Viral serine palmitoyltransferase induces metabolic switch in sphingolipid biosynthesis and is required for infection of a marine alga

Carmit Ziv, Sergey Malitsky, Alaa Othman, Shifra Ben-Dor, Yu Wei, Shuning Zheng, Asaph Aharoni, Thorsten Hornemann, Assaf Vardi

Research output: Contribution to journalArticlepeer-review

Abstract

Marine viruses are the most abundant biological entities in the oceans shaping community structure and nutrient cycling. The interaction between the bloom-forming alga Emiliania huxleyi and its specific large dsDNA virus (EhV) is a major factor determining the fate of carbon in the ocean, thus serving as a key host-pathogen model system. The EhV genome encodes for a set of genes involved in the de novo sphingolipid biosynthesis, not reported in any viral genome to date. We combined detailed lipidomic and biochemical analyses to characterize the functional role of this virus-encoded pathway during lytic viral infection. We identified a major metabolic shift, mediated by differential substrate specificity of virus-encoded serine palmitoyltransferase, a key enzyme of sphingolipid biosynthesis. Consequently, unique viral glycosphingolipids, composed of unusual hydroxylated C17 sphingoid bases (t17:0) were highly enriched in the infected cells, and their synthesis was found to be essential for viral assembly. These findings uncover the biochemical bases of the virus-induced metabolic rewiring of the host sphingolipid biosynthesis during the chemical "arms race" in the ocean.

Original languageEnglish
Pages (from-to)E1907-E1916
Number of pages10
JournalProceedings of the National Academy of Sciences of the United States of America
Volume113
Issue number13
Early online date16 Mar 2016
DOIs
StatePublished - 29 Mar 2016

All Science Journal Classification (ASJC) codes

  • General

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