A rare missense variant abrogates the signaling activity of tetherin/BST-2 without affecting its effect on virus release

Background Tetherin (or BST-2) is an antiviral host restriction factor that suppresses the release of HIV-1 and other enveloped viruses by tethering them to the cell surface. Recently, it has been demonstrated that tetherin also acts as an innate sensor of HIV-1 assembly that induces NF-κB-dependent...
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Autor*in:	Sauter, Daniel [verfasserIn] Hotter, Dominik Engelhart, Susanne Giehler, Fabian Kieser, Arnd Kubisch, Christian Kirchhoff, Frank

Format:	E-Artikel
Sprache:	Englisch

Erschienen:	2013

Schlagwörter:	293T Cell Missense Variant Internalization Rate Chugai Pharmaceutical Gaussia Luciferase

Anmerkung:	© Sauter et al.; licensee BioMed Central Ltd. 2013

Übergeordnetes Werk:	Enthalten in: Retrovirology - London : BioMed Central, 2004, 10(2013), 1 vom: 10. Aug.
Übergeordnetes Werk:	volume:10 ; year:2013 ; number:1 ; day:10 ; month:08

Links:	Volltext

DOI / URN:	10.1186/1742-4690-10-85

Katalog-ID:	SPR029170125

Internformat


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100	1		\|a Sauter, Daniel \|e verfasserin \|4 aut
245	1	2	\|a A rare missense variant abrogates the signaling activity of tetherin/BST-2 without affecting its effect on virus release
264		1	\|c 2013
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520			\|a Background Tetherin (or BST-2) is an antiviral host restriction factor that suppresses the release of HIV-1 and other enveloped viruses by tethering them to the cell surface. Recently, it has been demonstrated that tetherin also acts as an innate sensor of HIV-1 assembly that induces NF-κB-dependent proinflammatory responses. Furthermore, it has been reported that polymorphisms in the promoter and 3‘ untranslated region of the bst2 gene may affect the clinical outcome of HIV-1 infection. However, non-synonymous polymorphisms in the bst2 open reading frame have not yet been described or functionally characterized. Results Mining of the Exome Variant Server database identified seven very rare naturally occurring missense variants of tetherin (Y8H, R19H, N49S, D103N, E117A, D129E and V146L) in human populations. Functional analyses showed that none of these sequence variants significantly affects the ability of tetherin to inhibit HIV-1 virion release or its sensitivity to antagonism by HIV-1 Vpu or SIVtan Env, although Y8H alters a potential YxY endocytic motif proposed to play a role in virion uptake. Thus, these variants do most likely not represent an evolutionary advantage in directly controlling HIV-1 replication or spread. Interestingly, however, the R19H variant selectively abrogated the signaling activity of tetherin. Conclusions Restriction of HIV-1 virion release and immune sensing are two separable functions of human tetherin and the latter activity is severely impaired by a single amino acid variant (R19H) in the cytoplasmic part of tetherin.
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700	1		\|a Hotter, Dominik \|4 aut
700	1		\|a Engelhart, Susanne \|4 aut
700	1		\|a Giehler, Fabian \|4 aut
700	1		\|a Kieser, Arnd \|4 aut
700	1		\|a Kubisch, Christian \|4 aut
700	1		\|a Kirchhoff, Frank \|4 aut
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912			\|a GBV_ILN_4338
912			\|a GBV_ILN_4367
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952			\|d 10 \|j 2013 \|e 1 \|b 10 \|c 08

