HIV-1 ENVELOPE. Effect of the cytoplasmic domain on antigenic characteristics of HIV-1 envelope glycoprotein
A major goal for HIV-1 vaccine development is the production of an immunogen to mimic native, functional HIV-1 envelope trimeric spikes (Env) on the virion surface. We lack a reliable description of a native, functional trimer, however, because of inherent instability and heterogeneity in most prepa...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
Chen, Bing [verfasserIn] |
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| Format: |
Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
2015 |
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| Rechteinformationen: |
Nutzungsrecht: Copyright © 2015, American Association for the Advancement of Science. |
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| Übergeordnetes Werk: |
Enthalten in: Science - Washington, DC : AAAS, American Assoc. for the Advancement of Science, 1883, 349(2015), 6244, Seite 191 |
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| Übergeordnetes Werk: |
volume:349 ; year:2015 ; number:6244 ; pages:191 |
| Links: |
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| Katalog-ID: |
OLC1969532998 |
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| 245 | 1 | 0 | |a HIV-1 ENVELOPE. Effect of the cytoplasmic domain on antigenic characteristics of HIV-1 envelope glycoprotein |
| 264 | 1 | |c 2015 | |
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| 520 | |a A major goal for HIV-1 vaccine development is the production of an immunogen to mimic native, functional HIV-1 envelope trimeric spikes (Env) on the virion surface. We lack a reliable description of a native, functional trimer, however, because of inherent instability and heterogeneity in most preparations. We describe here two conformationally homogeneous Envs derived from difficult-to-neutralize primary isolates. All their non-neutralizing epitopes are fully concealed and independent of their proteolytic processing. Most broadly neutralizing antibodies (bnAbs) recognize these native trimers. Truncation of their cytoplasmic tail has little effect on membrane fusion, but it diminishes binding to trimer-specific bnAbs while exposing non-neutralizing epitopes. These results yield a more accurate antigenic picture than hitherto possible of a genuinely untriggered and functional HIV-1 Env; they can guide effective vaccine development. | ||
| 540 | |a Nutzungsrecht: Copyright © 2015, American Association for the Advancement of Science. | ||
| 650 | 4 | |a Antigens - chemistry | |
| 650 | 4 | |a Antigens - genetics | |
| 650 | 4 | |a HIV-1 - immunology | |
| 650 | 4 | |a Virion - immunology | |
| 650 | 4 | |a HIV Envelope Protein gp160 - chemistry | |
| 650 | 4 | |a HIV Antibodies - immunology | |
| 650 | 4 | |a HIV Envelope Protein gp41 - chemistry | |
| 650 | 4 | |a HIV Envelope Protein gp120 - immunology | |
| 650 | 4 | |a Cytoplasm - immunology | |
| 650 | 4 | |a HIV-1 - chemistry | |
| 650 | 4 | |a HIV Envelope Protein gp120 - genetics | |
| 650 | 4 | |a Epitopes - chemistry | |
| 650 | 4 | |a HIV Envelope Protein gp41 - genetics | |
| 650 | 4 | |a HIV Envelope Protein gp120 - chemistry | |
| 650 | 4 | |a Antigens, CD4 - immunology | |
| 650 | 4 | |a AIDS Vaccines - chemistry | |
| 650 | 4 | |a HIV Envelope Protein gp41 - immunology | |
| 650 | 4 | |a HIV Envelope Protein gp160 - immunology | |
| 650 | 4 | |a AIDS Vaccines - genetics | |
| 650 | 4 | |a AIDS Vaccines - immunology | |
| 650 | 4 | |a Antibodies, Neutralizing - immunology | |
| 650 | 4 | |a HIV Infections - prevention & control | |
| 650 | 4 | |a Epitopes - immunology | |
| 650 | 4 | |a Antigens - immunology | |
| 650 | 4 | |a Virion - chemistry | |
| 700 | 1 | |a Peng, Hanqin |4 oth | |
| 700 | 1 | |a Seaman, Michael S |4 oth | |
