Enterocin CRL35 inhibits late stages of HSV-1 and HSV-2 replication in vitro

Autores
Wachsman, Mónica B.; Castilla, Viviana; Pesce de Ruiz Holgado, Aida Argentina; de Torres Puigarnau, Ramon Alberto; Sesma, Fernando Juan Manuel; Coto, Celia Esther
Año de publicación
2003
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
The replication of herpes simplex virus (HSV) type 1 and 2 in Vero cells is inhibited in the presence of enterocin CRL35 (ECRL), a bacteriocin produced by Enterococcus faecium CRL35. Attempts to resolve the mode of action of ECRL indicate that virus adsorption and penetration are not affected. Instead, a late step of virus multiplication is hindered since the addition of 100μg/ml of ECRL at 8h post infection still causes a 90% inhibition of virus release. The effect of ECRL on HSV antigen expression was studied by immunofluorescence using a polyclonal serum and a monoclonal antibody against glycoprotein D (γ protein). These studies indicated that ECRL impeded the second round of infection, apparently as a consequence of the inhibition of glycoprotein D expression. The replication of syncytial mutants of HSV-1 was significantly inhibited at a ECRL concentration of 25μg/ml. Both the percentage of fused cells and the polykaryocyte size were affected. Studies on the effect of ECRL on viral protein synthesis showed that in the presence of ECRL, HSV late γ proteins were not synthesized. From these findings, it is concluded that inhibition of HSV spreading by ECRL is due to the prevention of mainly late glycoprotein synthesis.
Fil: Wachsman, Mónica B.. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Química Biológica. Laboratorio de Virología; Argentina
Fil: Castilla, Viviana. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Química Biológica. Laboratorio de Virología; Argentina
Fil: Pesce de Ruiz Holgado, Aida Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Centro de Referencia para Lactobacilos; Argentina
Fil: de Torres Puigarnau, Ramon Alberto. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Departamento de Microbiología, Inmunología y Biotecnología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Sesma, Fernando Juan Manuel. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Centro de Referencia para Lactobacilos; Argentina
Fil: Coto, Celia Esther. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Química Biológica. Laboratorio de Virología; Argentina
Materia
Antiviral
Bacteriocin
Enterococcus Faecium
Herpes Simplex Type 1 And 2
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/58991
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/58991
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Enterocin CRL35 inhibits late stages of HSV-1 and HSV-2 replication in vitroWachsman, Mónica B.Castilla, VivianaPesce de Ruiz Holgado, Aida Argentinade Torres Puigarnau, Ramon AlbertoSesma, Fernando Juan ManuelCoto, Celia EstherAntiviralBacteriocinEnterococcus FaeciumHerpes Simplex Type 1 And 2https://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1The replication of herpes simplex virus (HSV) type 1 and 2 in Vero cells is inhibited in the presence of enterocin CRL35 (ECRL), a bacteriocin produced by Enterococcus faecium CRL35. Attempts to resolve the mode of action of ECRL indicate that virus adsorption and penetration are not affected. Instead, a late step of virus multiplication is hindered since the addition of 100μg/ml of ECRL at 8h post infection still causes a 90% inhibition of virus release. The effect of ECRL on HSV antigen expression was studied by immunofluorescence using a polyclonal serum and a monoclonal antibody against glycoprotein D (γ protein). These studies indicated that ECRL impeded the second round of infection, apparently as a consequence of the inhibition of glycoprotein D expression. The replication of syncytial mutants of HSV-1 was significantly inhibited at a ECRL concentration of 25μg/ml. Both the percentage of fused cells and the polykaryocyte size were affected. Studies on the effect of ECRL on viral protein synthesis showed that in the presence of ECRL, HSV late γ proteins were not synthesized. From these findings, it is concluded that inhibition of HSV spreading by ECRL is due to the prevention of mainly late glycoprotein synthesis.Fil: Wachsman, Mónica B.. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Química Biológica. Laboratorio de Virología; ArgentinaFil: Castilla, Viviana. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Química Biológica. Laboratorio de Virología; ArgentinaFil: Pesce de Ruiz Holgado, Aida Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Centro de Referencia para Lactobacilos; ArgentinaFil: de Torres Puigarnau, Ramon Alberto. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Departamento de Microbiología, Inmunología y Biotecnología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Sesma, Fernando Juan Manuel. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Centro de Referencia para Lactobacilos; ArgentinaFil: Coto, Celia Esther. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Química Biológica. Laboratorio de Virología; ArgentinaElsevier Science2003-03info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/58991Wachsman, Mónica B.; Castilla, Viviana; Pesce de Ruiz Holgado, Aida Argentina; de Torres Puigarnau, Ramon Alberto; Sesma, Fernando Juan Manuel; et al.; Enterocin CRL35 inhibits late stages of HSV-1 and HSV-2 replication in vitro; Elsevier Science; Antiviral Research; 58; 1; 3-2003; 17-240166-35421872-9096CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1016/S0166-3542(02)00099-2info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S0166354202000992info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-10-15T15:46:32Zoai:ri.conicet.gov.ar:11336/58991instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-10-15 15:46:32.439CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Enterocin CRL35 inhibits late stages of HSV-1 and HSV-2 replication in vitro
title Enterocin CRL35 inhibits late stages of HSV-1 and HSV-2 replication in vitro
spellingShingle Enterocin CRL35 inhibits late stages of HSV-1 and HSV-2 replication in vitro
Wachsman, Mónica B.