Indexfelder

author_variant	d s ds d h dh s e se f g fg a k ak c k ck f k fk
matchkey_str	article:17424690:2013----::rrmsesvratboaeteinlnatvtotteibtwtotfe
hierarchy_sort_str	2013
publishDate	2013
allfields	10.1186/1742-4690-10-85 doi (DE-627)SPR029170125 (SPR)1742-4690-10-85-e DE-627 ger DE-627 rakwb eng Sauter, Daniel verfasserin aut A rare missense variant abrogates the signaling activity of tetherin/BST-2 without affecting its effect on virus release 2013 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Sauter et al.; licensee BioMed Central Ltd. 2013 Background Tetherin (or BST-2) is an antiviral host restriction factor that suppresses the release of HIV-1 and other enveloped viruses by tethering them to the cell surface. Recently, it has been demonstrated that tetherin also acts as an innate sensor of HIV-1 assembly that induces NF-κB-dependent proinflammatory responses. Furthermore, it has been reported that polymorphisms in the promoter and 3‘ untranslated region of the bst2 gene may affect the clinical outcome of HIV-1 infection. However, non-synonymous polymorphisms in the bst2 open reading frame have not yet been described or functionally characterized. Results Mining of the Exome Variant Server database identified seven very rare naturally occurring missense variants of tetherin (Y8H, R19H, N49S, D103N, E117A, D129E and V146L) in human populations. Functional analyses showed that none of these sequence variants significantly affects the ability of tetherin to inhibit HIV-1 virion release or its sensitivity to antagonism by HIV-1 Vpu or SIVtan Env, although Y8H alters a potential YxY endocytic motif proposed to play a role in virion uptake. Thus, these variants do most likely not represent an evolutionary advantage in directly controlling HIV-1 replication or spread. Interestingly, however, the R19H variant selectively abrogated the signaling activity of tetherin. Conclusions Restriction of HIV-1 virion release and immune sensing are two separable functions of human tetherin and the latter activity is severely impaired by a single amino acid variant (R19H) in the cytoplasmic part of tetherin. 293T Cell (dpeaa)DE-He213 Missense Variant (dpeaa)DE-He213 Internalization Rate (dpeaa)DE-He213 Chugai Pharmaceutical (dpeaa)DE-He213 Gaussia Luciferase (dpeaa)DE-He213 Hotter, Dominik aut Engelhart, Susanne aut Giehler, Fabian aut Kieser, Arnd aut Kubisch, Christian aut Kirchhoff, Frank aut Enthalten in Retrovirology London : BioMed Central, 2004 10(2013), 1 vom: 10. Aug. (DE-627)385612931 (DE-600)2142602-8 1742-4690 nnns volume:10 year:2013 number:1 day:10 month:08 https://dx.doi.org/10.1186/1742-4690-10-85 kostenfrei Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2031 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2061 GBV_ILN_2111 GBV_ILN_2113 GBV_ILN_2190 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 10 2013 1 10 08
spelling	10.1186/1742-4690-10-85 doi (DE-627)SPR029170125 (SPR)1742-4690-10-85-e DE-627 ger DE-627 rakwb eng Sauter, Daniel verfasserin aut A rare missense variant abrogates the signaling activity of tetherin/BST-2 without affecting its effect on virus release 2013 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Sauter et al.; licensee BioMed Central Ltd. 2013 Background Tetherin (or BST-2) is an antiviral host restriction factor that suppresses the release of HIV-1 and other enveloped viruses by tethering them to the cell surface. Recently, it has been demonstrated that tetherin also acts as an innate sensor of HIV-1 assembly that induces NF-κB-dependent proinflammatory responses. Furthermore, it has been reported that polymorphisms in the promoter and 3‘ untranslated region of the bst2 gene may affect the clinical outcome of HIV-1 infection. However, non-synonymous polymorphisms in the bst2 open reading frame have not yet been described or functionally characterized. Results Mining of the Exome Variant Server database identified seven very rare naturally occurring missense variants of tetherin (Y8H, R19H, N49S, D103N, E117A, D129E and V146L) in human populations. Functional analyses showed that none of these sequence variants significantly affects the ability of tetherin to inhibit HIV-1 virion release or its sensitivity to antagonism by HIV-1 Vpu or SIVtan Env, although Y8H alters a potential YxY endocytic motif proposed to play a role in virion uptake. Thus, these variants do most likely not represent an evolutionary advantage in directly controlling HIV-1 replication or spread. Interestingly, however, the R19H variant selectively abrogated the signaling activity of tetherin. Conclusions Restriction of HIV-1 virion release and immune sensing are two separable functions of human tetherin and the latter activity is severely impaired by a single amino acid variant (R19H) in the cytoplasmic part of tetherin. 