Antagonism of BST-2/Tetherin is a conserved function of the Env glycoprotein of primary HIV-2 isolates

Detalhes bibliográficos
Autor(a) principal: Chen, Chia-Yen
Data de Publicação: 2016
Outros Autores: Shingai, Masashi, Welbourn, Sarah, Martin, Malcolm A., Borrego, Pedro, Taveira, Nuno, Strebel, Klaus
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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spelling 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
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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 reponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação
instacron:RCAAP
instname_str Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação
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collection Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
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