Inhibition of foot and mouth disease virus (FMDV) uncoating by a plant-derived peptide isolated from Melia azedarach L leaves

Meliacine (MA), a peptide isolated from leaves of the high plant Melia azedarach L inhibited the multiplication of foot and mouth disease virus (FMDV) in BHK-21 cells. In this report, we establish that the MA-inhibitable process takes place within the first hour of the viral reproductive cycle. MA h...

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Autor principal: Wachsman, M.B
Otros Autores: Castilla, V., Coto, C.E
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Lenguaje:Inglés
Publicado: 1998
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024 7 |2 scopus  |a 2-s2.0-0031961054 
024 7 |2 cas  |a Antiviral Agents; meliacin; Peptides; Plant Extracts; Plant Proteins 
040 |a Scopus  |b spa  |c AR-BaUEN  |d AR-BaUEN 
030 |a ARVID 
100 1 |a Wachsman, M.B. 
245 1 0 |a Inhibition of foot and mouth disease virus (FMDV) uncoating by a plant-derived peptide isolated from Melia azedarach L leaves 
260 |c 1998 
270 1 0 |m Wachsman, M.B.; Universidad de Buenos Aires, Departamento de Quimica Biologica, Facul. de Cienc. Exactas./Naturales, Piso 4, 1428 Buenos Aires, Argentina 
506 |2 openaire  |e Política editorial 
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504 |a Andrei, G.M., Couto, A.G., Lederkremer, R.M., Goto, C.E., Purification and partial characterization of an antiviral active peptide from Melia azedarach L (1994) Antiviral Chem Chemother, 5, pp. 105-110 
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504 |a Gutierrez, A., Rodriguez, A., Pintado, B., Sobrino, F., Transient inhibition of foot-and-mouth disease virus infection of BHK-21 cells by antisense oligonucleotides directed against the second functional initiator AUG (1993) Antiviral Res, 22, pp. 1-13 
504 |a Jackson, T., Ellard, F.M., Ghazaleh, R.A., Brookes, S.M., Blackemore, W.E., Corteyn, A.H., Stuart, D.I., King, A.M.Q., Efficient infection of cells in culture by type O foot-and-mouth disease virus requires binding to cell surface heparan sulfate (1996) J Virol, 70, pp. 5282-5287 
504 |a Kato, N., Eggers, H.J., Inhibition of uncoating of fowl plague virus by L-adamantanamine hydrochloride (1969) Virology, 37, pp. 632-641 
504 |a Kleina, L.G., Grubman, M.J., Antiviral effect of a thiol protease inhibitor on foot-and-mouth disease virus (1992) J Virol, 66, pp. 7168-7175 
504 |a Kraus, W., Zimmerman, H., Eggers, H.J., Nelsen-Salz, B., Rhodanine resistance and dependence of echovirus 12: A possible consequence of capsid flexibility (1997) J Virol, 71, pp. 1697-1702 
504 |a Mandel, B., The relationship between penetration and uncoating of poliovirus in Hela cells (1967) Virology, 31, pp. 702-712 
504 |a Marsh, M., Helenius, A., Virus entry into animal cells (1989) Adv Virus Res, 36, pp. 107-151 
504 |a Mason, P.W., Baxt, B., Brown, F., Harber, J., Murdin, A., Wimmer, E., Antibody-complexed foot-and-mouth disease virus, but not poliovirus, can infect normally in susceptible cells via the Fc receptor (1993) Virology, 192, pp. 568-577 
504 |a Mc Sharry, J.J., Caliguiri, L.A., Eggers, H.J., Inhibition of uncoating of poliovirus by arildone, a new antiviral drug (1979) Virology, 97, pp. 307-315 
504 |a Ohkuma, J., Poole, B., Fluorescence probe measurement of the intralysosomal pH in living cells and the perturbation of pH by various agents (1978) Proc Natl Acad Sci USA, 75, pp. 3327-3331 
504 |a Pérez, L., Carrasco, L., Involvement of the vacuolar H+-ATPase in animal virus entry (1994) J Gen Virol, 75, pp. 2595-2606 