| 700 | 1 | |a Lu, Jianming |4 oth | |
| 700 | 1 | |a Kovacs, James M |4 oth | |
| 700 | 1 | |a Rits-Volloch, Sophia |4 oth | |
| 700 | 1 | |a Zablowsky, Elise |4 oth | |
| 700 | 1 | |a Park, Donghyun |4 oth | |
| 700 | 1 | |a Chen, Jia |4 oth | |
| 773 | 0 | 8 | |i Enthalten in |t Science |d Washington, DC : AAAS, American Assoc. for the Advancement of Science, 1883 |g 349(2015), 6244, Seite 191 |w (DE-627)12931482X |w (DE-600)128410-1 |w (DE-576)014533189 |x 0036-8075 |7 nnns |
| 773 | 1 | 8 | |g volume:349 |g year:2015 |g number:6244 |g pages:191 |
| 856 | 4 | 2 | |u http://www.ncbi.nlm.nih.gov/pubmed/26113642 |
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PQ20160211 (DE-627)OLC1969532998 (DE-599)GBVOLC1969532998 (PRQ)pubmed_primary_261136420 (KEY)0063888920150000349624400191hiv1envelopeeffectofthecytoplasmicdomainonantigeni DE-627 ger DE-627 rakwb eng 500 DNB LING fid Chen, Bing verfasserin aut HIV-1 ENVELOPE. Effect of the cytoplasmic domain on antigenic characteristics of HIV-1 envelope glycoprotein 2015 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier A major goal for HIV-1 vaccine development is the production of an immunogen to mimic native, functional HIV-1 envelope trimeric spikes (Env) on the virion surface. We lack a reliable description of a native, functional trimer, however, because of inherent instability and heterogeneity in most preparations. We describe here two conformationally homogeneous Envs derived from difficult-to-neutralize primary isolates. All their non-neutralizing epitopes are fully concealed and independent of their proteolytic processing. Most broadly neutralizing antibodies (bnAbs) recognize these native trimers. Truncation of their cytoplasmic tail has little effect on membrane fusion, but it diminishes binding to trimer-specific bnAbs while exposing non-neutralizing epitopes. These results yield a more accurate antigenic picture than hitherto possible of a genuinely untriggered and functional HIV-1 Env; they can guide effective vaccine development. Nutzungsrecht: Copyright © 2015, American Association for the Advancement of Science. Antigens - chemistry Antigens - genetics HIV-1 - immunology Virion - immunology HIV Envelope Protein gp160 - chemistry HIV Antibodies - immunology HIV Envelope Protein gp41 - chemistry HIV Envelope Protein gp120 - immunology Cytoplasm - immunology HIV-1 - chemistry HIV Envelope Protein gp120 - genetics Epitopes - chemistry HIV Envelope Protein gp41 - genetics HIV Envelope Protein gp120 - chemistry Antigens, CD4 - immunology AIDS Vaccines - chemistry HIV Envelope Protein gp41 - immunology HIV Envelope Protein gp160 - immunology AIDS Vaccines - genetics AIDS Vaccines - immunology Antibodies, Neutralizing - immunology HIV Infections - prevention & control Epitopes - immunology Antigens - immunology Virion - chemistry Peng, Hanqin oth Seaman, Michael S oth Lu, Jianming oth Kovacs, James M oth Rits-Volloch, Sophia oth Zablowsky, Elise oth Park, Donghyun oth Chen, Jia oth Enthalten in Science Washington, DC : AAAS, American Assoc. for the Advancement of Science, 1883 349(2015), 6244, Seite 191 (DE-627)12931482X (DE-600)128410-1 (DE-576)014533189 0036-8075 nnns volume:349 year:2015 number:6244 pages:191 http://www.ncbi.nlm.nih.gov/pubmed/26113642 GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-LING SSG-OLC-PHY SSG-OLC-CHE SSG-OLC-MAT SSG-OLC-FOR SSG-OLC-SPO SSG-OLC-IBL SSG-OLC-PHA SSG-OLC-DE-84 SSG-OPC-FOR GBV_ILN_11 GBV_ILN_20 GBV_ILN_21 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_30 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_47 GBV_ILN_55 GBV_ILN_59 GBV_ILN_60 GBV_ILN_62 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_92 GBV_ILN_101 GBV_ILN_110 GBV_ILN_120 GBV_ILN_131 GBV_ILN_170 GBV_ILN_171 GBV_ILN_179 GBV_ILN_181 GBV_ILN_211 GBV_ILN_252 GBV_ILN_259 GBV_ILN_290 