title: Release of Plasmodium sporozoites requires proteins with histone-fold dimerization domains.
abstract: The sporozoite, the stage of the malaria parasite transmitted by the mosquito, first develops for ∼2 weeks in an oocyst. Rupture of the oocyst capsule is required for release of sporozoites, which then transfer to the salivary gland where they are injected into a new host. Here we identify two parasite proteins that we call oocyst rupture proteins 1 (ORP1) and ORP2. These proteins have a histone-fold domain (HFD) that promotes heterodimer formation in the oocyst capsule at the time of rupture. Oocyst rupture is prevented in mutants lacking either protein. Mutational analysis confirms the HFD as essential for ORP1 and ORP2 function, and heterodimer formation was verified in vitro. These two proteins are potential targets for blocking transmission of the parasite in the mosquito.
authors.affiliation: Foundation for Research and Technology-Hellas, Institute of Molecular Biology and Biotechnology, N. Plastira 100, GR 700 13 Heraklion, Greece.
authors.forename: Chiara
authors.initials: C
authors.lastname: Currà
authors.affiliation: Foundation for Research and Technology-Hellas, Institute of Molecular Biology and Biotechnology, N. Plastira 100, GR 700 13 Heraklion, Greece.
authors.forename: Renate
authors.initials: R
authors.lastname: Gessmann
authors.affiliation: Istituto Superiore di Sanità, Dipartimento di Malattie Infettive, Parassitarie ed Immunomediate, 0161 Roma, Italy.
authors.forename: Tomasino
authors.initials: T
authors.lastname: Pace
authors.affiliation: Istituto Superiore di Sanità, Dipartimento di Malattie Infettive, Parassitarie ed Immunomediate, 0161 Roma, Italy.
authors.forename: Leonardo
authors.initials: L
authors.lastname: Picci
authors.affiliation: Department of Experimental Medicine, University of Perugia, 06132 Perugia, Italy.
authors.forename: Giulia
authors.initials: G
authors.lastname: Peruzzi
authors.affiliation: Foundation for Research and Technology-Hellas, Institute of Molecular Biology and Biotechnology, N. Plastira 100, GR 700 13 Heraklion, Greece.
authors.forename: Vassiliki
authors.initials: V
authors.lastname: Varamogianni-Mamatsi
authors.affiliation: Foundation for Research and Technology-Hellas, Institute of Molecular Biology and Biotechnology, N. Plastira 100, GR 700 13 Heraklion, Greece.
authors.forename: Lefteris
authors.initials: L
authors.lastname: Spanos
authors.affiliation: Departamento de Fisiologia, Instituto de Biociências, Universidade de São Paulo, São Paulo 05508-900, Brazil.
authors.forename: Célia R S
authors.initials: CR
authors.lastname: Garcia
authors.affiliation: Department of Experimental Medicine, University of Perugia, 06132 Perugia, Italy.
authors.forename: Roberta
authors.initials: R
authors.lastname: Spaccapelo
authors.affiliation: Istituto Superiore di Sanità, Dipartimento di Malattie Infettive, Parassitarie ed Immunomediate, 0161 Roma, Italy.
authors.forename: Marta
authors.initials: M
authors.lastname: Ponzi
authors.affiliation: Foundation for Research and Technology-Hellas, Institute of Molecular Biology and Biotechnology, N. Plastira 100, GR 700 13 Heraklion, Greece.
authors.forename: Inga
authors.initials: I
authors.lastname: Siden-Kiamos
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D005260:Female; D008288:Malaria / Q000469:parasitology; D008297:Male; D051379:Mice; D008958:Models, Molecular; D010962:Plasmodium berghei / Q000502:physiology*; D011487:Protein Conformation; D000072417:Protein Domains; D017510:Protein Folding; D015800:Protozoan Proteins / Q000235:genetics / Q000378:metabolism*; D034101:Sporozoites / Q000502:physiology*
chemical_list: D015800:Protozoan Proteins