504 |a Reggio, H., Baiton, D., Harms, E., Coudrier, E., Louvard, D., Antibodies against lysosomal membranes reveal a 100,000- Mol-wt protein that cross-reacts with purified H+, K+ATPase from gastric mucose (1984) J Cell Biol, 99, pp. 1511-1526 
504 |a Singh, A.K., Sidhu, G.S., Friedman, R.M., Maheshwari, R.K., Mechanism of enhancement of the antiviral action of Interferon against herpes simplex virus-1 by chloroquine (1996) J Interferon Cytokine Res, 16, pp. 725-731 
504 |a Singh, I.R., Suomalainen, M., Varadarajan, S., Garoff, H., Helenius, A., Multiple mechanisms for inhibition of entry and uncoating of superinfecting Semliki Forest virus (1997) Virology, 231, pp. 59-71 
504 |a Villamil, S.M., Alché, L.E., Coto, C.E., Inhibition of herpes simplex type-1 multiplication by meliacine, a peptide of plant origin (1995) Antiviral Chem Chemother, 6, pp. 239-244 
504 |a Wachsman, M.B., Coto, C.E., Susceptibility of picornaviruses to an antiviral of vegetal origin (meliacine) (1995) Rev Arg Microbiol, 27, pp. 33-37 
504 |a Wachsman, M.B., Damonte, E.B., Coto, C.E., De Torres, R.A., Antiviral effects of Melia azedarach L leaves extracts on sindhis virus infected cells (1987) Antiviral Res, 8, pp. 1-12 
520 3 |a Meliacine (MA), a peptide isolated from leaves of the high plant Melia azedarach L inhibited the multiplication of foot and mouth disease virus (FMDV) in BHK-21 cells. In this report, we establish that the MA-inhibitable process takes place within the first hour of the viral reproductive cycle. MA had no virucidal effect and did not affect adsorption and penetration of the virus in cells. In experiments with neutral red-labeled virus, it was found that MA significantly suppressed the development of photoresistance of the virus in infected cells. In untreated cultures nearly all virus which adsorbed to cells was uncoated within 1 h at 37°C, whereas in treated cultures, even after 3 h only 3% of the virus was uncoated. Labeling of BHK-21 cells with acridine orange showed that MA affects the pH of intracellular acidic vesicles. Therefore, it is concluded that MA prevents the process of uncoating of FMDV in BHK-21 cells by inhibiting vacuolar acidification. Foot and mouth disease virus (FMDV) is a pathogen that affects a wide range of cloven-hoofed animals of agricultural and economic importance throughout the world. The seven serotypes of FMDV (types O, A, C, and Asia and the South African territories types 1, 2 and 3) constitute the Aphthovirus gene of the family Picornaviridae. FMDV is a small, non-enveloped, icosahedral virus with a single-stranded, positive-sense RNA genome of approximately 8 400 nucleotides [8]. Control of the disease is carried out using inactivated vaccines [4], but the major problem in control by vaccination is the antigenic variation of the virus [9, 10].  |l eng 
593 |a Depto. de Quim. Biológica, Fac. de Ciencias Exactas y Naturales, Universidad de Buenos Aires, Buenos Aires, Argentina 
593 |a Depto. de Quim. Biológica, Fac. de Ciencias Exactas y Naturales, Universidad de Buenos Aires, Pabellón 2, 1428, Buenos Aires, Argentina 
690 1 0 |a ANTIVIRAL ACTIVITY 
690 1 0 |a CELL LINE 
690 1 0 |a FOOT AND MOUTH DISEASE VIRUS 
690 1 0 |a PHYSICAL RESISTANCE 
690 1 0 |a SEROTYPE 
690 1 0 |a VIRUS GENOME 
690 1 0 |a VIRUS INHIBITION 
690 1 0 |a VIRUS REPLICATION 
690 1 0 |a ANIMALS 
690 1 0 |a ANTIVIRAL AGENTS 
690 1 0 |a APHTHOVIRUS 
690 1 0 |a CELL LINE 
690 1 0 |a CRICETINAE 
690 1 0 |a PEPTIDES 
690 1 0 |a PLANT EXTRACTS 
690 1 0 |a PLANT LEAVES 
690 1 0 |a PLANT PROTEINS 
690 1 0 |a TREES 
650 1 7 |2 spines  |a VIRUS RNA 
700 1 |a Castilla, V. 
700 1 |a Coto, C.E. 
773 0 |d 1998  |g v. 143  |h pp. 581-590  |k n. 3  |p Arch. Virol.  |x 03048608  |t Archives of Virology 
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