GBV_ILN_600 GBV_ILN_601 GBV_ILN_647 GBV_ILN_754 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2012 GBV_ILN_2015 GBV_ILN_2018 GBV_ILN_2020 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2116 GBV_ILN_2120 GBV_ILN_2121 GBV_ILN_2173 GBV_ILN_2185 GBV_ILN_2219 GBV_ILN_2221 GBV_ILN_2279 GBV_ILN_2286 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4036 GBV_ILN_4046 GBV_ILN_4125 GBV_ILN_4219 GBV_ILN_4251 GBV_ILN_4277 GBV_ILN_4302 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4310 GBV_ILN_4314 GBV_ILN_4317 GBV_ILN_4318 GBV_ILN_4320 GBV_ILN_4324 GBV_ILN_4328 GBV_ILN_4333 GBV_ILN_4700 AR 349 2015 6244 191 |
| spelling |
PQ20160211 (DE-627)OLC1969532998 (DE-599)GBVOLC1969532998 (PRQ)pubmed_primary_261136420 (KEY)0063888920150000349624400191hiv1envelopeeffectofthecytoplasmicdomainonantigeni DE-627 ger DE-627 rakwb eng 500 DNB LING fid Chen, Bing verfasserin aut HIV-1 ENVELOPE. Effect of the cytoplasmic domain on antigenic characteristics of HIV-1 envelope glycoprotein 2015 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier A major goal for HIV-1 vaccine development is the production of an immunogen to mimic native, functional HIV-1 envelope trimeric spikes (Env) on the virion surface. We lack a reliable description of a native, functional trimer, however, because of inherent instability and heterogeneity in most preparations. We describe here two conformationally homogeneous Envs derived from difficult-to-neutralize primary isolates. All their non-neutralizing epitopes are fully concealed and independent of their proteolytic processing. Most broadly neutralizing antibodies (bnAbs) recognize these native trimers. Truncation of their cytoplasmic tail has little effect on membrane fusion, but it diminishes binding to trimer-specific bnAbs while exposing non-neutralizing epitopes. These results yield a more accurate antigenic picture than hitherto possible of a genuinely untriggered and functional HIV-1 Env; they can guide effective vaccine development. Nutzungsrecht: Copyright © 2015, American Association for the Advancement of Science. Antigens - chemistry Antigens - genetics HIV-1 - immunology Virion - immunology HIV Envelope Protein gp160 - chemistry HIV Antibodies - immunology HIV Envelope Protein gp41 - chemistry HIV Envelope Protein gp120 - immunology Cytoplasm - immunology HIV-1 - chemistry HIV Envelope Protein gp120 - genetics Epitopes - chemistry HIV Envelope Protein gp41 - genetics HIV Envelope Protein gp120 - chemistry Antigens, CD4 - immunology AIDS Vaccines - chemistry HIV Envelope Protein gp41 - immunology HIV Envelope Protein gp160 - immunology AIDS Vaccines - genetics AIDS Vaccines - immunology Antibodies, Neutralizing - immunology HIV Infections - prevention & control Epitopes - immunology Antigens - immunology Virion - chemistry Peng, Hanqin oth Seaman, Michael S oth Lu, Jianming oth Kovacs, James M oth Rits-Volloch, Sophia oth Zablowsky, Elise oth Park, Donghyun oth Chen, Jia oth Enthalten in Science Washington, DC : AAAS, American Assoc. for the Advancement of Science, 1883 349(2015), 6244, Seite 191 (DE-627)12931482X (DE-600)128410-1 (DE-576)014533189 0036-8075 nnns volume:349 year:2015 number:6244 pages:191 http://www.ncbi.nlm.nih.gov/pubmed/26113642 GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-LING SSG-OLC-PHY SSG-OLC-CHE SSG-OLC-MAT SSG-OLC-FOR SSG-OLC-SPO SSG-OLC-IBL SSG-OLC-PHA SSG-OLC-DE-84 SSG-OPC-FOR GBV_ILN_11 GBV_ILN_20 GBV_ILN_21 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_30 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_47 GBV_ILN_55 GBV_ILN_59 GBV_ILN_60 GBV_ILN_62 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_92 GBV_ILN_101 GBV_ILN_110 GBV_ILN_120 GBV_ILN_131 GBV_ILN_170 GBV_ILN_171 GBV_ILN_179 GBV_ILN_181 GBV_ILN_211 GBV_ILN_252 GBV_ILN_259 GBV_ILN_290 GBV_ILN_600 GBV_ILN_601 GBV_ILN_647 