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The HIV-1 Vpu transmembrane domain topology and formation of a hydrophobic interface with BST-2 are critical for Vpu-mediated BST-2 downregulation

View ORCID ProfileNabab Khan, Siladitya Padhi, Paresh Patel, U. Deva Priyakumar, Shahid Jameel
doi: https://doi.org/10.1101/2020.06.28.176289
Nabab Khan
1Virology Group, International Centre for Genetic Engineering and Biotechnology, New Delhi 110067, India
3Department of Biomedical Sciences, University of North Dakota School of Medicine and Health Sciences, Grand Forks, North Dakota 58203, USA
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  • For correspondence: nabab.khan@ndus.edu
Siladitya Padhi
2Centre for Computational Natural Sciences and Bioinformatics, International Institute of Information Technology, Hyderabad 500032, India
5TCS Innovation Labs-Hyderabad (Life sciences Division), Tata Consultancy Services Limited, Hyderabad 500081, India
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Paresh Patel
1Virology Group, International Centre for Genetic Engineering and Biotechnology, New Delhi 110067, India
4Discovery Innovation Accelerator, Centre for Cellular and Molecular Platforms, GKVK post, Bellary Road, Bangalore 560065, India
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U. Deva Priyakumar
2Centre for Computational Natural Sciences and Bioinformatics, International Institute of Information Technology, Hyderabad 500032, India
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Shahid Jameel
1Virology Group, International Centre for Genetic Engineering and Biotechnology, New Delhi 110067, India
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Abstract

Viruses belonging to the M group of human immunodeficiency virus (HIV-1) are the most virulent among the four HIV-1 groups. One factor that distinguishes the M group HIV-1 from others is Vpu, a membrane localized accessory protein, which promotes the release of virions by neutralizing the antiviral host cell protein BST-2. To investigate if this activity is determined by the topology of Vpu or by conserved amino acid residues, we prepared chimeric forms of Vpu by replacing its transmembrane domain with those from its topological homologs. Although the chimeric Vpu proteins downregulated BST-2, these substantially reduced virus production as well. Molecular modeling studies on Vpu from different HIV-1 groups and the chimeric Vpu proteins showed that shape and the availability of a hydrophobic interface are more important for BST-2 antagonism than conservation of the amino acid sequence. Our data suggest that the HIV-1 Vpu-M protein has evolved topologically to interact with BST-2, and that the Vpu/BST-2 interface can be exploited as a target to limit HIV-1 replication.

Competing Interest Statement

The authors have declared no competing interest.

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The copyright holder for this preprint is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made available under a CC-BY-NC-ND 4.0 International license.
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Posted June 28, 2020.
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The HIV-1 Vpu transmembrane domain topology and formation of a hydrophobic interface with BST-2 are critical for Vpu-mediated BST-2 downregulation
Nabab Khan, Siladitya Padhi, Paresh Patel, U. Deva Priyakumar, Shahid Jameel
bioRxiv 2020.06.28.176289; doi: https://doi.org/10.1101/2020.06.28.176289
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The HIV-1 Vpu transmembrane domain topology and formation of a hydrophobic interface with BST-2 are critical for Vpu-mediated BST-2 downregulation
Nabab Khan, Siladitya Padhi, Paresh Patel, U. Deva Priyakumar, Shahid Jameel
bioRxiv 2020.06.28.176289; doi: https://doi.org/10.1101/2020.06.28.176289

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