ArticlePLoS neglected tropical diseases2023
Structural similarities between the metacyclic and bloodstream form variant surface glycoproteins of the African trypanosome.
Article in PLoS neglected tropical diseases, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 8 citations in OpenAlex.
- The major diagnostic VSG LiTat 1.3 of the human parasite Trypanosoma brucei gambiense is a trimer in solution.PLoS pathogens · 2026Article
- Animal Trypanosomiasis: Challenges and Prospects for New Vaccination Strategies.Microorganisms · 2024Review
- Sorting of GPI-anchored proteins at the trypanosome surface is independent of GPI insertion signals.Cell surface (Amsterdam, Netherlands) · 2024Article
- Loss to gain: pseudogenes in microorganisms, focusing on eubacteria, and their biological significance.Applied microbiology and biotechnology · 2024Review
- A structural classification of the variant surface glycoproteins of the African trypanosome.PLoS neglected tropical diseases · 2023Article
- Competition among variants is predictable and contributes to the antigenic variation dynamics of African trypanosomes.PLoS pathogens · 2023Article
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Authors and funding
12 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
During infection of mammalian hosts, African trypanosomes thwart immunity using antigenic variation of the dense Variant Surface Glycoprotein (VSG) coat, accessing a large repertoire of several thousand genes and pseudogenes, and switching to antigenically distinct copies. The parasite is transferred to mammalian hosts by the tsetse fly. In the salivary glands of the fly, the pathogen adopts the metacyclic form and expresses a limited repertoire of VSG genes specific to that developmental stage. It has remained unknown whether the metacyclic VSGs possess distinct properties associated with this particular and discrete phase of the parasite life cycle. We present here three novel metacyclic form VSG N-terminal domain crystal structures (mVSG397, mVSG531, and mVSG1954) and show that they mirror closely in architecture, oligomerization, and surface diversity the known classes of bloodstream form VSGs. These data suggest that the mVSGs are unlikely to be a specialized subclass of VSG proteins, and thus could be poor candidates as the major components of prophylactic vaccines against trypanosomiasis.
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