GBV_ILN_754 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2012 GBV_ILN_2015 GBV_ILN_2018 GBV_ILN_2020 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2116 GBV_ILN_2120 GBV_ILN_2121 GBV_ILN_2173 GBV_ILN_2185 GBV_ILN_2219 GBV_ILN_2221 GBV_ILN_2279 GBV_ILN_2286 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4036 GBV_ILN_4046 GBV_ILN_4125 GBV_ILN_4219 GBV_ILN_4251 GBV_ILN_4277 GBV_ILN_4302 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4310 GBV_ILN_4314 GBV_ILN_4317 GBV_ILN_4318 GBV_ILN_4320 GBV_ILN_4324 GBV_ILN_4328 GBV_ILN_4333 GBV_ILN_4700 AR 349 2015 6244 191 |
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PQ20160211 (DE-627)OLC1969532998 (DE-599)GBVOLC1969532998 (PRQ)pubmed_primary_261136420 (KEY)0063888920150000349624400191hiv1envelopeeffectofthecytoplasmicdomainonantigeni DE-627 ger DE-627 rakwb eng 500 DNB LING fid Chen, Bing verfasserin aut HIV-1 ENVELOPE. Effect of the cytoplasmic domain on antigenic characteristics of HIV-1 envelope glycoprotein 2015 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier A major goal for HIV-1 vaccine development is the production of an immunogen to mimic native, functional HIV-1 envelope trimeric spikes (Env) on the virion surface. We lack a reliable description of a native, functional trimer, however, because of inherent instability and heterogeneity in most preparations. We describe here two conformationally homogeneous Envs derived from difficult-to-neutralize primary isolates. All their non-neutralizing epitopes are fully concealed and independent of their proteolytic processing. Most broadly neutralizing antibodies (bnAbs) recognize these native trimers. Truncation of their cytoplasmic tail has little effect on membrane fusion, but it diminishes binding to trimer-specific bnAbs while exposing non-neutralizing epitopes. These results yield a more accurate antigenic picture than hitherto possible of a genuinely untriggered and functional HIV-1 Env; they can guide effective vaccine development. Nutzungsrecht: Copyright © 2015, American Association for the Advancement of Science. Antigens - chemistry Antigens - genetics HIV-1 - immunology Virion - immunology HIV Envelope Protein gp160 - chemistry HIV Antibodies - immunology HIV Envelope Protein gp41 - chemistry HIV Envelope Protein gp120 - immunology Cytoplasm - immunology HIV-1 - chemistry HIV Envelope Protein gp120 - genetics Epitopes - chemistry HIV Envelope Protein gp41 - genetics HIV Envelope Protein gp120 - chemistry Antigens, CD4 - immunology AIDS Vaccines - chemistry HIV Envelope Protein gp41 - immunology HIV Envelope Protein gp160 - immunology AIDS Vaccines - genetics AIDS Vaccines - immunology Antibodies, Neutralizing - immunology HIV Infections - prevention & control Epitopes - immunology Antigens - immunology Virion - chemistry Peng, Hanqin oth Seaman, Michael S oth Lu, Jianming oth Kovacs, James M oth Rits-Volloch, Sophia oth Zablowsky, Elise oth Park, Donghyun oth Chen, Jia oth Enthalten in Science Washington, DC : AAAS, American Assoc. for the Advancement of Science, 1883 349(2015), 6244, Seite 191 (DE-627)12931482X (DE-600)128410-1 (DE-576)014533189 0036-8075 nnns volume:349 year:2015 number:6244 pages:191 http://www.ncbi.nlm.nih.gov/pubmed/26113642 GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-LING SSG-OLC-PHY SSG-OLC-CHE SSG-OLC-MAT SSG-OLC-FOR SSG-OLC-SPO SSG-OLC-IBL SSG-OLC-PHA SSG-OLC-DE-84 SSG-OPC-FOR GBV_ILN_11 GBV_ILN_20 GBV_ILN_21 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_30 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_47 GBV_ILN_55 GBV_ILN_59 GBV_ILN_60 GBV_ILN_62 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_92 GBV_ILN_101 GBV_ILN_110 GBV_ILN_120 GBV_ILN_131 GBV_ILN_170 GBV_ILN_171 GBV_ILN_179 GBV_ILN_181 GBV_ILN_211 GBV_ILN_252 GBV_ILN_259 GBV_ILN_290 GBV_ILN_600 GBV_ILN_601 