Antiviral
Bacteriocin
Enterococcus Faecium
Herpes Simplex Type 1 And 2
title_short Enterocin CRL35 inhibits late stages of HSV-1 and HSV-2 replication in vitro
title_full Enterocin CRL35 inhibits late stages of HSV-1 and HSV-2 replication in vitro
title_fullStr Enterocin CRL35 inhibits late stages of HSV-1 and HSV-2 replication in vitro
title_full_unstemmed Enterocin CRL35 inhibits late stages of HSV-1 and HSV-2 replication in vitro
title_sort Enterocin CRL35 inhibits late stages of HSV-1 and HSV-2 replication in vitro
dc.creator.none.fl_str_mv Wachsman, Mónica B.
Castilla, Viviana
Pesce de Ruiz Holgado, Aida Argentina
de Torres Puigarnau, Ramon Alberto
Sesma, Fernando Juan Manuel
Coto, Celia Esther
author Wachsman, Mónica B.
author_facet Wachsman, Mónica B.
Castilla, Viviana
Pesce de Ruiz Holgado, Aida Argentina
de Torres Puigarnau, Ramon Alberto
Sesma, Fernando Juan Manuel
Coto, Celia Esther
author_role author
author2 Castilla, Viviana
Pesce de Ruiz Holgado, Aida Argentina
de Torres Puigarnau, Ramon Alberto
Sesma, Fernando Juan Manuel
Coto, Celia Esther
author2_role author
author
author
author
author
dc.subject.none.fl_str_mv Antiviral
Bacteriocin
Enterococcus Faecium
Herpes Simplex Type 1 And 2
topic Antiviral
Bacteriocin
Enterococcus Faecium
Herpes Simplex Type 1 And 2
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv The replication of herpes simplex virus (HSV) type 1 and 2 in Vero cells is inhibited in the presence of enterocin CRL35 (ECRL), a bacteriocin produced by Enterococcus faecium CRL35. Attempts to resolve the mode of action of ECRL indicate that virus adsorption and penetration are not affected. Instead, a late step of virus multiplication is hindered since the addition of 100μg/ml of ECRL at 8h post infection still causes a 90% inhibition of virus release. The effect of ECRL on HSV antigen expression was studied by immunofluorescence using a polyclonal serum and a monoclonal antibody against glycoprotein D (γ protein). These studies indicated that ECRL impeded the second round of infection, apparently as a consequence of the inhibition of glycoprotein D expression. The replication of syncytial mutants of HSV-1 was significantly inhibited at a ECRL concentration of 25μg/ml. Both the percentage of fused cells and the polykaryocyte size were affected. Studies on the effect of ECRL on viral protein synthesis showed that in the presence of ECRL, HSV late γ proteins were not synthesized. From these findings, it is concluded that inhibition of HSV spreading by ECRL is due to the prevention of mainly late glycoprotein synthesis.
Fil: Wachsman, Mónica B.. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Química Biológica. Laboratorio de Virología; Argentina
Fil: Castilla, Viviana. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Química Biológica. Laboratorio de Virología; Argentina
Fil: Pesce de Ruiz Holgado, Aida Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Centro de Referencia para Lactobacilos; Argentina
Fil: de Torres Puigarnau, Ramon Alberto. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Departamento de Microbiología, Inmunología y Biotecnología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Sesma, Fernando Juan Manuel. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Centro de Referencia para Lactobacilos; Argentina
Fil: Coto, Celia Esther. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Química Biológica. Laboratorio de Virología; Argentina
description The replication of herpes simplex virus (HSV) type 1 and 2 in Vero cells is inhibited in the presence of enterocin CRL35 (ECRL), a bacteriocin produced by Enterococcus faecium CRL35. Attempts to resolve the mode of action of ECRL indicate that virus adsorption and penetration are not affected. Instead, a late step of virus multiplication is hindered since the addition of 100μg/ml of ECRL at 8h post infection still causes a 90% inhibition of virus release. The effect of ECRL on HSV antigen expression was studied by immunofluorescence using a polyclonal serum and a monoclonal antibody against glycoprotein D (γ protein). These studies indicated that ECRL impeded the second round of infection, apparently as a consequence of the inhibition of glycoprotein D expression. The replication of syncytial mutants of HSV-1 was significantly inhibited at a ECRL concentration of 25μg/ml. Both the percentage of fused cells and the polykaryocyte size were affected. Studies on the effect of ECRL on viral protein synthesis showed that in the presence of ECRL, HSV late γ proteins were not synthesized. From these findings, it is concluded that inhibition of HSV spreading by ECRL is due to the prevention of mainly late glycoprotein synthesis.
publishDate 2003
dc.date.none.fl_str_mv 2003-03
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/11336/58991
Wachsman, Mónica B.; Castilla, Viviana; Pesce de Ruiz Holgado, Aida Argentina; de Torres Puigarnau, Ramon Alberto; Sesma, Fernando Juan Manuel; et al.; Enterocin CRL35 inhibits late stages of HSV-1 and HSV-2 replication in vitro; Elsevier Science; Antiviral Research; 58; 1; 3-2003; 17-24
0166-3542
1872-9096
CONICET Digital
CONICET
url http://hdl.handle.net/11336/58991
identifier_str_mv Wachsman, Mónica B.; Castilla, Viviana; Pesce de Ruiz Holgado, Aida Argentina; de Torres Puigarnau, Ramon Alberto; Sesma, Fernando Juan Manuel; et al.; Enterocin CRL35 inhibits late stages of HSV-1 and HSV-2 replication in vitro; Elsevier Science; Antiviral Research; 58; 1; 3-2003; 17-24
0166-3542
1872-9096
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/10.1016/S0166-3542(02)00099-2
info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S0166354202000992
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
dc.publisher.none.fl_str_mv Elsevier Science
publisher.none.fl_str_mv Elsevier Science
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
repository.name.fl_str_mv CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas
repository.mail.fl_str_mv dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar
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score 13.22299

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