Insights from aquaporin structures into drug-resistant sleeping sickness Article Swipe
Modestas Matusevicius
,
Robin A. Corey
,
Marcos Gragera
,
Keitaro Yamashita
,
Teresa Sprenger
,
Marzuq A. Ungogo
,
James N. Blaza
,
Pablo Castro‐Hartmann
,
Dimitri Y. Chirgadze
,
Sundeep Chaitanya Vedithi
,
Pavel Afanasyev
,
Roberto Melero
,
Rangana Warshamanage
,
Anastasiia Gusach
,
James Krieger
,
Mark Carrington
,
Tom L. Blundell
,
Garib N. Murshudov
,
Phillip J. Stansfeld
,
Mark S.P. Sansom
,
Harry P. de Koning
,
Christopher G. Tate
,
Simone Weyand
·
YOU?
·
· 2025
· Open Access
·
· DOI: https://doi.org/10.7554/elife.107460
YOU?
·
· 2025
· Open Access
·
· DOI: https://doi.org/10.7554/elife.107460
Trypanosoma brucei is the causal agent of African trypanosomiasis in humans and animals, the latter resulting in significant negative economic impacts in afflicted areas of the world. Resistance has arisen to the trypanocidal drugs pentamidine and melarsoprol through mutations in the aquaglyceroporin TbAQP2 that prevent their uptake. Here we use cryogenic electron microscopy to determine the structure of TbAQP2 from Trypanosoma brucei, bound to either the substrate glycerol or to the sleeping sickness drugs, pentamidine or melarsoprol. The drugs bind within the AQP2 channel at a site completely overlapping that of glycerol. Mutations leading to a drug-resistant phenotype were found in the channel lining. Molecular dynamics simulations showed the channel can be traversed by pentamidine, with a low energy binding site at the centre of the channel, flanked by regions of high energy association at the extracellular and intracellular ends. Drug-resistant TbAQP2 mutants are still predicted to bind pentamidine, but the much weaker binding in the centre of the channel observed in the MD simulations would be insufficient to compensate for the high energy processes of ingress and egress, hence impairing transport at pharmacologically relevant concentrations. The structures of drug-bound TbAQP2 represent a novel paradigm for drug-transporter interactions that could provide new mechanisms for targeting drugs into pathogens and human cells.
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- Type
- preprint
- Language
- en
- Landing Page
- https://doi.org/10.7554/elife.107460
- OA Status
- gold
- References
- 88
- Related Works
- 10
- OpenAlex ID
- https://openalex.org/W4411933361
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Raw OpenAlex JSON
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https://doi.org/10.7554/elife.107460Digital Object Identifier
- Title
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Insights from aquaporin structures into drug-resistant sleeping sicknessWork title
- Type
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preprintOpenAlex work type
- Language
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enPrimary language
- Publication year
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2025Year of publication
- Publication date
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2025-07-02Full publication date if available
- Authors
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Modestas Matusevicius, Robin A. Corey, Marcos Gragera, Keitaro Yamashita, Teresa Sprenger, Marzuq A. Ungogo, James N. Blaza, Pablo Castro‐Hartmann, Dimitri Y. Chirgadze, Sundeep Chaitanya Vedithi, Pavel Afanasyev, Roberto Melero, Rangana Warshamanage, Anastasiia Gusach, James Krieger, Mark Carrington, Tom L. Blundell, Garib N. Murshudov, Phillip J. Stansfeld, Mark S.P. Sansom, Harry P. de Koning, Christopher G. Tate, Simone WeyandList of authors in order
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https://doi.org/10.7554/elife.107460Publisher landing page
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YesWhether a free full text is available
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goldOpen access status per OpenAlex
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https://doi.org/10.7554/elife.107460Direct OA link when available
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Drug, Business, Medicine, PharmacologyTop concepts (fields/topics) attached by OpenAlex
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0Total citation count in OpenAlex
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88Number of works referenced by this work
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10Other works algorithmically related by OpenAlex
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