File Download

There are no files associated with this item.

  Links for fulltext
     (May Require Subscription)
Supplementary

Article: Exploiting fluorescent polymers to probe the self-assembly of virus-like particles

TitleExploiting fluorescent polymers to probe the self-assembly of virus-like particles
Authors
Issue Date2011
PublisherAmerican Chemical Society. The Journal's web site is located at http://pubs.acs.org/journal/jpcbfk
Citation
The Journal of Physical Chemistry Part B: Condensed Matter, Materials, Surfaces, Interfaces & Biophysical, 2011, v. 115 n. 10, p. 2386-2391 How to Cite?
AbstractThe inside surfaces of the protein shells of many viruses are positively charged, thereby enhancing the self-assembly of capsid proteins around their (oppositely charged) RNA genome. These proteins have been shown to organize similarly around a variety of nonbiological, negatively charged, polymers, for example, poly(styrene sulfonate) (PSS), forming virus-like particles (VLPs). We have demonstrated recently that the VLPs formed from cowpea chlorotic mottle virus (CCMV) capsid protein increase in size (from T=2 to T=3 structures) upon increase in PSS molecular weight (from 400 kDa to 3.4 MDa), and that the total charge on the PSS exceeds that of the capsid protein by as much as a factor of 9. Here, we extend studies of this kind to PSS molecules that are sufficiently small that two or more can be packaged into VLPs. The use of 38 kDa PSS polymers that have been fluorescently labeled with Rhodamine B allows us to determine the number of PSS molecules per capsid. Electron micrographs of the VLPs show a bimodal distribution of particle diameters, with one peak centered around 19 nm, typical of a T=1 triangulation number, and the other around 21 nm, consistent with a pseudo T=2 structure; increasing the molar ratio of protein to PSS in the reaction mix shifts the VLP distribution from T=1 to T=2 structures. By combining fluorescence and gel electrophoresis measurements, it is determined that, on average, there are two polymers in each T=1 capsid and three in each T=2, with the PSS charge less than that of the capsid protein by as much as a factor of 2. VLPs of this kind provide a versatile model system for determining the principles underlying self-assembly of controlled numbers of cargo molecules in nanocontainers of increasing size.
Persistent Identifierhttp://hdl.handle.net/10722/199884
ISSN
2023 Impact Factor: 2.8
2023 SCImago Journal Rankings: 0.760
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorCadena-Nava, RD-
dc.contributor.authorHu, Y-
dc.contributor.authorGarmann, RF-
dc.contributor.authorNg, BCH-
dc.contributor.authorZelikin, AN-
dc.contributor.authorKnolber, CM-
dc.contributor.authorGelbart, WM-
dc.date.accessioned2014-07-25T00:49:04Z-
dc.date.available2014-07-25T00:49:04Z-
dc.date.issued2011-
dc.identifier.citationThe Journal of Physical Chemistry Part B: Condensed Matter, Materials, Surfaces, Interfaces & Biophysical, 2011, v. 115 n. 10, p. 2386-2391-
dc.identifier.issn1520-6106-
dc.identifier.urihttp://hdl.handle.net/10722/199884-
dc.description.abstractThe inside surfaces of the protein shells of many viruses are positively charged, thereby enhancing the self-assembly of capsid proteins around their (oppositely charged) RNA genome. These proteins have been shown to organize similarly around a variety of nonbiological, negatively charged, polymers, for example, poly(styrene sulfonate) (PSS), forming virus-like particles (VLPs). We have demonstrated recently that the VLPs formed from cowpea chlorotic mottle virus (CCMV) capsid protein increase in size (from T=2 to T=3 structures) upon increase in PSS molecular weight (from 400 kDa to 3.4 MDa), and that the total charge on the PSS exceeds that of the capsid protein by as much as a factor of 9. Here, we extend studies of this kind to PSS molecules that are sufficiently small that two or more can be packaged into VLPs. The use of 38 kDa PSS polymers that have been fluorescently labeled with Rhodamine B allows us to determine the number of PSS molecules per capsid. Electron micrographs of the VLPs show a bimodal distribution of particle diameters, with one peak centered around 19 nm, typical of a T=1 triangulation number, and the other around 21 nm, consistent with a pseudo T=2 structure; increasing the molar ratio of protein to PSS in the reaction mix shifts the VLP distribution from T=1 to T=2 structures. By combining fluorescence and gel electrophoresis measurements, it is determined that, on average, there are two polymers in each T=1 capsid and three in each T=2, with the PSS charge less than that of the capsid protein by as much as a factor of 2. VLPs of this kind provide a versatile model system for determining the principles underlying self-assembly of controlled numbers of cargo molecules in nanocontainers of increasing size.-
dc.languageeng-
dc.publisherAmerican Chemical Society. The Journal's web site is located at http://pubs.acs.org/journal/jpcbfk-
dc.relation.ispartofThe Journal of Physical Chemistry Part B: Condensed Matter, Materials, Surfaces, Interfaces & Biophysical-
dc.subject.meshBiomimetic Materials - chemistry-
dc.subject.meshBromovirus - chemistry-
dc.subject.meshFluorescent Dyes - chemistry-
dc.subject.meshPolymers - chemistry-
dc.subject.meshViruses - chemistry-
dc.titleExploiting fluorescent polymers to probe the self-assembly of virus-like particlesen_US
dc.typeArticleen_US
dc.identifier.emailCadena-Nava, RD: slchan@hku.hk-
dc.identifier.emailNg, BCH: ngbenny@hku.hk-
dc.identifier.doi10.1021/jp1094118-
dc.identifier.pmid21338131-
dc.identifier.scopuseid_2-s2.0-79952580177-
dc.identifier.hkuros202532-
dc.identifier.volume115-
dc.identifier.issue10-
dc.identifier.spage2386-
dc.identifier.epage2391-
dc.identifier.isiWOS:000288113300029-
dc.publisher.placeUnited States-
dc.identifier.issnl1520-5207-

Export via OAI-PMH Interface in XML Formats


OR


Export to Other Non-XML Formats