1-Cinnamoyl-3,11-dihydroxymeliacarpin delays glycoprotein transport restraining virus multiplication without cytotoxicity
The 1-cinnamoyl-3,11-dihydroxymeliacarpin (CDM), isolated from extracts of Melia azedarach L., displays antiviral and immunomodulating properties. CDM is the first reported tetranortriterpenoid responsible for the alkalinization of intracellular compartments affecting both, viral endocytic and exocy...
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2010
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| Acceso en línea: | https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_0006291X_v393_n1_p32_Bueno http://hdl.handle.net/20.500.12110/paper_0006291X_v393_n1_p32_Bueno |
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paper:paper_0006291X_v393_n1_p32_Bueno2023-06-08T14:30:18Z 1-Cinnamoyl-3,11-dihydroxymeliacarpin delays glycoprotein transport restraining virus multiplication without cytotoxicity Bueno, Carlos Alberto Alche, Laura Edith Barquero, Andrea Alejandra Antiviral Golgi apparatus Medicinal plants Secretory pathway Transferrin receptor 1 cinnamoyl 3,11 dihydroxymeliacarpin concanamycin A glycoprotein Melia azedarach extract monensin transferrin receptor triterpenoid unclassified drug alkalinization article cell compartmentalization cell membrane controlled study cytotoxicity drug activity drug inhibition endosome glycoprotein synthesis Herpes simplex virus 1 human human cell immunomodulation integument Melia azedarach membrane transport nonhuman priority journal protein binding protein localization protein transport virogenesis virus capsid Antiviral Agents Cell Line Glycoproteins Herpesvirus 1, Human Humans Limonins Macrolides Melia azedarach Monensin Protein Transport Receptors, Transferrin Tumor Necrosis Factor-alpha Viral Envelope Proteins Virus Replication Human herpesvirus 1 Melia azedarach Miridae The 1-cinnamoyl-3,11-dihydroxymeliacarpin (CDM), isolated from extracts of Melia azedarach L., displays antiviral and immunomodulating properties. CDM is the first reported tetranortriterpenoid responsible for the alkalinization of intracellular compartments affecting both, viral endocytic and exocytic pathways. Considering that viral glycoprotein synthesis is completely dependent upon cellular membrane trafficking, we questioned whether CDM might also interfere with the normal transport of cellular glycoproteins. This study demonstrates that CDM promoted a transient block in the transport of two cellular glycoproteins, the transferrin receptor (TfR) and TNF-α. Nevertheless, CDM did not affect the transferrin binding ability of TfR and did not impede the TNF-α secretion. On the other hand, CDM disturbed the intracellular localization of capsid, glycoprotein and tegument proteins simultaneously in the same HSV-1 infected cells. Besides, we show that concanamycin A and monensin provoke a permanent blockage of viral and cellular glycoproteins, in contrast to the delay observed after CDM treatment. Thus, the delay on glycoprotein transport caused by CDM would account for the strong inhibition on virus multiplication without interfering with the bioactivity of cellular glycoproteins. © 2010 Elsevier Inc. All rights reserved. Fil:Bueno, C.A. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Alché, L.E. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Barquero, A.A. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. 2010 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_0006291X_v393_n1_p32_Bueno http://hdl.handle.net/20.500.12110/paper_0006291X_v393_n1_p32_Bueno |
| institution |
Universidad de Buenos Aires |
| institution_str |
I-28 |
| repository_str |
R-134 |
| collection |
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
| topic |
Antiviral Golgi apparatus Medicinal plants Secretory pathway Transferrin receptor 1 cinnamoyl 3,11 dihydroxymeliacarpin concanamycin A glycoprotein Melia azedarach extract monensin transferrin receptor triterpenoid unclassified drug alkalinization article cell compartmentalization cell membrane controlled study cytotoxicity drug activity drug inhibition endosome glycoprotein synthesis Herpes simplex virus 1 human human cell immunomodulation integument Melia azedarach membrane transport nonhuman priority journal protein binding protein localization protein transport virogenesis virus capsid Antiviral Agents Cell Line Glycoproteins Herpesvirus 1, Human Humans Limonins Macrolides Melia azedarach Monensin Protein Transport Receptors, Transferrin Tumor Necrosis Factor-alpha Viral Envelope Proteins Virus Replication Human herpesvirus 1 Melia azedarach Miridae |
| spellingShingle |
