Characterization of Junín virus particles inactivated by a zinc finger-reactive compound

Our previous studies reported the inhibitory action against arenaviruses of antiretroviral zinc finger-reactive compounds provided by the National Cancer Institute (USA). These compounds were able to inactivate virions as well as to reduce virus yields from infected cells. Here, the inactivation of...

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Autor principal: García, C.C
Otros Autores: Ellenberg, P.C, Artuso, M.C, Scolaro, L.A, Damonte, E.B
Formato: Capítulo de libro
Lenguaje:Inglés
Publicado: 2009
Acceso en línea:Registro en Scopus
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Registro en la Biblioteca Digital
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024 7 |2 scopus  |a 2-s2.0-67349181010 
024 7 |2 cas  |a disulfide, 16734-12-6; 1,1-azobisformamide, 123-77-3; Anti-HIV Agents; Azo Compounds; Carrier Proteins; Disulfides; Green Fluorescent Proteins, 147336-22-9; Nucleocapsid Proteins; Recombinant Fusion Proteins 
040 |a Scopus  |b spa  |c AR-BaUEN  |d AR-BaUEN 
030 |a VIRED 
100 1 |a García, C.C. 
245 1 0 |a Characterization of Junín virus particles inactivated by a zinc finger-reactive compound 
260 |c 2009 
270 1 0 |m Damonte, E.B.; Laboratorio de Virología, Departamento de Química Biológica, Facultad de Ciencias Exactas y Naturales, Ciudad Universitaria, Pabellon 2, Piso 4, 1428 Buenos Aires, Argentina; email: edamonte@qb.fcen.uba.ar 
506 |2 openaire  |e Política editorial 
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504 |a López, N., Scolaro, L., Rossi, C., Jácamo, R., Candurra, N., Pujol, C., Damonte, E.B., Franze-Fernández, M.T., Homologous and heterologous glycoproteins induce protection against Junín virus challenge in guinea pigs (2000) J. Gen. Virol., 81, pp. 1273-1281 
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504 |a Okada, A., Miura, T., Takeuchi, H., Zinc- and pH-dependent conformational transition in a putative interdomain linker region of the influenza virus matrix protein M1 (2003) Biochemistry, 42, pp. 1978-1984 
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504 |a Rice, W.G., Turpin, J.A., Huang, M., Clanton, D., Buckheit Jr., R.W., Covell, D.G., Wallquist, A., Sausville, E.A., Azodicarbonamide inhibits HIV-1 replication by targeting the nucleocapsid protein (1997) Nat. Med., 3, pp. 341-345 
504 |a Rotz, L.D., Khan, A.S., Lillibridge, S.R., Ostroff, S.M., Hughes, J.M., Public health assessment of potential biological terrorism agents (2002) Emerg. Infect. Dis., 8, pp. 225-230 
504 |a Salvato, M.S., Schweighofer, K.J., Burns, J., Shimomaye, E.M., Biochemical and immunological evidence that the 11-kDa zinc-binding protein of lymphocytic choriomeningitis virus is a structural component of the virus (1992) Virus Res., 22, pp. 185-198 
504 |a Salvato, M.S., Molecular biology of the prototype arenavirus, lymphocytic choriomeningitis virus (1993) The Arenaviridae, pp. 133-156. , Salvato M.S. (Ed), Plenum Press, New York 
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504 |a Strecker, T., Eichler, R., ter Meulen, J., Weissenhorn, W., Klenk, H.D., Garten, W., Lenz, O., Lassa virus Z protein is a matrix protein and sufficient for the release of virus-like particles (2003) J. Virol., 77, pp. 10700-10705 
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504 |a Tesh, R.B., Jahrling, P.B., Salas, R., Shope, R.E., Description of Guanarito virus (Arenaviridae: Arenavirus), the etiologic agent of Venezuelan hemorrhagic fever (1994) Am. J. Trop. Med. Hyg., 50, pp. 452-459 
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504 |a York, J., Nunberg, J.H., A novel zinc-binding domain is essential for formation of the functional Junín virus envelope glycoprotein complex (2007) J. Virol., 81, pp. 13385-13391 
