Structural insights into HIV-2 CA lattice formation and FG-pocket binding revealed by single-particle cryo-EM
Summary: One of the striking features of human immunodeficiency virus (HIV) is the capsid, a fullerene cone comprised of pleomorphic capsid protein (CA) that shields the viral genome and recruits cofactors. Despite significant advances in understanding the mechanisms of HIV-1 CA assembly and host fa...
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| Language: | English |
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Elsevier
2025-02-01
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| Series: | Cell Reports |
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| Online Access: | http://www.sciencedirect.com/science/article/pii/S2211124725000166 |
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| author | Matthew Cook Christian Freniere Chunxiang Wu Faith Lozano Yong Xiong |
| author_facet | Matthew Cook Christian Freniere Chunxiang Wu Faith Lozano Yong Xiong |
| author_sort | Matthew Cook |
| collection | DOAJ |
| description | Summary: One of the striking features of human immunodeficiency virus (HIV) is the capsid, a fullerene cone comprised of pleomorphic capsid protein (CA) that shields the viral genome and recruits cofactors. Despite significant advances in understanding the mechanisms of HIV-1 CA assembly and host factor interactions, HIV-2 CA assembly remains poorly understood. By templating the assembly of HIV-2 CA on functionalized liposomes, we report high-resolution structures of the HIV-2 CA lattice, including both CA hexamers and pentamers, alone and with peptides of host phenylalanine-glycine (FG)-motif proteins Nup153 and CPSF6. While the overall fold and mode of FG-peptide binding is conserved with HIV-1, this study reveals distinctive features of the HIV-2 CA lattice, including differing structural character at regions of host factor interactions and divergence in the mechanism of formation of CA hexamers and pentamers. This study extends our understanding of HIV capsids and highlights an approach facilitating the study of lentiviral capsid biology. |
| format | Article |
| id | doaj-art-cb35c6bd1eaa4e079bac3c9c0b7cc8f7 |
| institution | Kabale University |
| issn | 2211-1247 |
| language | English |
| publishDate | 2025-02-01 |
| publisher | Elsevier |
| record_format | Article |
| series | Cell Reports |
| spelling | doaj-art-cb35c6bd1eaa4e079bac3c9c0b7cc8f72025-01-27T04:21:53ZengElsevierCell Reports2211-12472025-02-01442115245Structural insights into HIV-2 CA lattice formation and FG-pocket binding revealed by single-particle cryo-EMMatthew Cook0Christian Freniere1Chunxiang Wu2Faith Lozano3Yong Xiong4Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT, USADepartment of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT, USADepartment of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT, USADepartment of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT, USADepartment of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT, USA; Corresponding authorSummary: One of the striking features of human immunodeficiency virus (HIV) is the capsid, a fullerene cone comprised of pleomorphic capsid protein (CA) that shields the viral genome and recruits cofactors. Despite significant advances in understanding the mechanisms of HIV-1 CA assembly and host factor interactions, HIV-2 CA assembly remains poorly understood. By templating the assembly of HIV-2 CA on functionalized liposomes, we report high-resolution structures of the HIV-2 CA lattice, including both CA hexamers and pentamers, alone and with peptides of host phenylalanine-glycine (FG)-motif proteins Nup153 and CPSF6. While the overall fold and mode of FG-peptide binding is conserved with HIV-1, this study reveals distinctive features of the HIV-2 CA lattice, including differing structural character at regions of host factor interactions and divergence in the mechanism of formation of CA hexamers and pentamers. This study extends our understanding of HIV capsids and highlights an approach facilitating the study of lentiviral capsid biology.http://www.sciencedirect.com/science/article/pii/S2211124725000166CP: Microbiology |
| spellingShingle | Matthew Cook Christian Freniere Chunxiang Wu Faith Lozano Yong Xiong Structural insights into HIV-2 CA lattice formation and FG-pocket binding revealed by single-particle cryo-EM Cell Reports CP: Microbiology |
| title | Structural insights into HIV-2 CA lattice formation and FG-pocket binding revealed by single-particle cryo-EM |
| title_full | Structural insights into HIV-2 CA lattice formation and FG-pocket binding revealed by single-particle cryo-EM |
| title_fullStr | Structural insights into HIV-2 CA lattice formation and FG-pocket binding revealed by single-particle cryo-EM |
| title_full_unstemmed | Structural insights into HIV-2 CA lattice formation and FG-pocket binding revealed by single-particle cryo-EM |
| title_short | Structural insights into HIV-2 CA lattice formation and FG-pocket binding revealed by single-particle cryo-EM |
| title_sort | structural insights into hiv 2 ca lattice formation and fg pocket binding revealed by single particle cryo em |
| topic | CP: Microbiology |
| url | http://www.sciencedirect.com/science/article/pii/S2211124725000166 |
| work_keys_str_mv | AT matthewcook structuralinsightsintohiv2calatticeformationandfgpocketbindingrevealedbysingleparticlecryoem AT christianfreniere structuralinsightsintohiv2calatticeformationandfgpocketbindingrevealedbysingleparticlecryoem AT chunxiangwu structuralinsightsintohiv2calatticeformationandfgpocketbindingrevealedbysingleparticlecryoem AT faithlozano structuralinsightsintohiv2calatticeformationandfgpocketbindingrevealedbysingleparticlecryoem AT yongxiong structuralinsightsintohiv2calatticeformationandfgpocketbindingrevealedbysingleparticlecryoem |