ArticleMolecular and biochemical parasitology2017
LCCL protein complex formation in Plasmodium is critically dependent on LAP1.
Article in Molecular and biochemical parasitology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 16 citations in OpenAlex.
- Transcriptomics of Plasmodium vivax rosettingMemorias do Instituto Oswaldo Cruz · 2026Article
- A 3D culture model facilitates mass production of in vitro Plasmodium falciparum haemolymph-like sporozoites.Malaria journal · 2025Article
- Widespread release of translational repression across Plasmodium's host-to-vector transmission event.PLoS pathogens · 2025Article
- Article
- Global Release of Translational Repression AcrossbioRxiv : the preprint server for biology · 2024Article
- The Multiple Roles of LCCL Domain-Containing Proteins for Malaria Parasite Transmission.Microorganisms · 2024Review
- Transcriptomic approaches for identifying potential transmission blocking vaccine candidates in3 Biotech · 2023Review
- Identification of genes required for Plasmodium gametocyte-to-sporozoite development in the mosquito vector.Cell host & microbe · 2023Article
- Plasmodium berghei LAPs form an extended protein complex that facilitates crystalloid targeting and biogenesis.Journal of proteomics · 2020Article
- NAD(P) transhydrogenase has vital non-mitochondrial functions in malaria parasite transmission.EMBO reports · 2020Article
- Dysregulated gene expression in oocysts of Plasmodium berghei LAP mutants.Molecular and biochemical parasitology · 2019Article
- The Plasmodium LAP complex affects crystalloid biogenesis and oocyst cell division.International journal for parasitology · 2018Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
Successful sporogony of Plasmodium berghei in vector mosquitoes requires expression of a family of six modular proteins named LCCL lectin domain adhesive-like proteins (LAPs). The LAPs share a subcellular localization in the crystalloid, a unique parasite organelle that forms during ookinete development. Here, LAP interactions in P. berghei were studied using a series of parasite lines stably expressing reporter-tagged LAPs combined with affinity purification and high accuracy label free quantitative mass spectrometry. Our results show that abundant complexes containing LAP1, LAP2 and LAP3 are formed in gametocytes through high avidity interactions. Following fertilization, LAP4, LAP5 and LAP6 are recruited to this complex, a process that is facilitated by LAP1 chiefly through its scavenger receptor cysteine-rich modules. These collective findings provide new insight into the temporal and molecular dynamics of protein complex formation that lead up to, and are required for, crystalloid biogenesis and downstream sporozoite transmission of malaria parasites.
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