an N‐terminal histidine tag can be stabilized at pH 7.5 by the addition of nickel ions to the assembled capsids at pH 5.0, followed by dialysis to pH 7.5.
Bibliography:	ark:/67375/WNG-HFJ72GNG-W istex:9BD6C0F981261EC0ECC514BADDCED49FBD97D18F ArticleID:SMLL201001777 ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 ObjectType-Article-2 ObjectType-Feature-1
ISSN:	1613-6810 1613-6829 1613-6829
DOI:	10.1002/smll.201001777