293T Cell (dpeaa)DE-He213 Missense Variant (dpeaa)DE-He213 Internalization Rate (dpeaa)DE-He213 Chugai Pharmaceutical (dpeaa)DE-He213 Gaussia Luciferase (dpeaa)DE-He213 Hotter, Dominik aut Engelhart, Susanne aut Giehler, Fabian aut Kieser, Arnd aut Kubisch, Christian aut Kirchhoff, Frank aut Enthalten in Retrovirology London : BioMed Central, 2004 10(2013), 1 vom: 10. Aug. (DE-627)385612931 (DE-600)2142602-8 1742-4690 nnns volume:10 year:2013 number:1 day:10 month:08 https://dx.doi.org/10.1186/1742-4690-10-85 kostenfrei Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2031 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2061 GBV_ILN_2111 GBV_ILN_2113 GBV_ILN_2190 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 10 2013 1 10 08
allfields_unstemmed	10.1186/1742-4690-10-85 doi (DE-627)SPR029170125 (SPR)1742-4690-10-85-e DE-627 ger DE-627 rakwb eng Sauter, Daniel verfasserin aut A rare missense variant abrogates the signaling activity of tetherin/BST-2 without affecting its effect on virus release 2013 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Sauter et al.; licensee BioMed Central Ltd. 2013 Background Tetherin (or BST-2) is an antiviral host restriction factor that suppresses the release of HIV-1 and other enveloped viruses by tethering them to the cell surface. Recently, it has been demonstrated that tetherin also acts as an innate sensor of HIV-1 assembly that induces NF-κB-dependent proinflammatory responses. Furthermore, it has been reported that polymorphisms in the promoter and 3‘ untranslated region of the bst2 gene may affect the clinical outcome of HIV-1 infection. However, non-synonymous polymorphisms in the bst2 open reading frame have not yet been described or functionally characterized. Results Mining of the Exome Variant Server database identified seven very rare naturally occurring missense variants of tetherin (Y8H, R19H, N49S, D103N, E117A, D129E and V146L) in human populations. Functional analyses showed that none of these sequence variants significantly affects the ability of tetherin to inhibit HIV-1 virion release or its sensitivity to antagonism by HIV-1 Vpu or SIVtan Env, although Y8H alters a potential YxY endocytic motif proposed to play a role in virion uptake. Thus, these variants do most likely not represent an evolutionary advantage in directly controlling HIV-1 replication or spread. Interestingly, however, the R19H variant selectively abrogated the signaling activity of tetherin. Conclusions Restriction of HIV-1 virion release and immune sensing are two separable functions of human tetherin and the latter activity is severely impaired by a single amino acid variant (R19H) in the cytoplasmic part of tetherin. 293T Cell (dpeaa)DE-He213 Missense Variant (dpeaa)DE-He213 Internalization Rate (dpeaa)DE-He213 Chugai Pharmaceutical (dpeaa)DE-He213 Gaussia Luciferase (dpeaa)DE-He213 Hotter, Dominik aut Engelhart, Susanne aut Giehler, Fabian aut Kieser, Arnd aut Kubisch, Christian aut Kirchhoff, Frank aut Enthalten in Retrovirology London : BioMed Central, 2004 10(2013), 1 vom: 10. Aug. (DE-627)385612931 (DE-600)2142602-8 1742-4690 nnns volume:10 year:2013 number:1 day:10 month:08 https://dx.doi.org/10.1186/1742-4690-10-85 kostenfrei Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2031 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2061 GBV_ILN_2111 GBV_ILN_2113 GBV_ILN_2190 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 10 2013 1 10 08
allfieldsGer	10.1186/1742-4690-10-85 doi (DE-627)SPR029170125 (SPR)1742-4690-10-85-e DE-627 ger DE-627 rakwb eng Sauter, Daniel verfasserin aut A rare missense variant abrogates the signaling activity of tetherin/BST-2 without affecting its effect on virus release 2013 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Sauter et al.; licensee BioMed Central Ltd. 2013 Background Tetherin (or BST-2) is an antiviral host restriction factor that suppresses the release of HIV-1 and other enveloped viruses by tethering them to the cell surface. Recently, it has been demonstrated that tetherin also acts as an innate sensor of HIV-1 assembly that induces NF-κB-dependent proinflammatory responses. Furthermore, it has been reported that polymorphisms in the promoter and 3‘ untranslated region of the bst2 gene may affect the clinical outcome of HIV-1 infection. However, non-synonymous polymorphisms in the bst2 open reading frame