Complexome profiling of mitochondria in the myzozoan parasite of oysters, Perkinsus marinus
6 affiliations
- 1Institute of Immunology and Infection Research, University of Edinburgh, Edinburgh, United Kingdom
- 2Centre for Parasitology, University of Glasgow, Glasgow, United Kingdom
- 3School of Infection and Immunity, University of Glasgow, Glasgow, United Kingdom
- 4Institute of Parasitology, Biology Centre, Czech Academy of Sciences, České Budějovice, Czech Republic
- 5Faculty of Science, University of South Bohemia, České Budějovice, Czech Republic
- 6College of Medical, Veterinary & Life Sciences Shared Research Facilities, University of Glasgow, Glasgow, United Kingdom
Abstract
Mitochondrial complexes, such as the mitochondrial electron transport chain (mETC), the F1Fo-ATP synthase, the mitochondrial ribosome and the Translocase of the Outer Membrane (TOM) complex are centrally important for mitochondrial function and cell survival. Recently, an unexpected diversity in the composition of these complexes across unicellular eukaryotic lineages, with the apicomplexan parasites featuring prominently, has been revealed. However, whether the observed enlarged and divergent mitochondrial complexes are conserved across the wider lineages has not been investigated. Here, using a complexome profiling proteomic approach, we have characterised the composition of the mitochondrial complexes of the myzozoan parasite of oysters, Perkinsus marinus. We show that it shares new components of ATP synthase and the mETC complexes that in the deadly apicomplexan Plasmodium and Toxoplasma were shown to be important for growth. Moreover, the Perkinsus mitoribosome possesses many of the divergent features recently discovered in apicomplexans, including members of the ApiAP2 family that until recently were all considered to be transcription factors. Our study reveals that the divergent subunit composition of mitochondrial complexes is an ancestral and highly conserved feature of Myzozoa. Author summary: Mitochondria are a unique feature of eukaryotes and, through the synthesis of ATP, play a key role in cell energy metabolism. Mitochondrial functions rely on the coordinated function of several large protein complexes, including the mitochondrial electron transport chain (mETC), F1Fo-ATP synthase, mitochondrial ribosomes and the Translocase of the Outer Membrane (TOM). Historically, most of our knowledge on the structure and function of these critical complexes comes from studies on mammals and yeast. Research over the last decade has started to reveal that mitochondrial complexes of understudied unicellular eukaryotic lineages display considerable diversity in their composition, with many novel lineage-specific subunits being uncovered. A striking example is the apicomplexans, a lineage of parasites including those causing malaria and toxoplasmosis. However, it remained an open question whether the divergent mitochondrial complexes in apicomplexans were conserved across the broader myzozoan lineage, which in addition to parasitic species, contains free-living algae and coral symbionts. Here, using a proteomic technique called complexome profiling, we report the composition of the mitochondrial complexes from the marine parasite of oysters Perkinsus marinus. Our study highlights the broad conservation of mitochondrial complex composition across the myzozoans.
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BibTeX
@article{maclean2026complexome,
title = {{Complexome profiling of mitochondria in the myzozoan parasite of oysters, Perkinsus marinus}},
author = {Andrew E. Maclean and Orsola Iorillo and Drahomíra Faktorová and Monika Singh and Suzanne McGill and Julius Lukeš and Lilach Sheiner},
journal = {PLOS Pathogens},
year = {2026},
month = sep,
doi = {10.1371/journal.ppat.1014543},
url = {https://journals.plos.org/plospathogens/article?id=10.1371/journal.ppat.1014543},
note = {CC BY 4.0},
}
RIS
TY - JOUR
TI - Complexome profiling of mitochondria in the myzozoan parasite of oysters, Perkinsus marinus
AU - Andrew E. Maclean
AU - Orsola Iorillo
AU - Drahomíra Faktorová
AU - Monika Singh
AU - Suzanne McGill
AU - Julius Lukeš
AU - Lilach Sheiner
PY - 2026
DA - 2026/09/29
JO - PLOS Pathogens
DO - 10.1371/journal.ppat.1014543
UR - https://journals.plos.org/plospathogens/article?id=10.1371/journal.ppat.1014543
AB - Mitochondrial complexes, such as the mitochondrial electron transport chain (mETC), the F1Fo-ATP synthase, the mitochondrial ribosome and the Translocase of the Outer Membrane (TOM) complex are centrally important for mitochondrial function and cell survival. Recently, an unexpected diversity in the composition of these complexes across unicellular eukaryotic lineages, with the apicomplexan parasites featuring prominently, has been revealed. However, whether the observed enlarged and divergent mitochondrial complexes are conserved across the wider lineages has not been investigated. Here, using a complexome profiling proteomic approach, we have characterised the composition of the mitochondrial complexes of the myzozoan parasite of oysters, Perkinsus marinus. We show that it shares new components of ATP synthase and the mETC complexes that in the deadly apicomplexan Plasmodium and Toxoplasma were shown to be important for growth. Moreover, the Perkinsus mitoribosome possesses many of the divergent features recently discovered in apicomplexans, including members of the ApiAP2 family that until recently were all considered to be transcription factors. Our study reveals that the divergent subunit composition of mitochondrial complexes is an ancestral and highly conserved feature of Myzozoa. Author summary: Mitochondria are a unique feature of eukaryotes and, through the synthesis of ATP, play a key role in cell energy metabolism. Mitochondrial functions rely on the coordinated function of several large protein complexes, including the mitochondrial electron transport chain (mETC), F1Fo-ATP synthase, mitochondrial ribosomes and the Translocase of the Outer Membrane (TOM). Historically, most of our knowledge on the structure and function of these critical complexes comes from studies on mammals and yeast. Research over the last decade has started to reveal that mitochondrial complexes of understudied unicellular eukaryotic lineages display considerable diversity in their composition, with many novel lineage-specific subunits being uncovered. A striking example is the apicomplexans, a lineage of parasites including those causing malaria and toxoplasmosis. However, it remained an open question whether the divergent mitochondrial complexes in apicomplexans were conserved across the broader myzozoan lineage, which in addition to parasitic species, contains free-living algae and coral symbionts. Here, using a proteomic technique called complexome profiling, we report the composition of the mitochondrial complexes from the marine parasite of oysters Perkinsus marinus. Our study highlights the broad conservation of mitochondrial complex composition across the myzozoans.
SN - 1553-7374
ER -