The human allicin-proteome: global protein S-thioallylation of by the garlic defence substance allicin and its biological effects

ABSTRACT: A single clove of edible garlic (Allium sativum L.) produces up to 5 mg of allicin (diallylthiosulfinate), a thiol-reactive sulfur-containing defence substance that gives injured garlic tissue its characteristic smell. Allicin induces apoptosis or necrosis in a dose-dependent manner but sublethal doses influence cellular metabolism and signalling cascades. Oxidation of protein thiols and depletion of the glutathione pool are thought to be responsible for allicin’s physiological effects. Here, we studied the effect of Allicin on post-translational thiol-modification in human Jurkat cells using shotgun LC-MS/MS analyses. We identified 332 proteins in the human Jurkat cell proteome that were modified by S-thioallylation which causes a mass shift of 72 Dalton on cysteines. Many S-thioallylated proteins are high abundant proteins, including the cytoskeletal proteins tubulin, actin, cofilin, filamin and plastin-2, the heat shock chaperones HSP90 and HSPA4, the glycolytic enzymes GAPDH, ALDOA, PKM as well the protein translation factor EEF2. We confirmed that Allicin disrupted the actin cytoskeleton in mouseL929 fibroblasts. Allicin further resulted in Zn2+ release from proteins and stimulated the Zn2+-dependent IL1-triggered release of IL2 in murine EL4 T-cells. Allicin further caused inhibition of enolase activity. In conclusion, our study revealed the overall extent of widespread S-thioallylation in the human Jurkat cell proteome after allicin exposure which affects essential cellular functions of selected allicin targets.

INSTRUMENT(S): LTQ Orbitrap Velos

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Jurkat Cell

SUBMITTER: Van Loi Vu  

LAB HEAD: Prof. Dr. Haike Antelmann

PROVIDER: PXD010201 | Pride | 2018-11-30

REPOSITORIES: Pride