520 3 |a Our previous studies reported the inhibitory action against arenaviruses of antiretroviral zinc finger-reactive compounds provided by the National Cancer Institute (USA). These compounds were able to inactivate virions as well as to reduce virus yields from infected cells. Here, the inactivation of the arenavirus Junín (JUNV), agent of Argentine hemorrhagic fever, by the aromatic disulfide NSC20625 was analyzed. The treatment of purified JUNV with this compound eliminated infectivity apparently through irreversible modifications in the matrix Z protein detected by: (a) alterations in the electrophoretic migration profile of Z under non-reducing conditions; (b) an electrodense labeling in the internal layer beneath the envelope and around the matrix Z protein, in negatively stained preparations; (c) changes in the subcellular localization of Z in cells transfected with a recombinant fusion protein JUNVZ-eGFP. The infection of Vero cells with JUNV inactivated particles was blocked at the uncoating of viral nucleocapsid from endosomes, providing new evidence for a functional role of Z in this stage of arenavirus cycle. Furthermore, the inactivated JUNV particles retained the immunoreactivity of the surface glycoprotein GP1 suggesting that this disulfide may be useful in the pursuit of an inactivating agent to obtain a vaccine antigen or diagnostic tool. © 2009 Elsevier B.V. All rights reserved.  |l eng 
536 |a Detalles de la financiación: Agencia Nacional de Promoción Científica y Tecnológica 
536 |a Detalles de la financiación: Consejo Nacional de Investigaciones Científicas y Técnicas 
536 |a Detalles de la financiación: The authors acknowledge the National Cancer Institute, Frederick, USA, for providing the zinc finger-reactive compounds. This work was supported by grants from Consejo Nacional de Investigaciones Científicas y Técnicas (CONICET), Agencia Nacional de Promoción Científica y Tecnológica and Universidad de Buenos Aires, Argentina. CCG, LAS and EBD are members of the Research Career from CONICET. 
593 |a Laboratorio de Virología, Departamento de Química Biológica, Facultad de Ciencias Exactas y Naturales, Ciudad Universitaria, Pabellon 2, Piso 4, 1428 Buenos Aires, Argentina 
690 1 0 |a ARENAVIRUS 
690 1 0 |a JUNIN VIRUS 
690 1 0 |a MATRIX PROTEIN 
690 1 0 |a VIRUS INACTIVATION 
690 1 0 |a ZINC FINGER 
690 1 0 |a DISULFIDE 
690 1 0 |a DISULFIDE NSC20625 
690 1 0 |a ENHANCED GREEN FLUORESCENT PROTEIN 
690 1 0 |a FATTY ACID BINDING PROTEIN 
690 1 0 |a HYBRID PROTEIN 
690 1 0 |a MATRIX PROTEIN 
690 1 0 |a UNCLASSIFIED DRUG 
690 1 0 |a ANIMAL CELL 
690 1 0 |a ARTICLE 
690 1 0 |a CELLULAR DISTRIBUTION 
690 1 0 |a CONTROLLED STUDY 
690 1 0 |a ELECTROPHORESIS 
690 1 0 |a ENDOSOME 
690 1 0 |a GENETIC TRANSFECTION 
690 1 0 |a HEMORRHAGIC FEVER 
690 1 0 |a JUNIN VIRUS 
690 1 0 |a NONHUMAN 
690 1 0 |a PRIORITY JOURNAL 
690 1 0 |a VIROGENESIS 
690 1 0 |a VIRUS INACTIVATION 
690 1 0 |a VIRUS INFECTIVITY 
690 1 0 |a VIRUS NUCLEOCAPSID 
690 1 0 |a VIRUS PARTICLE 
690 1 0 |a ZINC FINGER MOTIF 
690 1 0 |a ANIMALS 
690 1 0 |a ANTI-HIV AGENTS 
690 1 0 |a ARENAVIRIDAE INFECTIONS 
690 1 0 |a AZO COMPOUNDS 
690 1 0 |a CARRIER PROTEINS 
690 1 0 |a CERCOPITHECUS AETHIOPS 
690 1 0 |a DISULFIDES 
690 1 0 |a GREEN FLUORESCENT PROTEINS 
690 1 0 |a JUNIN VIRUS 
690 1 0 |a MICROSCOPY, ELECTRON, TRANSMISSION 
690 1 0 |a NUCLEOCAPSID PROTEINS 
690 1 0 |a RECOMBINANT FUSION PROTEINS 
690 1 0 |a VERO CELLS 
690 1 0 |a VIRION 
690 1 0 |a VIRUS INACTIVATION 
690 1 0 |a ZINC FINGERS 
690 1 0 |a ARENAVIRUS 
690 1 0 |a JUNIN VIRUS 
700 1 |a Ellenberg, P.C. 
700 1 |a Artuso, M.C. 
700 1 |a Scolaro, L.A. 
700 1 |a Damonte, E.B. 
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