GBV_ILN_647 GBV_ILN_754 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2012 GBV_ILN_2015 GBV_ILN_2018 GBV_ILN_2020 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2116 GBV_ILN_2120 GBV_ILN_2121 GBV_ILN_2173 GBV_ILN_2185 GBV_ILN_2219 GBV_ILN_2221 GBV_ILN_2279 GBV_ILN_2286 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4036 GBV_ILN_4046 GBV_ILN_4125 GBV_ILN_4219 GBV_ILN_4251 GBV_ILN_4277 GBV_ILN_4302 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4310 GBV_ILN_4314 GBV_ILN_4317 GBV_ILN_4318 GBV_ILN_4320 GBV_ILN_4324 GBV_ILN_4328 GBV_ILN_4333 GBV_ILN_4700 AR 349 2015 6244 191 |
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PQ20160211 (DE-627)OLC1969532998 (DE-599)GBVOLC1969532998 (PRQ)pubmed_primary_261136420 (KEY)0063888920150000349624400191hiv1envelopeeffectofthecytoplasmicdomainonantigeni DE-627 ger DE-627 rakwb eng 500 DNB LING fid Chen, Bing verfasserin aut HIV-1 ENVELOPE. Effect of the cytoplasmic domain on antigenic characteristics of HIV-1 envelope glycoprotein 2015 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier A major goal for HIV-1 vaccine development is the production of an immunogen to mimic native, functional HIV-1 envelope trimeric spikes (Env) on the virion surface. We lack a reliable description of a native, functional trimer, however, because of inherent instability and heterogeneity in most preparations. We describe here two conformationally homogeneous Envs derived from difficult-to-neutralize primary isolates. All their non-neutralizing epitopes are fully concealed and independent of their proteolytic processing. Most broadly neutralizing antibodies (bnAbs) recognize these native trimers. Truncation of their cytoplasmic tail has little effect on membrane fusion, but it diminishes binding to trimer-specific bnAbs while exposing non-neutralizing epitopes. These results yield a more accurate antigenic picture than hitherto possible of a genuinely untriggered and functional HIV-1 Env; they can guide effective vaccine development. Nutzungsrecht: Copyright © 2015, American Association for the Advancement of Science. Antigens - chemistry Antigens - genetics HIV-1 - immunology Virion - immunology HIV Envelope Protein gp160 - chemistry HIV Antibodies - immunology HIV Envelope Protein gp41 - chemistry HIV Envelope Protein gp120 - immunology Cytoplasm - immunology HIV-1 - chemistry HIV Envelope Protein gp120 - genetics Epitopes - chemistry HIV Envelope Protein gp41 - genetics HIV Envelope Protein gp120 - chemistry Antigens, CD4 - immunology AIDS Vaccines - chemistry HIV Envelope Protein gp41 - immunology HIV Envelope Protein gp160 - immunology AIDS Vaccines - genetics AIDS Vaccines - immunology Antibodies, Neutralizing - immunology HIV Infections - prevention & control Epitopes - immunology Antigens - immunology Virion - chemistry Peng, Hanqin oth Seaman, Michael S oth Lu, Jianming oth Kovacs, James M oth Rits-Volloch, Sophia oth Zablowsky, Elise oth Park, Donghyun oth Chen, Jia oth Enthalten in Science Washington, DC : AAAS, American Assoc. for the Advancement of Science, 1883 349(2015), 6244, Seite 191 (DE-627)12931482X (DE-600)128410-1 (DE-576)014533189 0036-8075 nnns volume:349 year:2015 number:6244 pages:191 http://www.ncbi.nlm.nih.gov/pubmed/26113642 GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-LING SSG-OLC-PHY SSG-OLC-CHE SSG-OLC-MAT SSG-OLC-FOR SSG-OLC-SPO SSG-OLC-IBL SSG-OLC-PHA SSG-OLC-DE-84 SSG-OPC-FOR GBV_ILN_11 GBV_ILN_20 GBV_ILN_21 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_30 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_47 GBV_ILN_55 GBV_ILN_59 GBV_ILN_60 GBV_ILN_62 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_92 GBV_ILN_101 GBV_ILN_110 GBV_ILN_120 GBV_ILN_131 GBV_ILN_170 GBV_ILN_171 GBV_ILN_179 GBV_ILN_181 GBV_ILN_211 GBV_ILN_252 GBV_ILN_259 GBV_ILN_290 GBV_ILN_600 