title: Bacterial lipids activate, synergize, and inhibit a developmental switch in choanoflagellates.
abstract: In choanoflagellates, the closest living relatives of animals, multicellular rosette development is regulated by environmental bacteria. The simplicity of this evolutionarily relevant interaction provides an opportunity to identify the molecules and regulatory logic underpinning bacterial regulation of development. We find that the rosette-inducing bacterium Algoriphagus machipongonensis produces three structurally divergent classes of bioactive lipids that, together, activate, enhance, and inhibit rosette development in the choanoflagellate Salpingoeca rosetta. One class of molecules, the lysophosphatidylethanolamines (LPEs), elicits no response on its own but synergizes with activating sulfonolipid rosette-inducing factors (RIFs) to recapitulate the full bioactivity of live Algoriphagus. LPEs, although ubiquitous in bacteria and eukaryotes, have not previously been implicated in the regulation of a host-microbe interaction. This study reveals that multiple bacterially produced lipids converge to activate, enhance, and inhibit multicellular development in a choanoflagellate.
authors.affiliation: Howard Hughes Medical Institute, University of California, Berkeley, CA 94720; Department of Molecular and Cell Biology, University of California, Berkeley, CA 94720;
authors.forename: Arielle
authors.initials: A
authors.lastname: Woznica
authors.affiliation: Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA 02115;
authors.forename: Alexandra M
authors.initials: AM
authors.lastname: Cantley
authors.affiliation: Leibniz Institute for Natural Product Research and Infection Biology, Hans-Knöll Institute, 07745 Jena, Germany;
authors.forename: Christine
authors.initials: C
authors.lastname: Beemelmanns
authors.affiliation: Whitehead Institute for Biomedical Research, Cambridge, MA 02142.
authors.forename: Elizaveta
authors.initials: E
authors.lastname: Freinkman
authors.affiliation: Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA 02115; nking@berkeley.edu jon_clardy@hms.harvard.edu.
authors.forename: Jon
authors.initials: J
authors.lastname: Clardy
authors.affiliation: Howard Hughes Medical Institute, University of California, Berkeley, CA 94720; Department of Molecular and Cell Biology, University of California, Berkeley, CA 94720; nking@berkeley.edu jon_clardy@hms.harvard.edu.
authors.forename: Nicole
authors.initials: N
authors.lastname: King
mesh_terms: D001426:Bacterial Proteins / Q000302:isolation & purification / Q000502:physiology*; D041963:Bacteroidetes / Q000502:physiology*; D056897:Choanoflagellata / Q000502:physiology*; D008055:Lipids / Q000502:physiology
chemical_list: D001426:Bacterial Proteins; D008055:Lipids; C015518:sulfolipids
keywords: bacteria; choanoflagellates; host–microbe; multicellularity; sulfonolipid