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Viruses
Volume 14
Issue 4
10.3390/v14040824
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Article

Specific Interaction of DARPin with HIV-1 CANTD Disturbs the Distribution of Gag, RNA Packaging, and Tetraspanin Remodelling in the Membrane

by
Sutpirat Moonmuang
1,2,
Rawiwan Maniratanachote
3,
Paninee Chetprayoon
3,
Kanokporn Sornsuwan
1,
Weeraya Thongkum
1,4,
Koollawat Chupradit
1,5 and
Chatchai Tayapiwatana
1,2,4,*
1
Center of Biomolecular Therapy and Diagnostic, Faculty of Associated Medical Sciences, Chiang Mai University, Chiang Mai 50200, Thailand
2
Department of Medical Technology, Division of Clinical Immunology, Faculty of Associated Medical Sciences, Chiang Mai University, Chiang Mai 50200, Thailand
3
Toxicology and Bio Evaluation Service Center (TBES), National Science and Technology Development Agency (NSTDA), Pathum Thani 12120, Thailand
4
Center of Innovative Immunodiagnostic Development, Faculty of Associated Medical Sciences, Chiang Mai University, Chiang Mai 50200, Thailand
5
Siriraj Center for Regenerative Medicine, Faculty of Medicine Siriraj Hospital, Mahidol University, Bangkok 10700, Thailand
*
Author to whom correspondence should be addressed.
Viruses 2022, 14(4), 824; https://doi.org/10.3390/v14040824
Submission received: 6 March 2022 / Revised: 12 April 2022 / Accepted: 13 April 2022 / Published: 15 April 2022
(This article belongs to the Special Issue Antiviral Molecular Mechanisms)
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Abstract

A designed repeat scaffold protein (AnkGAG1D4) recognizing the human immunodeficiency virus-1 (HIV-1) capsid (CA) was formerly established with antiviral assembly. Here, we investigated the molecular mechanism of AnkGAG1D4 function during the late stages of the HIV-1 replication cycle. By applying stimulated emission-depletion (STED) microscopy, Gag polymerisation was interrupted at the plasma membrane. Disturbance of Gag polymerisation triggered Gag accumulation inside producer cells and trapping of the CD81 tetraspanin on the plasma membrane. Moreover, reverse transcriptase-quantitative polymerase chain reaction (RT-qPCR) experiments were performed to validate the packaging efficiency of RNAs. Our results advocated that AnkGAG1D4 interfered with the Gag precursor protein from selecting HIV-1 and cellular RNAs for encapsidation into viral particles. These findings convey additional information on the antiviral activity of AnkGAG1D4 at late stages of the HIV-1 life cycle, which is potential for an alternative anti-HIV molecule.
Keywords: HIV-1; Gag polyprotein; virus assembly inhibitor; ankyrin; tetraspanin HIV-1; Gag polyprotein; virus assembly inhibitor; ankyrin; tetraspanin

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MDPI and ACS Style

Moonmuang, S.; Maniratanachote, R.; Chetprayoon, P.; Sornsuwan, K.; Thongkum, W.; Chupradit, K.; Tayapiwatana, C. Specific Interaction of DARPin with HIV-1 CANTD Disturbs the Distribution of Gag, RNA Packaging, and Tetraspanin Remodelling in the Membrane. Viruses 2022, 14, 824. https://doi.org/10.3390/v14040824

AMA Style

Moonmuang S, Maniratanachote R, Chetprayoon P, Sornsuwan K, Thongkum W, Chupradit K, Tayapiwatana C. Specific Interaction of DARPin with HIV-1 CANTD Disturbs the Distribution of Gag, RNA Packaging, and Tetraspanin Remodelling in the Membrane. Viruses. 2022; 14(4):824. https://doi.org/10.3390/v14040824

Chicago/Turabian Style

Moonmuang, Sutpirat, Rawiwan Maniratanachote, Paninee Chetprayoon, Kanokporn Sornsuwan, Weeraya Thongkum, Koollawat Chupradit, and Chatchai Tayapiwatana. 2022. "Specific Interaction of DARPin with HIV-1 CANTD Disturbs the Distribution of Gag, RNA Packaging, and Tetraspanin Remodelling in the Membrane" Viruses 14, no. 4: 824. https://doi.org/10.3390/v14040824

APA Style

Moonmuang, S., Maniratanachote, R., Chetprayoon, P., Sornsuwan, K., Thongkum, W., Chupradit, K., & Tayapiwatana, C. (2022). Specific Interaction of DARPin with HIV-1 CANTD Disturbs the Distribution of Gag, RNA Packaging, and Tetraspanin Remodelling in the Membrane. Viruses, 14(4), 824. https://doi.org/10.3390/v14040824

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