GBV_ILN_601 GBV_ILN_647 GBV_ILN_754 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2012 GBV_ILN_2015 GBV_ILN_2018 GBV_ILN_2020 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2116 GBV_ILN_2120 GBV_ILN_2121 GBV_ILN_2173 GBV_ILN_2185 GBV_ILN_2219 GBV_ILN_2221 GBV_ILN_2279 GBV_ILN_2286 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4036 GBV_ILN_4046 GBV_ILN_4125 GBV_ILN_4219 GBV_ILN_4251 GBV_ILN_4277 GBV_ILN_4302 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4310 GBV_ILN_4314 GBV_ILN_4317 GBV_ILN_4318 GBV_ILN_4320 GBV_ILN_4324 GBV_ILN_4328 GBV_ILN_4333 GBV_ILN_4700 AR 349 2015 6244 191 |
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PQ20160211 (DE-627)OLC1969532998 (DE-599)GBVOLC1969532998 (PRQ)pubmed_primary_261136420 (KEY)0063888920150000349624400191hiv1envelopeeffectofthecytoplasmicdomainonantigeni DE-627 ger DE-627 rakwb eng 500 DNB LING fid Chen, Bing verfasserin aut HIV-1 ENVELOPE. Effect of the cytoplasmic domain on antigenic characteristics of HIV-1 envelope glycoprotein 2015 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier A major goal for HIV-1 vaccine development is the production of an immunogen to mimic native, functional HIV-1 envelope trimeric spikes (Env) on the virion surface. We lack a reliable description of a native, functional trimer, however, because of inherent instability and heterogeneity in most preparations. We describe here two conformationally homogeneous Envs derived from difficult-to-neutralize primary isolates. All their non-neutralizing epitopes are fully concealed and independent of their proteolytic processing. Most broadly neutralizing antibodies (bnAbs) recognize these native trimers. Truncation of their cytoplasmic tail has little effect on membrane fusion, but it diminishes binding to trimer-specific bnAbs while exposing non-neutralizing epitopes. These results yield a more accurate antigenic picture than hitherto possible of a genuinely untriggered and functional HIV-1 Env; they can guide effective vaccine development. Nutzungsrecht: Copyright © 2015, American Association for the Advancement of Science. Antigens - chemistry Antigens - genetics HIV-1 - immunology Virion - immunology HIV Envelope Protein gp160 - chemistry HIV Antibodies - immunology HIV Envelope Protein gp41 - chemistry HIV Envelope Protein gp120 - immunology Cytoplasm - immunology HIV-1 - chemistry HIV Envelope Protein gp120 - genetics Epitopes - chemistry HIV Envelope Protein gp41 - genetics HIV Envelope Protein gp120 - chemistry Antigens, CD4 - immunology AIDS Vaccines - chemistry HIV Envelope Protein gp41 - immunology HIV Envelope Protein gp160 - immunology AIDS Vaccines - genetics AIDS Vaccines - immunology Antibodies, Neutralizing - immunology HIV Infections - prevention & control Epitopes - immunology Antigens - immunology Virion - chemistry Peng, Hanqin oth Seaman, Michael S oth Lu, Jianming oth Kovacs, James M oth Rits-Volloch, Sophia oth Zablowsky, Elise oth Park, Donghyun oth Chen, Jia oth Enthalten in Science Washington, DC : AAAS, American Assoc. for the Advancement of Science, 1883 349(2015), 6244, Seite 191 (DE-627)12931482X (DE-600)128410-1 (DE-576)014533189 0036-8075 nnns volume:349 year:2015 number:6244 pages:191 http://www.ncbi.nlm.nih.gov/pubmed/26113642 GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-LING SSG-OLC-PHY SSG-OLC-CHE SSG-OLC-MAT SSG-OLC-FOR SSG-OLC-SPO SSG-OLC-IBL SSG-OLC-PHA SSG-OLC-DE-84 SSG-OPC-FOR GBV_ILN_11 GBV_ILN_20 GBV_ILN_21 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_30 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_47 GBV_ILN_55 GBV_ILN_59 GBV_ILN_60 GBV_ILN_62 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_92 GBV_ILN_101 GBV_ILN_110 GBV_ILN_120 GBV_ILN_131 GBV_ILN_170 GBV_ILN_171 GBV_ILN_179 GBV_ILN_181 GBV_ILN_211 GBV_ILN_252 GBV_ILN_259 GBV_ILN_290 