have not yet been described or functionally characterized. Results Mining of the Exome Variant Server database identified seven very rare naturally occurring missense variants of tetherin (Y8H, R19H, N49S, D103N, E117A, D129E and V146L) in human populations. Functional analyses showed that none of these sequence variants significantly affects the ability of tetherin to inhibit HIV-1 virion release or its sensitivity to antagonism by HIV-1 Vpu or SIVtan Env, although Y8H alters a potential YxY endocytic motif proposed to play a role in virion uptake. Thus, these variants do most likely not represent an evolutionary advantage in directly controlling HIV-1 replication or spread. Interestingly, however, the R19H variant selectively abrogated the signaling activity of tetherin. Conclusions Restriction of HIV-1 virion release and immune sensing are two separable functions of human tetherin and the latter activity is severely impaired by a single amino acid variant (R19H) in the cytoplasmic part of tetherin. 293T Cell (dpeaa)DE-He213 Missense Variant (dpeaa)DE-He213 Internalization Rate (dpeaa)DE-He213 Chugai Pharmaceutical (dpeaa)DE-He213 Gaussia Luciferase (dpeaa)DE-He213 Hotter, Dominik aut Engelhart, Susanne aut Giehler, Fabian aut Kieser, Arnd aut Kubisch, Christian aut Kirchhoff, Frank aut Enthalten in Retrovirology London : BioMed Central, 2004 10(2013), 1 vom: 10. Aug. (DE-627)385612931 (DE-600)2142602-8 1742-4690 nnns volume:10 year:2013 number:1 day:10 month:08 https://dx.doi.org/10.1186/1742-4690-10-85 kostenfrei Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2031 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2061 GBV_ILN_2111 GBV_ILN_2113 GBV_ILN_2190 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 10 2013 1 10 08
allfieldsSound	10.1186/1742-4690-10-85 doi (DE-627)SPR029170125 (SPR)1742-4690-10-85-e DE-627 ger DE-627 rakwb eng Sauter, Daniel verfasserin aut A rare missense variant abrogates the signaling activity of tetherin/BST-2 without affecting its effect on virus release 2013 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Sauter et al.; licensee BioMed Central Ltd. 2013 Background Tetherin (or BST-2) is an antiviral host restriction factor that suppresses the release of HIV-1 and other enveloped viruses by tethering them to the cell surface. Recently, it has been demonstrated that tetherin also acts as an innate sensor of HIV-1 assembly that induces NF-κB-dependent proinflammatory responses. Furthermore, it has been reported that polymorphisms in the promoter and 3‘ untranslated region of the bst2 gene may affect the clinical outcome of HIV-1 infection. However, non-synonymous polymorphisms in the bst2 open reading frame have not yet been described or functionally characterized. Results Mining of the Exome Variant Server database identified seven very rare naturally occurring missense variants of tetherin (Y8H, R19H, N49S, D103N, E117A, D129E and V146L) in human populations. Functional analyses showed that none of these sequence variants significantly affects the ability of tetherin to inhibit HIV-1 virion release or its sensitivity to antagonism by HIV-1 Vpu or SIVtan Env, although Y8H alters a potential YxY endocytic motif proposed to play a role in virion uptake. Thus, these variants do most likely not represent an evolutionary advantage in directly controlling HIV-1 replication or spread. Interestingly, however, the R19H variant selectively abrogated the signaling activity of tetherin. Conclusions Restriction of HIV-1 virion release and immune sensing are two separable functions of human tetherin and the latter activity is severely impaired by a single amino acid variant (R19H) in the cytoplasmic part of tetherin. 293T Cell (dpeaa)DE-He213 Missense Variant (dpeaa)DE-He213 Internalization Rate (dpeaa)DE-He213 Chugai Pharmaceutical (dpeaa)DE-He213 Gaussia Luciferase (dpeaa)DE-He213 Hotter, Dominik aut Engelhart, Susanne aut Giehler, Fabian aut Kieser, Arnd aut Kubisch, Christian aut Kirchhoff, Frank aut Enthalten in Retrovirology London : BioMed Central, 2004 10(2013), 1 vom: 10. Aug. (DE-627)385612931 (DE-600)2142602-8 1742-4690 nnns volume:10 year:2013 number:1 day:10 month:08 https://dx.doi.org/10.1186/1742-4690-10-85 kostenfrei Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2031 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2061 GBV_ILN_2111 GBV_ILN_2113 GBV_ILN_2190 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 10 2013 1 10 08
language	English
source	Enthalten in Retrovirology 10(2013), 1 vom: 10. Aug. volume:10 year:2013 number:1 day:10 month:08
