title: Genomic insights into processes driving the infection of Alexandrium tamarense by the Parasitoid Amoebophrya sp.
abstract: The regulatory circuits during infection of dinoflagellates by their parasites are largely unknown on the molecular level. Here we provide molecular insights into these infection dynamics. Alexandrium tamarense is one of the most prominent harmful algal bloom dinoflagellates. Its pathogen, the dinoflagellate parasitoid Amoebophrya sp., has been observed to infect and control the blooms of this species. We generated a data set of transcripts from three time points (0, 6, and 96 h) during the infection of this parasite-host system. Assembly of all transcript data from the parasitoid (>900,000 reads/313 Mbp with 454/Roche next-generation sequencing [NGS]) yielded 14,455 contigs, to which we mapped the raw transcript reads of each time point of the infection cycle. We show that particular surface lectins are expressed at the beginning of the infection cycle which likely mediate the attachment to the host cell. In a later phase, signal transduction-related genes together with transmembrane transport and cytoskeleton proteins point to a high integration of processes involved in host recognition, adhesion, and invasion. At the final maturation stage, cell division- and proliferation-related genes were highly expressed, reflecting the fast cell growth and nuclear division of the parasitoid. Our molecular insights into dinoflagellate parasitoid interactions point to general mechanisms also known from other eukaryotic parasites, especially from the Alveolata. These similarities indicate the presence of fundamental processes of parasitoid infection that have remained stable throughout evolution within different phyla.
authors.affiliation: Department of Ecological Chemistry, Alfred-Wegener-Institut Helmholtz-Zentrum für Polar- und Meeresforschung, Bremerhaven, Germany Lu.Yameng@awi.de.
authors.forename: Yameng
authors.initials: Y
authors.lastname: Lu
authors.affiliation: Department of Ecological Chemistry, Alfred-Wegener-Institut Helmholtz-Zentrum für Polar- und Meeresforschung, Bremerhaven, Germany.
authors.forename: Sylke
authors.initials: S
authors.lastname: Wohlrab
authors.affiliation: Biochemistry I, Medical Faculty, University of Cologne, Cologne, Germany Leibniz Institute of Freshwater Ecology and Inland Fisheries, IGB, Berlin, Germany.
authors.forename: Gernot
authors.initials: G
authors.lastname: Glöckner
authors.affiliation: Station Biologique de Roscoff, Roscoff, France.
authors.forename: Laure
authors.initials: L
authors.lastname: Guillou
authors.affiliation: Department of Ecological Chemistry, Alfred-Wegener-Institut Helmholtz-Zentrum für Polar- und Meeresforschung, Bremerhaven, Germany.
authors.forename: Uwe
authors.initials: U
authors.lastname: John
mesh_terms: D001483:Base Sequence; D002448:Cell Adhesion / Q000235:genetics; D002455:Cell Division / Q000235:genetics; D049109:Cell Proliferation / Q000235:genetics; D003598:Cytoskeletal Proteins / Q000235:genetics*; D004141:Dinoflagellida / Q000235:genetics / Q000469:parasitology* / Q000472:pathogenicity*; D005786:Gene Expression Regulation / Q000235:genetics; D057097:Harmful Algal Bloom; D037102:Lectins / Q000096:biosynthesis / Q000235:genetics; D026901:Membrane Transport Proteins / Q000235:genetics*; D017423:Sequence Analysis, RNA; D015398:Signal Transduction / Q000235:genetics; D033761:Spores, Protozoan / Q000235:genetics
chemical_list: D003598:Cytoskeletal Proteins; D037102:Lectins; D026901:Membrane Transport Proteins