Antiviral Golgi apparatus Medicinal plants Secretory pathway Transferrin receptor 1 cinnamoyl 3,11 dihydroxymeliacarpin concanamycin A glycoprotein Melia azedarach extract monensin transferrin receptor triterpenoid unclassified drug alkalinization article cell compartmentalization cell membrane controlled study cytotoxicity drug activity drug inhibition endosome glycoprotein synthesis Herpes simplex virus 1 human human cell immunomodulation integument Melia azedarach membrane transport nonhuman priority journal protein binding protein localization protein transport virogenesis virus capsid Antiviral Agents Cell Line Glycoproteins Herpesvirus 1, Human Humans Limonins Macrolides Melia azedarach Monensin Protein Transport Receptors, Transferrin Tumor Necrosis Factor-alpha Viral Envelope Proteins Virus Replication Human herpesvirus 1 Melia azedarach Miridae Bueno, Carlos Alberto Alche, Laura Edith Barquero, Andrea Alejandra 1-Cinnamoyl-3,11-dihydroxymeliacarpin delays glycoprotein transport restraining virus multiplication without cytotoxicity |
| topic_facet |
Antiviral Golgi apparatus Medicinal plants Secretory pathway Transferrin receptor 1 cinnamoyl 3,11 dihydroxymeliacarpin concanamycin A glycoprotein Melia azedarach extract monensin transferrin receptor triterpenoid unclassified drug alkalinization article cell compartmentalization cell membrane controlled study cytotoxicity drug activity drug inhibition endosome glycoprotein synthesis Herpes simplex virus 1 human human cell immunomodulation integument Melia azedarach membrane transport nonhuman priority journal protein binding protein localization protein transport virogenesis virus capsid Antiviral Agents Cell Line Glycoproteins Herpesvirus 1, Human Humans Limonins Macrolides Melia azedarach Monensin Protein Transport Receptors, Transferrin Tumor Necrosis Factor-alpha Viral Envelope Proteins Virus Replication Human herpesvirus 1 Melia azedarach Miridae |
| description |
The 1-cinnamoyl-3,11-dihydroxymeliacarpin (CDM), isolated from extracts of Melia azedarach L., displays antiviral and immunomodulating properties. CDM is the first reported tetranortriterpenoid responsible for the alkalinization of intracellular compartments affecting both, viral endocytic and exocytic pathways. Considering that viral glycoprotein synthesis is completely dependent upon cellular membrane trafficking, we questioned whether CDM might also interfere with the normal transport of cellular glycoproteins. This study demonstrates that CDM promoted a transient block in the transport of two cellular glycoproteins, the transferrin receptor (TfR) and TNF-α. Nevertheless, CDM did not affect the transferrin binding ability of TfR and did not impede the TNF-α secretion. On the other hand, CDM disturbed the intracellular localization of capsid, glycoprotein and tegument proteins simultaneously in the same HSV-1 infected cells. Besides, we show that concanamycin A and monensin provoke a permanent blockage of viral and cellular glycoproteins, in contrast to the delay observed after CDM treatment. Thus, the delay on glycoprotein transport caused by CDM would account for the strong inhibition on virus multiplication without interfering with the bioactivity of cellular glycoproteins. © 2010 Elsevier Inc. All rights reserved. |
| author |
Bueno, Carlos Alberto Alche, Laura Edith Barquero, Andrea Alejandra |
| author_facet |
Bueno, Carlos Alberto Alche, Laura Edith Barquero, Andrea Alejandra |
| author_sort |
Bueno, Carlos Alberto |
| title |
1-Cinnamoyl-3,11-dihydroxymeliacarpin delays glycoprotein transport restraining virus multiplication without cytotoxicity |
| title_short |
1-Cinnamoyl-3,11-dihydroxymeliacarpin delays glycoprotein transport restraining virus multiplication without cytotoxicity |
| title_full |
1-Cinnamoyl-3,11-dihydroxymeliacarpin delays glycoprotein transport restraining virus multiplication without cytotoxicity |
| title_fullStr |
1-Cinnamoyl-3,11-dihydroxymeliacarpin delays glycoprotein transport restraining virus multiplication without cytotoxicity |
| title_full_unstemmed |
1-Cinnamoyl-3,11-dihydroxymeliacarpin delays glycoprotein transport restraining virus multiplication without cytotoxicity |
| title_sort |
1-cinnamoyl-3,11-dihydroxymeliacarpin delays glycoprotein transport restraining virus multiplication without cytotoxicity |
| publishDate |
2010 |
| url |
https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_0006291X_v393_n1_p32_Bueno http://hdl.handle.net/20.500.12110/paper_0006291X_v393_n1_p32_Bueno |
| work_keys_str_mv |
AT buenocarlosalberto 1cinnamoyl311dihydroxymeliacarpindelaysglycoproteintransportrestrainingvirusmultiplicationwithoutcytotoxicity AT alchelauraedith 1cinnamoyl311dihydroxymeliacarpindelaysglycoproteintransportrestrainingvirusmultiplicationwithoutcytotoxicity AT barqueroandreaalejandra 1cinnamoyl311dihydroxymeliacarpindelaysglycoproteintransportrestrainingvirusmultiplicationwithoutcytotoxicity |
| _version_ |
1768541637951094784 |