sourceStr	Enthalten in Retrovirology 10(2013), 1 vom: 10. Aug. volume:10 year:2013 number:1 day:10 month:08
format_phy_str_mv	Article
institution	findex.gbv.de
topic_facet	293T Cell Missense Variant Internalization Rate Chugai Pharmaceutical Gaussia Luciferase
isfreeaccess_bool	true
container_title	Retrovirology
authorswithroles_txt_mv	Sauter, Daniel @@aut@@ Hotter, Dominik @@aut@@ Engelhart, Susanne @@aut@@ Giehler, Fabian @@aut@@ Kieser, Arnd @@aut@@ Kubisch, Christian @@aut@@ Kirchhoff, Frank @@aut@@
publishDateDaySort_date	2013-08-10T00:00:00Z
hierarchy_top_id	385612931
id	SPR029170125
language_de	englisch
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Recently, it has been demonstrated that tetherin also acts as an innate sensor of HIV-1 assembly that induces NF-κB-dependent proinflammatory responses. Furthermore, it has been reported that polymorphisms in the promoter and 3‘ untranslated region of the bst2 gene may affect the clinical outcome of HIV-1 infection. However, non-synonymous polymorphisms in the bst2 open reading frame have not yet been described or functionally characterized. Results Mining of the Exome Variant Server database identified seven very rare naturally occurring missense variants of tetherin (Y8H, R19H, N49S, D103N, E117A, D129E and V146L) in human populations. Functional analyses showed that none of these sequence variants significantly affects the ability of tetherin to inhibit HIV-1 virion release or its sensitivity to antagonism by HIV-1 Vpu or SIVtan Env, although Y8H alters a potential YxY endocytic motif proposed to play a role in virion uptake. 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author	Sauter, Daniel
spellingShingle	Sauter, Daniel misc 293T Cell misc Missense Variant misc Internalization Rate misc Chugai Pharmaceutical misc Gaussia Luciferase A rare missense variant abrogates the signaling activity of tetherin/BST-2 without affecting its effect on virus release
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topic_title	A rare missense variant abrogates the signaling activity of tetherin/BST-2 without affecting its effect on virus release 293T Cell (dpeaa)DE-He213 Missense Variant (dpeaa)DE-He213 Internalization Rate (dpeaa)DE-He213 Chugai Pharmaceutical (dpeaa)DE-He213 Gaussia Luciferase (dpeaa)DE-He213
topic	misc 293T Cell misc Missense Variant misc Internalization Rate misc Chugai Pharmaceutical misc Gaussia Luciferase
topic_unstemmed	misc 293T Cell misc Missense Variant misc Internalization Rate misc Chugai Pharmaceutical misc Gaussia Luciferase
topic_browse	misc 293T Cell misc Missense Variant misc Internalization Rate misc Chugai Pharmaceutical misc Gaussia Luciferase
format_facet	Elektronische Aufsätze Aufsätze Elektronische Ressource
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title	A rare missense variant abrogates the signaling activity of tetherin/BST-2 without affecting its effect on virus release
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title_full	A rare missense variant abrogates the signaling activity of tetherin/BST-2 without affecting its effect on virus release
author_sort	Sauter, Daniel
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author_browse	Sauter, Daniel Hotter, Dominik Engelhart, Susanne Giehler, Fabian Kieser, Arnd Kubisch, Christian Kirchhoff, Frank
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author-letter	Sauter, Daniel
doi_str_mv	10.1186/1742-4690-10-85
title_sort	rare missense variant abrogates the signaling activity of tetherin/bst-2 without affecting its effect on virus release
title_auth	A rare missense variant abrogates the signaling activity of tetherin/BST-2 without affecting its effect on virus release
abstract	Background Tetherin (or BST-2) is an antiviral host restriction factor that suppresses the release of HIV-1 and other enveloped viruses by tethering them to the cell surface. Recently, it has been demonstrated that tetherin also acts as an innate sensor of HIV-1 assembly that induces NF-κB-dependent proinflammatory responses. Furthermore, it has been reported that polymorphisms in the promoter and 3‘ untranslated region of the bst2 gene may affect the clinical outcome of HIV-1 infection. However, non-synonymous polymorphisms in the bst2 open reading frame have not yet been described or functionally characterized. Results Mining of the Exome Variant Server database identified seven very rare naturally occurring missense variants of tetherin (Y8H, R19H, N49S, D103N, E117A, D129E and V146L) in human populations. Functional analyses showed that none of these sequence variants significantly affects the ability of tetherin to inhibit HIV-1 virion release or its sensitivity to antagonism by HIV-1 Vpu or SIVtan Env, although Y8H alters a potential YxY endocytic motif proposed to play a role in virion uptake. Thus, these variants do most likely not represent an evolutionary advantage in directly controlling HIV-1 replication or spread. Interestingly, however, the R19H variant selectively abrogated the signaling activity of tetherin. Conclusions Restriction of HIV-1 virion release and immune sensing are two separable functions of human tetherin and the latter activity is severely impaired by a single amino acid variant (R19H) in the cytoplasmic part of tetherin. © Sauter et al.; licensee BioMed Central Ltd. 2013
abstractGer	Background Tetherin (or BST-2) is an antiviral host restriction factor that suppresses the release of HIV-1 and other enveloped viruses by tethering them to the cell surface. Recently, it has been demonstrated that tetherin also acts as an innate sensor of HIV-1 assembly that induces NF-κB-dependent proinflammatory responses. Furthermore, it has been reported that polymorphisms in the promoter and 3‘ untranslated region of the bst2 gene may affect the clinical outcome of HIV-1 infection. However, non-synonymous polymorphisms in the bst2 open reading frame have not yet been described or functionally characterized. Results Mining of the Exome Variant Server database identified seven very rare naturally occurring missense variants of tetherin (Y8H, R19H, N49S, D103N, E117A, D129E and V146L) in human populations. Functional analyses showed that none of these sequence variants significantly affects the ability of tetherin to inhibit HIV-1 virion release or its sensitivity to antagonism by HIV-1 Vpu or SIVtan Env, although Y8H alters a potential YxY endocytic motif proposed to play a role in virion uptake. Thus, these variants do most likely not represent an evolutionary advantage in directly controlling HIV-1 replication or spread. Interestingly, however, the R19H variant selectively abrogated the signaling activity of tetherin. Conclusions Restriction of HIV-1 virion release and immune sensing are two separable functions of human tetherin and the latter activity is severely impaired by a single amino acid variant (R19H) in the cytoplasmic part of tetherin. © Sauter et al.; licensee BioMed Central Ltd. 2013
abstract_unstemmed	Background Tetherin (or BST-2) is an antiviral host restriction factor that suppresses the release of HIV-1 and other enveloped viruses by tethering them to the cell surface. Recently, it has been demonstrated that tetherin also acts as an innate sensor of HIV-1 assembly that induces NF-κB-dependent proinflammatory responses. Furthermore, it has been reported that polymorphisms in the promoter and 3‘ untranslated region of the bst2 gene may affect the clinical outcome of HIV-1 infection. However, non-synonymous polymorphisms in the bst2 open reading frame have not yet been described or functionally characterized. Results Mining of the Exome Variant Server database identified seven very rare naturally occurring missense variants of tetherin (Y8H, R19H, N49S, D103N, E117A, D129E and V146L) in human populations. Functional analyses showed that none of these sequence variants significantly affects the ability of tetherin to inhibit HIV-1 virion release or its sensitivity to antagonism by HIV-1 Vpu or SIVtan Env, although Y8H alters a potential YxY endocytic motif proposed to play a role in virion uptake. Thus, these variants do most likely not represent an evolutionary advantage in directly controlling HIV-1 replication or spread. Interestingly, however, the R19H variant selectively abrogated the signaling activity of tetherin. Conclusions Restriction of HIV-1 virion release and immune sensing are two separable functions of human tetherin and the latter activity is severely impaired by a single amino acid variant (R19H) in the cytoplasmic part of tetherin. © Sauter et al.; licensee BioMed Central Ltd. 2013
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title_short	A rare missense variant abrogates the signaling activity of tetherin/BST-2 without affecting its effect on virus release
url	https://dx.doi.org/10.1186/1742-4690-10-85
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author2	Hotter, Dominik Engelhart, Susanne Giehler, Fabian Kieser, Arnd Kubisch, Christian Kirchhoff, Frank
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A rare missense variant abrogates the signaling activity of tetherin/BST-2 without affecting its effect on virus release

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