Proteomic Analysis of the Plasmodium berghei Gametocyte Egressome and Vesicular bioID of Osmiophilic Body Proteins Identifies Merozoite TRAP-like Protein (MTRAP) as an Essential Factor for Parasite Transmission
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Malaria transmission from an infected host to the mosquito vector requires the uptake of intraerythrocytic sexual precursor cells into the mosquito midgut. For the release of mature extracellular gametes two membrane barriers-the parasite parasitophorous vacuole membrane and the host red blood cell membrane-need to be dissolved. Membrane lysis occurs after the release of proteins from specialized secretory vesicles including osmiophilic bodies. In this study we conducted proteomic analyses of the P. berghei gametocyte egressome and developed a vesicular bioID approach to identify hitherto unknown proteins with a potential function in gametocyte egress. This first Plasmodium gametocyte egressome includes the proteins released by the parasite during the lysis of the parasitophorous vacuole membrane and red blood cell membrane. BioID of the osmiophilic body protein MDV1/PEG3 revealed a vesicular proteome of these gametocyte-specific secretory vesicles. Fluorescent protein tagging and gene deletion approaches were employed to validate and identify a set of novel factors essential for this lysis and egress process. Our study provides the first in vivo bioID for a rodent malaria parasite and together with the first Plasmodium gametocyte egressome identifies MTRAP as a novel factor essential for mosquito transmission. Our data provide an important resource for proteins potentially involved in a key step of gametogenesis.
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BioID has been used extensively in vitro to define interacting protein partners and proteins in subcellular compartments, but its application in vivo is limited.
“BioID has been used extensively in vitro [162–166] to define interacting protein partners and proteins in subcellular compartments, but its application in vivo is limited.”
From Systems-based proteomics to resolve the biology of Alzheimer’s disease beyond amyloid and tau (2021) · cites this paper as [166]
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- Authors
- Kehrer, J., Frischknecht, F., & Mair, G. R.
- Affiliations
- Heidelberg University (DE)
- Corresponding author
- Frischknecht, Friedrich
- Mair, Gunnar R.
- Venue
- Molecular & Cellular Proteomics
- Publisher
- Elsevier BV
- Published
- 2016-09
- Volume
- 15
- Issue
- 9
- Pages
- 2852-2862
- ISSN
- 1535-9476 (ISSN-L)
- PMC
- PMC5013303
- OpenAlex
- W2512042668
- Cited by
- 105
- References
- 43
- Citations by year
- 2026: 5 · 2025: 4 · 2024: 3 · 2023: 7 · 2022: 10 · 2021: 12 · 2020: 30 · 2019: 4 · 2018: 13 · 2017: 13 · 2016: 4
- FWCI
- 11.24
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Molecular & Cellular Proteomics (publishedVersion, cc-by)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- European Research Council (ERC-SG 281719)
- Topics
- Health Sciences › Medicine › Public Health, Environmental and Occupational Health › Malaria Research and Control
- Life Sciences › Immunology and Microbiology › Parasitology › Bird parasitology and diseases
- Life Sciences › Immunology and Microbiology › Parasitology › Toxoplasma gondii Research Studies
- Keywords
- Plasmodium berghei, osmiophilic bodies, secretory vesicles, gametogenesis, rodent malaria
- MeSH terms
- Animals, Erythrocyte Membrane, Life Cycle Stages, Malaria, Plasmodium berghei, Mass Spectrometry, Protozoan Proteins, Proteomics, Mice
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