The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
Structures of Native Doublet Microtubules from Trichomonas vaginalis Reveal Parasite-Specific Proteins as Potential Drug Targets
Open accessPreprint — published as 10.1038/s41467-025-59369-y · Paper page
Abstract
Doublet microtubules (DMTs) are flagellar components required for the protist Trichomonas vaginalis (Tv) to swim through the human genitourinary tract to cause trichomoniasis, the most common non-viral sexually transmitted disease. Lack of DMT structures has prevented structure-guided drug design to manage Tv infection. Here, we determined the cryo-EM structure of native Tv-DMTs, identifying 29 unique proteins, including 18 microtubule inner proteins and 9 microtubule outer proteins. While the A-tubule is simplistic compared to DMTs of other organisms, the B-tubule features specialized, parasite-specific proteins, such as TvFAP40 and TvFAP35 that form filaments near the inner and outer junctions, respectively, to stabilize DMTs and enable Tv locomotion. Notably, a small molecule, assigned as IP6, is coordinated within a pocket of TvFAP40 and has characteristics of a drug molecule. This first atomic model of the Tv-DMT highlights the diversity of eukaryotic motility machinery and provides a structural framework to inform rational design of therapeutics.
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Cites
Highly accurate protein structure prediction with AlphaFold
Jumper, J., Evans, R., Pritzel, A., Green, T., Figurnov, M., Ronneberger, O., Tunyasuvunakool, K., Bates, R., Žídek, A., Potapenko, A., et al. (2021) · Nature · doi:10.1038/s41586-021-03819-2 · Cited by 43,764
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Metadata
- Authors
- Zhou, Z. H., Stevens, A., Kashyap, S., Crofut, E., Wang, S., Muratore, K., & Johnson, P.
- Affiliations
- California NanoSystems Institute (US)
- University of California, Los Angeles (US)
- Corresponding author
- Zhou, Z. Hong
- Johnson, Patricia
- Venue
- Nature Communications
- Published
- 2024-09-02
- Volume
- 16
- Issue
- 1
- Pages
- 3996-3996
- ISSN
- 2041-1723 (ISSN-L)
- PMC
- PMC12041511
- OpenAlex
- W4409947646
- Cited by
- 4
- References
- 1
- Citations by year
- 2026: 3 · 2025: 1
- FWCI
- 1.99
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Locations
- Nature Communications (publishedVersion, cc-by)
- Research Square (acceptedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- PubMed Central (submittedVersion, cc-by)
- RePEc: Research Papers in Economics (submittedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Funders
- National Science Foundation (1338135, 1S10RR23057, 1548924)
- U.S. Department of Health and Human Services (1S10OD018111, 1S10RR23057)
- James B. Pendleton Charitable Trust
- National Institutes of Health (1s10od018111-01, AI007323)
- National Institute of General Medical Sciences (R01GM071940)
- National Institute of Allergy and Infectious Diseases (R33AI119721, R01AI103182, T32AI007323)
- Division of Materials Research (DMR1548924, 1548924)
- National Center for Research Resources (S10RR023057)
- UCLA AIDS Institute
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Microtubule and mitosis dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Advanced Electron Microscopy Techniques and Applications
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Enzyme Structure and Function
- Keywords
- Trichomonas vaginalis, doublet microtubules, flagella, trichomoniasis, microtubule inner proteins, tubulin, atomic models, structure-based drug design
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