GBV_ILN_600 GBV_ILN_601 GBV_ILN_647 GBV_ILN_754 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2012 GBV_ILN_2015 GBV_ILN_2018 GBV_ILN_2020 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2116 GBV_ILN_2120 GBV_ILN_2121 GBV_ILN_2173 GBV_ILN_2185 GBV_ILN_2219 GBV_ILN_2221 GBV_ILN_2279 GBV_ILN_2286 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4036 GBV_ILN_4046 GBV_ILN_4125 GBV_ILN_4219 GBV_ILN_4251 GBV_ILN_4277 GBV_ILN_4302 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4310 GBV_ILN_4314 GBV_ILN_4317 GBV_ILN_4318 GBV_ILN_4320 GBV_ILN_4324 GBV_ILN_4328 GBV_ILN_4333 GBV_ILN_4700 AR 349 2015 6244 191 |
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Enthalten in Science 349(2015), 6244, Seite 191 volume:349 year:2015 number:6244 pages:191 |
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Antigens - chemistry Antigens - genetics HIV-1 - immunology Virion - immunology HIV Envelope Protein gp160 - chemistry HIV Antibodies - immunology HIV Envelope Protein gp41 - chemistry HIV Envelope Protein gp120 - immunology Cytoplasm - immunology HIV-1 - chemistry HIV Envelope Protein gp120 - genetics Epitopes - chemistry HIV Envelope Protein gp41 - genetics HIV Envelope Protein gp120 - chemistry Antigens, CD4 - immunology AIDS Vaccines - chemistry HIV Envelope Protein gp41 - immunology HIV Envelope Protein gp160 - immunology AIDS Vaccines - genetics AIDS Vaccines - immunology Antibodies, Neutralizing - immunology HIV Infections - prevention & control Epitopes - immunology Antigens - immunology Virion - chemistry |
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Chen, Bing @@aut@@ Peng, Hanqin @@oth@@ Seaman, Michael S @@oth@@ Lu, Jianming @@oth@@ Kovacs, James M @@oth@@ Rits-Volloch, Sophia @@oth@@ Zablowsky, Elise @@oth@@ Park, Donghyun @@oth@@ Chen, Jia @@oth@@ |
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2015-01-01T00:00:00Z |
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Chen, Bing ddc 500 fid LING misc Antigens - chemistry misc Antigens - genetics misc HIV-1 - immunology misc Virion - immunology misc HIV Envelope Protein gp160 - chemistry misc HIV Antibodies - immunology misc HIV Envelope Protein gp41 - chemistry misc HIV Envelope Protein gp120 - immunology misc Cytoplasm - immunology misc HIV-1 - chemistry misc HIV Envelope Protein gp120 - genetics misc Epitopes - chemistry misc HIV Envelope Protein gp41 - genetics misc HIV Envelope Protein gp120 - chemistry misc Antigens, CD4 - immunology misc AIDS Vaccines - chemistry misc HIV Envelope Protein gp41 - immunology misc HIV Envelope Protein gp160 - immunology misc AIDS Vaccines - genetics misc AIDS Vaccines - immunology misc Antibodies, Neutralizing - immunology misc HIV Infections - prevention & control misc Epitopes - immunology misc Antigens - immunology misc Virion - chemistry HIV-1 ENVELOPE. Effect of the cytoplasmic domain on antigenic characteristics of HIV-1 envelope glycoprotein |
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500 DNB LING fid HIV-1 ENVELOPE. Effect of the cytoplasmic domain on antigenic characteristics of HIV-1 envelope glycoprotein Antigens - chemistry Antigens - genetics HIV-1 - immunology Virion - immunology HIV Envelope Protein gp160 - chemistry HIV Antibodies - immunology HIV Envelope Protein gp41 - chemistry HIV Envelope Protein gp120 - immunology Cytoplasm - immunology HIV-1 - chemistry HIV Envelope Protein gp120 - genetics Epitopes - chemistry HIV Envelope Protein gp41 - genetics HIV Envelope Protein gp120 - chemistry Antigens, CD4 - immunology AIDS Vaccines - chemistry HIV Envelope Protein gp41 - immunology HIV Envelope Protein gp160 - immunology AIDS Vaccines - genetics AIDS Vaccines - immunology Antibodies, Neutralizing - immunology HIV Infections - prevention & control Epitopes - immunology Antigens - immunology Virion - chemistry |
