SLDP: a Novel Protein Related to Caleosin Is Associated with the Endosymbiotic Symbiodinium Lipid Droplets from Euphyllia glabrescens

Intracellular lipid droplets (LDs) have been proposed to play a key role in the mutualistic endosymbiosis between reef-building corals and the dinoflagellate endosymbiont Symbiodinium spp. This study investigates and identifies LD proteins in Symbiodinium from Euphyllia glabrescens. Discontinuous Pe...

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Veröffentlicht in:Marine biotechnology (New York, N.Y.) N.Y.), 2014-10, Vol.16 (5), p.560-571
Hauptverfasser: Pasaribu, Buntora, Lin, I-Ping, Tzen, Jason T. C., Jauh, Guang-Yuh, Fan, Tung-Yung, Ju, Yu-Min, Cheng, Jing-O, Chen, Chii-Shiarng, Jiang, Pei-Luen
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container_issue 5
container_start_page 560
container_title Marine biotechnology (New York, N.Y.)
container_volume 16
creator Pasaribu, Buntora
Lin, I-Ping
Tzen, Jason T. C.
Jauh, Guang-Yuh
Fan, Tung-Yung
Ju, Yu-Min
Cheng, Jing-O
Chen, Chii-Shiarng
Jiang, Pei-Luen
description Intracellular lipid droplets (LDs) have been proposed to play a key role in the mutualistic endosymbiosis between reef-building corals and the dinoflagellate endosymbiont Symbiodinium spp. This study investigates and identifies LD proteins in Symbiodinium from Euphyllia glabrescens. Discontinuous Percoll gradient centrifugation was used to separate Symbiodinium cells from E. glabrescens tentacles. Furthermore, staining with a fluorescent probe, Nile red, indicated that lipids accumulated in that freshly isolated Symbiodinium cells and lipid analyses further showed polyunsaturated fatty acids (PUFA) was abundant. The stable LDs were purified from endosymbiotic Symbiodinium cells. The structural integrity of the Symbiodinium LDs was maintained via electronegative repulsion and steric hindrance possibly provided by their surface proteins. Protein extracts from the purified LDs revealed a major protein band with a molecular weight of 20 kDa, which was termed Symbiodinium lipid droplet protein (SLDP). Interestingly, immunological cross-recognition analysis revealed that SLDP was detected strongly by the anti-sesame and anti-cycad caleosin antibodies. It was suggested that the stable Symbiodinium LDs were sheltered by this unique structural protein and was suggested that SLDP might be homologous to caleosin to a certain extent.
doi_str_mv 10.1007/s10126-014-9574-z
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subjects Animals
Anthozoa - microbiology
Biomedical and Life Sciences
Biotechnology
Blotting, Western
Calcium-Binding Proteins - genetics
Calcium-Binding Proteins - metabolism
Centrifugation
Coral reefs
Dinoflagellida - genetics
Dinoflagellida - metabolism
Engineering
Euphyllia
Fatty acids
Freshwater & Marine Ecology
Gas Chromatography-Mass Spectrometry
Image Processing, Computer-Assisted
Life Sciences
Lipid Droplets - metabolism
Lipids
Marine
Marine biology
Marine ecology
Metabolism
Microbiology
Microorganisms
Microscopy, Electron, Transmission
Microscopy, Fluorescence
Molecular weight
Museums
Original Article
Plant Proteins - genetics
Plant Proteins - metabolism
Polyunsaturated fatty acids
Proteins
Seeds
Signal transduction
Sterols
Studies
Symbiodinium
Symbiosis
Taiwan
Zoology
title SLDP: a Novel Protein Related to Caleosin Is Associated with the Endosymbiotic Symbiodinium Lipid Droplets from Euphyllia glabrescens
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