title: Shared elements of host-targeting pathways among apicomplexan parasites of differing lifestyles.
abstract: Apicomplexans are a diverse group of obligate parasites occupying different intracellular niches that require modification to meet the needs of the parasite. To efficiently manipulate their environment, apicomplexans translocate numerous parasite proteins into the host cell. Whereas some parasites remain contained within a parasitophorous vacuole membrane (PVM) throughout their developmental cycle, others do not, a difference that affects the machinery needed for protein export. A signal-mediated pathway for protein export into the host cell has been characterized in Plasmodium parasites, which maintain the PVM. Here, we functionally demonstrate an analogous host-targeting pathway involving organellar staging prior to secretion in the related bovine parasite, Babesia bovis, a parasite that destroys the PVM shortly after invasion. Taking into account recent identification of a similar signal-mediated pathway in the coccidian parasite Toxoplasma gondii, we suggest a model in which this conserved pathway has evolved in multiple steps from signal-mediated trafficking to specific secretory organelles for controlled secretion to a complex protein translocation process across the PVM.
authors.affiliation: Department of Immunology and Infectious Diseases, Harvard School of Public Health, Boston, MA, USA.
authors.forename: Karell G
authors.initials: KG
authors.lastname: Pellé
authors.affiliation: Department of Immunology and Infectious Diseases, Harvard School of Public Health, Boston, MA, USA.|The Broad Institute of MIT and Harvard, Cambridge, MA, USA.
authors.forename: Rays H Y
authors.initials: RH
authors.lastname: Jiang
authors.affiliation: Department of Immunology and Infectious Diseases, Harvard School of Public Health, Boston, MA, USA.
authors.forename: Pierre-Yves
authors.initials: PY
authors.lastname: Mantel
authors.affiliation: Department of Infectious Diseases and Pathology, University of Florida, Gainesville, FL, USA.
authors.forename: Yu-Ping
authors.initials: YP
authors.lastname: Xiao
authors.affiliation: Department of Immunology and Infectious Diseases, Harvard School of Public Health, Boston, MA, USA.
authors.forename: Daisy
authors.initials: D
authors.lastname: Hjelmqvist
authors.affiliation: Department of Veterinary Microbiology and Pathology, Washington State University, Pullman, WA, USA.
authors.forename: Gina M
authors.initials: GM
authors.lastname: Gallego-Lopez
authors.affiliation: Department of Veterinary Microbiology and Pathology, Washington State University, Pullman, WA, USA.
authors.forename: Audrey
authors.initials: A
authors.lastname: O T Lau
authors.affiliation: Department of Microbiology and Cell Science, University of Florida, Gainesville, FL, USA.
authors.forename: Byung-Ho
authors.initials: BH
authors.lastname: Kang
authors.affiliation: Department of Infectious Diseases and Pathology, University of Florida, Gainesville, FL, USA.|Genetics Institute, University of Florida, Gainesville, FL, USA.
authors.forename: David R
authors.initials: DR
authors.lastname: Allred
authors.affiliation: Department of Immunology and Infectious Diseases, Harvard School of Public Health, Boston, MA, USA.
authors.forename: Matthias
authors.initials: M
authors.lastname: Marti
mesh_terms: D016793:Babesia bovis / Q000502:physiology*; D054884:Host-Pathogen Interactions; D010961:Plasmodium / Q000502:physiology; D021381:Protein Transport; D015800:Protozoan Proteins / Q000378:metabolism*; D017422:Sequence Analysis, DNA; D014122:Toxoplasma / Q000502:physiology; D014617:Vacuoles / Q000469:parasitology*; D037521:Virulence Factors / Q000378:metabolism*
chemical_list: D015800:Protozoan Proteins; D037521:Virulence Factors