Antagonism of BST-2/Tetherin is a conserved function of the Env glycoprotein of primary HIV-2 isolates
Autor(a) principal: | |
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Data de Publicação: | 2016 |
Outros Autores: | , , , , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
Texto Completo: | http://hdl.handle.net/10400.26/30460 |
Resumo: | Although HIV-2 does not encode a vpu gene, the ability to antagonize bone marrow stromal antigen 2 (BST-2) is conserved in some HIV-2 isolates, where it is controlled by the Env glycoprotein. We previously reported that a single-amino-acid difference between the laboratory-adapted ROD10 and ROD14 Envs controlled the enhancement of virus release (referred to here as Vpu-like) activity. Here, we investigated how conserved the Vpu-like activity is in primary HIV-2 isolates. We found that half of the 34 tested primary HIV-2 Env isolates obtained from 7 different patients enhanced virus release. Interestingly, most HIV-2 patients harbored a mixed population of viruses containing or lacking Vpu-like activity. Vpu-like activity and Envelope functionality varied significantly among Env isolates; however, there was no direct correlation between these two functions, suggesting they evolved independently. In comparing the Env sequences from one HIV-2 patient, we found that similar to the ROD10/ROD14 Envs, a single-amino-acid change (T568I) in the ectodomain of the TM subunit was sufficient to confer Vpu-like activity to an inactive Env variant. Surprisingly, however, absence of Vpu-like activity was not correlated with absence of BST-2 interaction. Taken together, our data suggest that maintaining the ability to antagonize BST-2 is of functional relevance not only to HIV-1 but also to HIV-2 as well. Our data show that as with Vpu, binding of HIV-2 Env to BST-2 is important but not sufficient for antagonism. Finally, as observed previously, the Vpu-like activity in HIV-2 Env can be controlled by single-residue changes in the TM subunit. |
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Antagonism of BST-2/Tetherin is a conserved function of the Env glycoprotein of primary HIV-2 isolatesBST-2/TetherinEnv GlycoproteinPrimary HIV-2 IsolatesAlthough HIV-2 does not encode a vpu gene, the ability to antagonize bone marrow stromal antigen 2 (BST-2) is conserved in some HIV-2 isolates, where it is controlled by the Env glycoprotein. We previously reported that a single-amino-acid difference between the laboratory-adapted ROD10 and ROD14 Envs controlled the enhancement of virus release (referred to here as Vpu-like) activity. Here, we investigated how conserved the Vpu-like activity is in primary HIV-2 isolates. We found that half of the 34 tested primary HIV-2 Env isolates obtained from 7 different patients enhanced virus release. Interestingly, most HIV-2 patients harbored a mixed population of viruses containing or lacking Vpu-like activity. Vpu-like activity and Envelope functionality varied significantly among Env isolates; however, there was no direct correlation between these two functions, suggesting they evolved independently. In comparing the Env sequences from one HIV-2 patient, we found that similar to the ROD10/ROD14 Envs, a single-amino-acid change (T568I) in the ectodomain of the TM subunit was sufficient to confer Vpu-like activity to an inactive Env variant. Surprisingly, however, absence of Vpu-like activity was not correlated with absence of BST-2 interaction. Taken together, our data suggest that maintaining the ability to antagonize BST-2 is of functional relevance not only to HIV-1 but also to HIV-2 as well. Our data show that as with Vpu, binding of HIV-2 Env to BST-2 is important but not sufficient for antagonism. Finally, as observed previously, the Vpu-like activity in HIV-2 Env can be controlled by single-residue changes in the TM subunit.American Society for MicrobiologyRepositório ComumChen, Chia-YenShingai, MasashiWelbourn, SarahMartin, Malcolm A.Borrego, PedroTaveira, NunoStrebel, Klaus2019-12-12T12:31:03Z2016-12-01T00:00:00Z2016-12-01T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfhttp://hdl.handle.net/10400.26/30460engChen C-Y, Shingai M, Welbourn S, Martin MA, Borrego P, Taveira N, Strebel K. 2016. Antagonism of BST-2/tetherin is a conserved function of the Env glycoprotein of primary HIV-2 isolates. J Virol 90:11062–11074. doi:10.1128/JVI.01451-160022-538X10.1128/JVI.01451-16info:eu-repo/semantics/openAccessreponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãoinstacron:RCAAP2022-10-06T14:53:51Zoai:comum.rcaap.pt:10400.26/30460Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-19T15:09:37.706814Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãofalse |
dc.title.none.fl_str_mv |
