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Background    Lobosphaera incisa  ( L. incisa ) is an oleaginous microalga that stores triacylglycerol (TAG) rich in arachidonic acid in lipid bodies (LBs). This organelle is gaining attention in algal research, since evidence is accumulating that proteins attached to its surface fulfill important functions in TAG storage and metabolism.    Results  Here, the composition of the LB proteome in  L incisa  was investigated by comparing different cell fractions in a semiquantitative proteomics approach. After applying stringent filters to the proteomics data in order to remove contaminating proteins from the list of possible LB proteins (LBPs), heterologous expression of candidate proteins in tobacco pollen tubes, allowed us to confirm 3 true LBPs: A member of the algal Major Lipid Droplet Protein family, a small protein of unknown function and a putative lipase. In addition, a TAG lipase that belongs to the SUGAR DEPENDENT 1 family of TAG lipases known from oilseed plants was identified. Its activity was verified by functional complementation of an  Arabidopsis thaliana  mutant lacking the major seed TAG lipases.    Conclusions  Here we describe 3 LBPs as well as a TAG lipase from the oleaginous microalga  L. incisa  and discuss their possible involvement in LB metabolism. This study highlights the importance of filtering LB proteome datasets and verifying the subcellular localization one by one, so that contaminating proteins can be recognized as such. Our dataset can serve as a valuable resource in the identification of additional LBPs, shedding more light on the intriguing roles of LBs in microalgae.    Electronic supplementary material  The online version of this article (doi:10.1186/s12870-017-1042-2) contains supplementary material, which is available to authorized users.

Analysis of the lipid body proteome of the oleaginous alga Lobosphaera incisa