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Unnatural Amino Acid Incorporation into Virus-Like Particles

Strable, Erica and Prasuhn, Duane E. and Udit, Andrew K. and Brown, Steven and Link, A. James and Ngo, John T. and Lander, Gabriel and Quispe, Joel and Potter, Clinton S. and Carragher, Bridget and Tirrell, David A. and Finn, M. G. (2008) Unnatural Amino Acid Incorporation into Virus-Like Particles. Bioconjugate Chemistry, 19 (4). pp. 866-875. ISSN 1043-1802. PMCID PMC2713011. https://resolver.caltech.edu/CaltechAUTHORS:20150107-082245467

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Abstract

Virus-like particles composed of hepatitis B virus (HBV) or bacteriophage Qβ capsid proteins have been labeled with azide- or alkyne-containing unnatural amino acids by expression in a methionine auxotrophic strain of E. coli. The substitution does not affect the ability of the particles to self-assemble into icosahedral structures indistinguishable from native forms. The azide and alkyne groups were addressed by Cu(I)-catalyzed [3 + 2] cycloaddition: HBV particles were decomposed by the formation of more than 120 triazole linkages per capsid in a location-dependent manner, whereas Qβ suffered no such instability. The marriage of these well-known techniques of sense-codon reassignment and bioorthogonal chemical coupling provides the capability to construct polyvalent particles displaying a wide variety of functional groups with near-perfect control of spacing.


Item Type:Article
Related URLs:
URLURL TypeDescription
http://dx.doi.org/10.1021/bc700390rDOIArticle
http://pubs.acs.org/doi/abs/10.1021/bc700390rPublisherArticle
http://pubs.acs.org/doi/suppl/10.1021/bc700390r/suppl_file/bc700390r-file002.pdfPublisherSupporting Information
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2713011/PubMed CentralArticle
ORCID:
AuthorORCID
Tirrell, David A.0000-0003-3175-4596
Additional Information:© 2008 American Chemical Society Received October 21, 2007; Revised Manuscript Received January 14, 2008 This work was supported by the NIH (AI056013, RR021886, GM62523), the David & Lucille Packard Foundation Interdisciplinary Science Program, and the Canadian Institutes of Health Research (postdoctoral fellowship to A.K.U.). Cryo-electron microscopy was performed at the National Resource for Automated Molecular Microscopy which is supported by the NIH NCRR P41 program (RR17573).
Funders:
Funding AgencyGrant Number
NIHAI056013
NIHRR021886
NIHGM62523
David and Lucile Packard FoundationUNSPECIFIED
Canadian Institutes of Health ResearchUNSPECIFIED
NIHRR17573
Issue or Number:4
PubMed Central ID:PMC2713011
Record Number:CaltechAUTHORS:20150107-082245467
Persistent URL:https://resolver.caltech.edu/CaltechAUTHORS:20150107-082245467
Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:53231
Collection:CaltechAUTHORS
Deposited By: Anne Hormann
Deposited On:07 Jan 2015 17:15
Last Modified:03 Oct 2019 07:48

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