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
- Institución
- Consejo Nacional de Investigaciones Científicas y Técnicas
- OAI Identificador
- oai:ri.conicet.gov.ar:11336/58991
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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 Técnicas2025-09-29T10:47:48Zoai: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:34982025-09-29 10:47:49.034CONICET 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 |
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Consejo Nacional de Investigaciones Científicas y Técnicas |
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CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas |
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dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar |
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13.070432 |