Evidence map›Paper›PMID 39966945›Full record

ArticleParasites & vectors2025

BBSome deficiency in Lotmaria passim reveals divergent functions in trypanosomatid parasites.

Xuye Yuan, Tatsuhiko Kadowaki

Abstract read
In one paragraph

Article in Parasites & vectors, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

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2citing papers in PubMed
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1 · What the graph read from it

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3 · Its place in the literature

Who cites it

2 citing papers in PubMed.

  1. Ciliary Membrane Lipid Homeostasis in Health and Disease.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
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4 · The record

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5 · Who and what money

Authors and funding

2 authors.

Xuye YuanDepartment of Biosciences and Bioinformatics, Xi'an Jiaotong-Liverpool University, 111 Ren'ai Road, Suzhou Dushu Lake Higher Education Town, Suzhou, 215123, Jiangsu Province, China.
Tatsuhiko KadowakiDepartment of Biosciences and Bioinformatics, Xi'an Jiaotong-Liverpool University, 111 Ren'ai Road, Suzhou Dushu Lake Higher Education Town, Suzhou, 215123, Jiangsu Province, China. Tatsuhiko.Kadowaki@xjtlu.edu.cn.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundThe BBSome is an octameric protein complex crucial for ciliary transport, though it also participates in multiple other cellular processes. These diverse functions may result from the co-option of its ancestral roles. Studying the BBSome in flagellated protists can provide insights into these ancestral functions and their subsequent adaptations.

methodsWe examined the functions of the BBSome (LpBBS1 and LpBBS2) in Lotmaria passim, a monoxenous trypanosomatid parasite infecting honey bees. The phenotypes resulting from depletion of LpBBS1 using the auxin-inducible degron system and disruption of LpBBS2 were characterized.

resultsParasites deficient in LpBBS2 are smaller and less motile compared with wild-type. Although intraflagellar transport of a marker membrane protein is only mildly impaired, its association with lipid rafts is significantly disrupted in the mutants. This suggests that the BBSome is essential for maintaining lipid raft integrity in L. passim. Transcriptomic comparisons between wild-type and LpBBS2-deficient parasites reveal that the BBSome may also influence processes related to metabolism, membrane localization of specific proteins, DNA repair, microtubules, and mitochondria.

conclusionsIn contrast to Leishmania mexicana, the BBSome in L. passim is crucial for efficient infection of the honey bee gut, demonstrating that its cellular functions vary between related trypanosomatid species. The BBSome is likely an adaptor that links multiple proteins in a species-specific manner under various cellular contexts.

Indexed as

Protozoan ProteinsTrypanosomatinaAnimalsBeesProtozoan ProteinsBBSomeLipid raftLotmaria passimTrypanosomatid parasite

Identifiers

PMID39966945
PMCPMC11837635

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.