Proteomics

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The influence of symbiosis on the proteome of the symbiotic dinoflagellate Breviolum


ABSTRACT: The physiology and cellular mechanisms of the dinoflagellate symbionts of cnidarians, the Symbiodiniaceae, change as a response to symbiosis, nutrient availability, and their surrounding microhabitat, but the underlying processes are poorly understood. Here, we employed liquid chromatography–mass spectrometry-based proteomics to elucidate the changes associated with the symbiotic and nutritional states of Breviolum minutum, a native symbiont of the sea anemone Exaiptasia diaphana. Both symbiosis and nutritional state had significant impacts on the B. minutum proteome. B. minutum in hospite showed increased abundance of proteins that are involved in phosphoinositol manipulation (e.g., glycerophosphoinositol permease 1 and phosphatidylinositol phosphatase), potentially as a means of interpartner signalling to prevent host phagosomal maturation. Proteins involved in carbon concentration and fixation (e.g. carbonic anhydrase, V-type ATPase) and nitrogen assimilation (e.g. glutamine synthase) were upregulated in ex hospite B. minutum, possibly due to nitrogen limitation by host in hospite and a lack of host carbon concentration mechanisms when ex hospite, respectively. Photosystem proteins increased in abundance at high nutrient levels, as were proteins involved in antioxidant mechanisms (e.g. superoxide dismutase, glutathione s-transferase). Proteins involved in iron metabolism was also affected by nutrient state, indicating increased iron demand and uptake in low nutrient treatments. These results provide better insight on the cellular mechanisms of symbiosis and provides potential target pathways for investigating a functional cnidarian-dinoflagellate symbiosis.

INSTRUMENT(S): Orbitrap Fusion Lumos

ORGANISM(S): Breviolum Minutum

SUBMITTER: Clinton Oakley  

LAB HEAD: Simon Davy

PROVIDER: PXD036981 | Pride | 2023-01-31

REPOSITORIES: Pride

Dataset's files

Source:
Action DRS
ASW2_200ng_ITHCDt20_90-70v4.raw Raw
Amir-min_assembly_longest_250_transdecoder.fasta Fasta
Amir_71.raw Raw
Amir_74.raw Raw
Amir_76.raw Raw
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