Antagonism of BST-2/Tetherin is a conserved function of the Env glycoprotein of primary HIV-2 isolates |
title |
Antagonism of BST-2/Tetherin is a conserved function of the Env glycoprotein of primary HIV-2 isolates |
spellingShingle |
Antagonism of BST-2/Tetherin is a conserved function of the Env glycoprotein of primary HIV-2 isolates Chen, Chia-Yen BST-2/Tetherin Env Glycoprotein Primary HIV-2 Isolates |
title_short |
Antagonism of BST-2/Tetherin is a conserved function of the Env glycoprotein of primary HIV-2 isolates |
title_full |
Antagonism of BST-2/Tetherin is a conserved function of the Env glycoprotein of primary HIV-2 isolates |
title_fullStr |
Antagonism of BST-2/Tetherin is a conserved function of the Env glycoprotein of primary HIV-2 isolates |
title_full_unstemmed |
Antagonism of BST-2/Tetherin is a conserved function of the Env glycoprotein of primary HIV-2 isolates |
title_sort |
Antagonism of BST-2/Tetherin is a conserved function of the Env glycoprotein of primary HIV-2 isolates |
author |
Chen, Chia-Yen |
author_facet |
Chen, Chia-Yen Shingai, Masashi Welbourn, Sarah Martin, Malcolm A. Borrego, Pedro Taveira, Nuno Strebel, Klaus |
author_role |
author |
author2 |
Shingai, Masashi Welbourn, Sarah Martin, Malcolm A. Borrego, Pedro Taveira, Nuno Strebel, Klaus |
author2_role |
author author author author author author |
dc.contributor.none.fl_str_mv |
Repositório Comum |
dc.contributor.author.fl_str_mv |
Chen, Chia-Yen Shingai, Masashi Welbourn, Sarah Martin, Malcolm A. Borrego, Pedro Taveira, Nuno Strebel, Klaus |
dc.subject.por.fl_str_mv |
BST-2/Tetherin Env Glycoprotein Primary HIV-2 Isolates |
topic |
BST-2/Tetherin Env Glycoprotein Primary HIV-2 Isolates |
description |
Although HIV-2 does not encode a vpu gene, the ability to antagonize bone marrow stromal antigen 2 (BST-2) is conserved in some HIV-2 isolates, where it is controlled by the Env glycoprotein. We previously reported that a single-amino-acid difference between the laboratory-adapted ROD10 and ROD14 Envs controlled the enhancement of virus release (referred to here as Vpu-like) activity. Here, we investigated how conserved the Vpu-like activity is in primary HIV-2 isolates. We found that half of the 34 tested primary HIV-2 Env isolates obtained from 7 different patients enhanced virus release. Interestingly, most HIV-2 patients harbored a mixed population of viruses containing or lacking Vpu-like activity. Vpu-like activity and Envelope functionality varied significantly among Env isolates; however, there was no direct correlation between these two functions, suggesting they evolved independently. In comparing the Env sequences from one HIV-2 patient, we found that similar to the ROD10/ROD14 Envs, a single-amino-acid change (T568I) in the ectodomain of the TM subunit was sufficient to confer Vpu-like activity to an inactive Env variant. Surprisingly, however, absence of Vpu-like activity was not correlated with absence of BST-2 interaction. Taken together, our data suggest that maintaining the ability to antagonize BST-2 is of functional relevance not only to HIV-1 but also to HIV-2 as well. Our data show that as with Vpu, binding of HIV-2 Env to BST-2 is important but not sufficient for antagonism. Finally, as observed previously, the Vpu-like activity in HIV-2 Env can be controlled by single-residue changes in the TM subunit. |
publishDate |
2016 |
dc.date.none.fl_str_mv |
2016-12-01T00:00:00Z 2016-12-01T00:00:00Z 2019-12-12T12:31:03Z |
dc.type.status.fl_str_mv |
info:eu-repo/semantics/publishedVersion |
dc.type.driver.fl_str_mv |
info:eu-repo/semantics/article |
format |
article |
status_str |
publishedVersion |
dc.identifier.uri.fl_str_mv |
http://hdl.handle.net/10400.26/30460 |
url |
http://hdl.handle.net/10400.26/30460 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
Chen C-Y, Shingai M, Welbourn S, Martin MA, Borrego P, Taveira N, Strebel K. 2016. Antagonism of BST-2/tetherin is a conserved function of the Env glycoprotein of primary HIV-2 isolates. J Virol 90:11062–11074. doi:10.1128/JVI.01451-16 0022-538X 10.1128/JVI.01451-16 |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.format.none.fl_str_mv |
application/pdf |
dc.publisher.none.fl_str_mv |
American Society for Microbiology |
publisher.none.fl_str_mv |
American Society for Microbiology |
dc.source.none.fl_str_mv |
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Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação |
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Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
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Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
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Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação |
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