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Volume 11
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10.3390/biom11101437
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Article

Performance of Affinity-Improved DARPin Targeting HIV Capsid Domain in Interference of Viral Progeny Production

by
Kanokporn Sornsuwan
1,2,
Weeraya Thongkhum
2,3,
Thanathat Pamonsupornwichit
2,
Tanawan Samleerat Carraway
4,
Suthinee Soponpong
2,3,
Supachai Sakkhachornphop
5,
Chatchai Tayapiwatana
1,2,3,* and
Umpa Yasamut
1,2,3,*
1
Division of Clinical Immunology, Department of Medical Technology, Faculty of Associated Medical Sciences, Chiang Mai University, Chiang Mai 50200, Thailand
2
Center of Biomolecular Therapy and Diagnostic, Faculty of Associated Medical Sciences, Chiang Mai University, Chiang Mai 50200, Thailand
3
Center of Innovative Immunodiagnostic Development, Faculty of Associated Medical Sciences, Chiang Mai University, Chiang Mai 50200, Thailand
4
Division of Clinical Microbiology, Department of Medical Technology, Faculty of Associated Medical Sciences, Chiang Mai University, Chiang Mai 50200, Thailand
5
Research Institute for Health Sciences, Chiang Mai University, Chiang Mai 50200, Thailand
*
Authors to whom correspondence should be addressed.
Biomolecules 2021, 11(10), 1437; https://doi.org/10.3390/biom11101437
Submission received: 31 August 2021 / Revised: 17 September 2021 / Accepted: 28 September 2021 / Published: 30 September 2021
(This article belongs to the Section Molecular Medicine)
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Abstract

Previously, a designed ankyrin repeat protein, AnkGAG1D4, was generated for intracellular targeting of the HIV-1 capsid domain. The efficiency was satisfactory in interfering with the HIV assembly process. Consequently, improved AnkGAG1D4 binding affinity was introduced by substituting tyrosine (Y) for serine (S) at position 45. However, the intracellular anti-HIV-1 activity of AnkGAG1D4-S45Y has not yet been validated. In this study, the performance of AnkGAG1D4 and AnkGAG1D4-S45Y in inhibiting wild-type HIV-1 and HIV-1 maturation inhibitor-resistant replication in SupT1 cells was evaluated. HIV-1 p24 and viral load assays were used to verify the biological activity of AnkGAG1D4 and AnkGAG1D4-S45Y as assembly inhibitors. In addition, retardation of syncytium formation in infected SupT1 cells was observed. Of note, the defense mechanism of both ankyrins did not induce the mutation of target amino acids in the capsid domain. The present data show that the potency of AnkGAG1D4-S45Y was superior to AnkGAG1D4 in interrupting either HIV-1 wild-type or the HIV maturation inhibitor-resistant strain.
Keywords: ankyrin; capsid; HIV-1 assembly; anti-HIV-1 molecule; HIV-1 drug resistance ankyrin; capsid; HIV-1 assembly; anti-HIV-1 molecule; HIV-1 drug resistance

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MDPI and ACS Style

Sornsuwan, K.; Thongkhum, W.; Pamonsupornwichit, T.; Carraway, T.S.; Soponpong, S.; Sakkhachornphop, S.; Tayapiwatana, C.; Yasamut, U. Performance of Affinity-Improved DARPin Targeting HIV Capsid Domain in Interference of Viral Progeny Production. Biomolecules 2021, 11, 1437. https://doi.org/10.3390/biom11101437

AMA Style

Sornsuwan K, Thongkhum W, Pamonsupornwichit T, Carraway TS, Soponpong S, Sakkhachornphop S, Tayapiwatana C, Yasamut U. Performance of Affinity-Improved DARPin Targeting HIV Capsid Domain in Interference of Viral Progeny Production. Biomolecules. 2021; 11(10):1437. https://doi.org/10.3390/biom11101437

Chicago/Turabian Style

Sornsuwan, Kanokporn, Weeraya Thongkhum, Thanathat Pamonsupornwichit, Tanawan Samleerat Carraway, Suthinee Soponpong, Supachai Sakkhachornphop, Chatchai Tayapiwatana, and Umpa Yasamut. 2021. "Performance of Affinity-Improved DARPin Targeting HIV Capsid Domain in Interference of Viral Progeny Production" Biomolecules 11, no. 10: 1437. https://doi.org/10.3390/biom11101437

APA Style

Sornsuwan, K., Thongkhum, W., Pamonsupornwichit, T., Carraway, T. S., Soponpong, S., Sakkhachornphop, S., Tayapiwatana, C., & Yasamut, U. (2021). Performance of Affinity-Improved DARPin Targeting HIV Capsid Domain in Interference of Viral Progeny Production. Biomolecules, 11(10), 1437. https://doi.org/10.3390/biom11101437

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