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Human herpesvirus 6 envelope components enriched in lipid rafts: evidence for virion-associated lipid rafts

In general, enveloped viruses are highly dependent on their lipid envelope for entry into host cells. Here, we demonstrated that during the course of virus maturation, a significant proportion of human herpesvirus 6 (HHV-6) envelope proteins were selectively concentrated in the detergent-resistant g...

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Detalles Bibliográficos
Autores principales: Kawabata, Akiko, Tang, Huamin, Huang, Honglan, Yamanishi, Koichi, Mori, Yasuko
Formato: Texto
Lenguaje:English
Publicado: BioMed Central 2009
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2743664/
https://www.ncbi.nlm.nih.gov/pubmed/19689819
http://dx.doi.org/10.1186/1743-422X-6-127
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author Kawabata, Akiko
Tang, Huamin
Huang, Honglan
Yamanishi, Koichi
Mori, Yasuko
author_facet Kawabata, Akiko
Tang, Huamin
Huang, Honglan
Yamanishi, Koichi
Mori, Yasuko
author_sort Kawabata, Akiko
collection PubMed
description In general, enveloped viruses are highly dependent on their lipid envelope for entry into host cells. Here, we demonstrated that during the course of virus maturation, a significant proportion of human herpesvirus 6 (HHV-6) envelope proteins were selectively concentrated in the detergent-resistant glycosphingolipid- and cholesterol-rich membranes (rafts) in HHV-6-infected cells. In addition, the ganglioside GM1, which is known to partition preferentially into lipid rafts, was detected in purified virions, along with viral envelope glycoproteins, gH, gL, gB, gQ1, gQ2 and gO indicating that at least one raft component was included in the viral particle during the assembly process.
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spelling pubmed-27436642009-09-15 Human herpesvirus 6 envelope components enriched in lipid rafts: evidence for virion-associated lipid rafts Kawabata, Akiko Tang, Huamin Huang, Honglan Yamanishi, Koichi Mori, Yasuko Virol J Research In general, enveloped viruses are highly dependent on their lipid envelope for entry into host cells. Here, we demonstrated that during the course of virus maturation, a significant proportion of human herpesvirus 6 (HHV-6) envelope proteins were selectively concentrated in the detergent-resistant glycosphingolipid- and cholesterol-rich membranes (rafts) in HHV-6-infected cells. In addition, the ganglioside GM1, which is known to partition preferentially into lipid rafts, was detected in purified virions, along with viral envelope glycoproteins, gH, gL, gB, gQ1, gQ2 and gO indicating that at least one raft component was included in the viral particle during the assembly process. BioMed Central 2009-08-19 /pmc/articles/PMC2743664/ /pubmed/19689819 http://dx.doi.org/10.1186/1743-422X-6-127 Text en Copyright ©2009 Kawabata et al; licensee BioMed Central Ltd. http://creativecommons.org/licenses/by/2.0 This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Research
Kawabata, Akiko
Tang, Huamin
Huang, Honglan
Yamanishi, Koichi
Mori, Yasuko
Human herpesvirus 6 envelope components enriched in lipid rafts: evidence for virion-associated lipid rafts
title Human herpesvirus 6 envelope components enriched in lipid rafts: evidence for virion-associated lipid rafts
title_full Human herpesvirus 6 envelope components enriched in lipid rafts: evidence for virion-associated lipid rafts
title_fullStr Human herpesvirus 6 envelope components enriched in lipid rafts: evidence for virion-associated lipid rafts
title_full_unstemmed Human herpesvirus 6 envelope components enriched in lipid rafts: evidence for virion-associated lipid rafts
title_short Human herpesvirus 6 envelope components enriched in lipid rafts: evidence for virion-associated lipid rafts
title_sort human herpesvirus 6 envelope components enriched in lipid rafts: evidence for virion-associated lipid rafts
topic Research
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2743664/
https://www.ncbi.nlm.nih.gov/pubmed/19689819
http://dx.doi.org/10.1186/1743-422X-6-127
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