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01.04.2009 | Brief Report

In vitro assembly of nucleocapsid-like particles from purified recombinant capsid protein of dengue-2 virus

verfasst von: Carlos López, Lázaro Gil, Laura Lazo, Ivón Menéndez, Ernesto Marcos, Jorge Sánchez, Iris Valdés, Viviana Falcón, María C. de la Rosa, Gabriel Márquez, Gerardo Guillén, Lisset Hermida

Erschienen in: Archives of Virology | Ausgabe 4/2009

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Abstract

The capsid protein is one of the three structural proteins of flaviviruses and is the building block of the nucleocapsid. It has also a predominant role in the replication of dengue virus. To obtain nucleocapsid-like particles from recombinant dengue-2 capsid protein produced in E. coli, a purification process using cation exchange chromatography was established. The purified protein exhibited a molecular mass corresponding to a dimer; therefore, similar to that reported for alphaviruses, an in vitro assembly reaction using single-stranded DNA was performed. In all cases, particles were obtained independently of the specificity and the length of the oligonucleotides used. The present work is the first report of in vitro assembly of the recombinant dengue capsid protein, which could constitute a powerful tool in the development of vaccine candidates.

Gubler DJ (2002) Epidemic dengue/dengue hemorrhagic fever as a public health, social and economic problem in the 21st century. Trends Microbiol 10:100–103PubMedCrossRef

Lindenbach BD, Rice CM (2003) Molecular biology of flaviviruses. Adv Virus Res 59:23–61PubMedCrossRef

Ma L, Jones CT, Groesch TD, Kuhn RJ, Post CB (2004) Solution structure of dengue virus capsid protein reveals another fold. Proc Natl Acad Sci USA 101:3414–3419PubMedCrossRef

Lobigs M (1993) Flavivirus premembrane protein cleavage and spike heterodimer secretion require the function of the viral proteinase NS3. Proc Natl Acad Sci U SA 90:6218–6222CrossRef

Dokland T, Walsh M, Mackenzie JM, Khromykh AA, Kim-Huey E, Wang S (2004) West Nile virus core protein: tetramer structure and ribbon formation. Structure 12:1157–1163PubMedCrossRef

Kuhn RJ, Zhang W, Rossmann MG, Pletnev SV, Corver J, Lenches E, Jones CT, Mukhopadhyay S, Chipman PR, Strauss EG, Baker TS, Strauss JH (2002) Structure of dengue virus: implications for flavivirus organization, maturation, and fusion. Cell 108:717–725PubMedCrossRef

Mukhopadhyay S, Kim BS, Chipman PR, Rossmann MG, Kuhn RJ (2003) Structure of West Nile virus. Science 302:248PubMedCrossRef

Ferlenghi I, Clarke M, Ruttan T, Allison SL, Schalich J, Heinz FX, Harrison SC, Rey FA, Fuller SD (2001) Molecular organization of a recombinant subviral particle from tick-borne encephalitis virus. Mol Cell 7:593–602PubMedCrossRef

Kummerer BM, Rice CM (2002) Mutations in the yellow fever virus nonstructural protein NS2A selectively blocks production of infectious particles. J Virol 76:4773–4784PubMedCrossRef

10.

Jones CT, Ma L, Burgner JW, Groesch TD, Post CB, Kuhn RJ (2003) Flavivirus capsid is a dimeric alpha-helical protein. J Virol 77:7143–7149PubMedCrossRef

11.

Kiermayr S, Kofler MR, Mandl WC, Messner P, Heinz F (2004) Isolation of capsid protein dimers from the tick-borne encephalitis flavivirus and in vitro assembly of capsid-like particles. J Virol 78:8078–8084PubMedCrossRef

12.

Lazo L, Hermida L, Zulueta A, Sánchez J, López C, Silva R, Guillén G, Guzmán MG (2007) A recombinant capsid protein from dengue-2 induces protection in mice against homologous virus. Vaccine 25:1064–1070PubMedCrossRef

13.

Falcón V (1999) Ultrastructural and immunocytochemical evidences of core-particle formation in the methylotrophic Pichia pastoris yeast when expressing HCV structural proteins. Tissue Cell 31:117–125PubMedCrossRef

14.

Wengler G, Wengler G, Boege U, Wahn K (1984) Establishment and analysis of a system which allows assembly and disassembly of alphavirus core-like particles under physiological conditions in vitro. Virology 132:401–412PubMedCrossRef

15.

Acosta-Rivero N, Alvarez-Obregón JC, Musacchio A, Falcón V, Dueñas-Carrera S, Marante J, Menéndez I, Morales J (2002) In vitro self-assembled HCV core virus-like particles induce a strong antibody immune response in sheep. Biochem Biophys Res Commun 290:300–304PubMedCrossRef

16.

Acosta-Rivero N, Rodríguez A, Musacchio A, Falcón V, Suarez V, Martinez G, Guerra I, Paz-Lago D, Morera Y, de la Rosa MC, Morales-Grillo J, Dueñas-Carrera S (2004) In vitro assembly into virus-like particles is an intrinsic quality of Pichia pastoris derived HCV core protein. Biochem Biophys Res Commun 325:68–74PubMedCrossRef

17.

Tleugabulova D, Falcón V, Pentón E (1998) Evidence for the denaturation of recombinant hepatitis surface antigen on aluminum hydroxide gel. J Chromatogr Biomed Sci Appl 720:153–163CrossRef

18.

Goicochea NL, De M, Rotello VM, Mukhopadhyay S, Dragnea B (2007) Core-like particles of an enveloped animal virus can self-assemble efficiently on artificial templates. Nano Lett 7:2281–2290PubMedCrossRef

19.

Lobaina Y, Palenzuela D, Pichardo D, Muzio V, Guillen G, Aguilar JC (2005) Immunological characterization of two hepatitis B core antigen variants and their immunoenhancing effect on co-delivered hepatitis B surface antigen. Mol Immunol 42:289–294PubMedCrossRef

Titel: In vitro assembly of nucleocapsid-like particles from purified recombinant capsid protein of dengue-2 virus
verfasst von: Carlos López
Lázaro Gil
Laura Lazo
Ivón Menéndez
Ernesto Marcos
Jorge Sánchez
Iris Valdés
Viviana Falcón
María C. de la Rosa
Gabriel Márquez
Gerardo Guillén
Lisset Hermida
Publikationsdatum: 01.04.2009
Verlag: Springer Vienna
Erschienen in: Archives of Virology / Ausgabe 4/2009
Print ISSN: 0304-8608
Elektronische ISSN: 1432-8798
DOI: https://doi.org/10.1007/s00705-009-0350-8

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In vitro assembly of nucleocapsid-like particles from purified recombinant capsid protein of dengue-2 virus

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