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HIV-1 ENVELOPE. Effect of the cytoplasmic domain on antigenic characteristics of HIV-1 envelope glycoprotein |
| abstract |
A major goal for HIV-1 vaccine development is the production of an immunogen to mimic native, functional HIV-1 envelope trimeric spikes (Env) on the virion surface. We lack a reliable description of a native, functional trimer, however, because of inherent instability and heterogeneity in most preparations. We describe here two conformationally homogeneous Envs derived from difficult-to-neutralize primary isolates. All their non-neutralizing epitopes are fully concealed and independent of their proteolytic processing. Most broadly neutralizing antibodies (bnAbs) recognize these native trimers. Truncation of their cytoplasmic tail has little effect on membrane fusion, but it diminishes binding to trimer-specific bnAbs while exposing non-neutralizing epitopes. These results yield a more accurate antigenic picture than hitherto possible of a genuinely untriggered and functional HIV-1 Env; they can guide effective vaccine development. |
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A major goal for HIV-1 vaccine development is the production of an immunogen to mimic native, functional HIV-1 envelope trimeric spikes (Env) on the virion surface. We lack a reliable description of a native, functional trimer, however, because of inherent instability and heterogeneity in most preparations. We describe here two conformationally homogeneous Envs derived from difficult-to-neutralize primary isolates. All their non-neutralizing epitopes are fully concealed and independent of their proteolytic processing. Most broadly neutralizing antibodies (bnAbs) recognize these native trimers. Truncation of their cytoplasmic tail has little effect on membrane fusion, but it diminishes binding to trimer-specific bnAbs while exposing non-neutralizing epitopes. These results yield a more accurate antigenic picture than hitherto possible of a genuinely untriggered and functional HIV-1 Env; they can guide effective vaccine development. |
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A major goal for HIV-1 vaccine development is the production of an immunogen to mimic native, functional HIV-1 envelope trimeric spikes (Env) on the virion surface. We lack a reliable description of a native, functional trimer, however, because of inherent instability and heterogeneity in most preparations. We describe here two conformationally homogeneous Envs derived from difficult-to-neutralize primary isolates. All their non-neutralizing epitopes are fully concealed and independent of their proteolytic processing. Most broadly neutralizing antibodies (bnAbs) recognize these native trimers. Truncation of their cytoplasmic tail has little effect on membrane fusion, but it diminishes binding to trimer-specific bnAbs while exposing non-neutralizing epitopes. These results yield a more accurate antigenic picture than hitherto possible of a genuinely untriggered and functional HIV-1 Env; they can guide effective vaccine development. |
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We lack a reliable description of a native, functional trimer, however, because of inherent instability and heterogeneity in most preparations. We describe here two conformationally homogeneous Envs derived from difficult-to-neutralize primary isolates. All their non-neutralizing epitopes are fully concealed and independent of their proteolytic processing. Most broadly neutralizing antibodies (bnAbs) recognize these native trimers. Truncation of their cytoplasmic tail has little effect on membrane fusion, but it diminishes binding to trimer-specific bnAbs while exposing non-neutralizing epitopes. 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