An Interactome-Centered Protein Discovery Approach Reveals Novel Components Involved in Mitosome Function and Homeostasis in Giardia lamblia

PLoS Pathog. 2016 Dec 7;12(12):e1006036. doi: 10.1371/journal.ppat.1006036. eCollection 2016 Dec.

Abstract

Protozoan parasites of the genus Giardia are highly prevalent globally, and infect a wide range of vertebrate hosts including humans, with proliferation and pathology restricted to the small intestine. This narrow ecological specialization entailed extensive structural and functional adaptations during host-parasite co-evolution. An example is the streamlined mitosomal proteome with iron-sulphur protein maturation as the only biochemical pathway clearly associated with this organelle. Here, we applied techniques in microscopy and protein biochemistry to investigate the mitosomal membrane proteome in association to mitosome homeostasis. Live cell imaging revealed a highly immobilized array of 30-40 physically distinct mitosome organelles in trophozoites. We provide direct evidence for the single giardial dynamin-related protein as a contributor to mitosomal morphogenesis and homeostasis. To overcome inherent limitations that have hitherto severely hampered the characterization of these unique organelles we applied a novel interaction-based proteome discovery strategy using forward and reverse protein co-immunoprecipitation. This allowed generation of organelle proteome data strictly in a protein-protein interaction context. We built an initial Tom40-centered outer membrane interactome by co-immunoprecipitation experiments, identifying small GTPases, factors with dual mitosome and endoplasmic reticulum (ER) distribution, as well as novel matrix proteins. Through iterative expansion of this protein-protein interaction network, we were able to i) significantly extend this interaction-based mitosomal proteome to include other membrane-associated proteins with possible roles in mitosome morphogenesis and connection to other subcellular compartments, and ii) identify novel matrix proteins which may shed light on mitosome-associated metabolic functions other than Fe-S cluster biogenesis. Functional analysis also revealed conceptual conservation of protein translocation despite the massive divergence and reduction of protein import machinery in Giardia mitosomes.

MeSH terms

  • Fluorescent Antibody Technique
  • Giardia lamblia / physiology*
  • Giardia lamblia / ultrastructure*
  • Homeostasis / physiology*
  • Immunoblotting
  • Immunoprecipitation
  • Mass Spectrometry
  • Microscopy, Electron, Transmission
  • Organelles
  • Organisms, Genetically Modified
  • Polymerase Chain Reaction
  • Protozoan Proteins / metabolism*
  • Trophozoites / physiology
  • Trophozoites / ultrastructure

Substances

  • Protozoan Proteins

Grants and funding

This work was partially supported by grant 31-140803/1, awarded to ABH by the Swiss National Science Fund (www.snf.ch). JPZ received grant 55080507 and CF received grant K-52201-06-01, all as fellowships from the Forschungskredit der Universität Zürich (www.researchers.uzh.ch). The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript.