Broad scale proteomic analysis of heat-destabilised symbiosis in the hard coral Acropora millepora

Abstract Coral reefs across the globe are threatened by warming oceans. The last few years have seen the worst mass coral bleaching events recorded, with more than one quarter of all reefs irreversibly impacted. Considering the widespread devastation, we need to increase our efforts to understanding...

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Autores principales: K. Petrou, B. L. Nunn, M. P. Padula, D. J. Miller, D. A. Nielsen
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Publicado: Nature Portfolio 2021
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spelling oai:doaj.org-article:7985aae22b5741aa9bb5977c63ac9aca2021-12-02T18:13:45ZBroad scale proteomic analysis of heat-destabilised symbiosis in the hard coral Acropora millepora10.1038/s41598-021-98548-x2045-2322https://doaj.org/article/7985aae22b5741aa9bb5977c63ac9aca2021-09-01T00:00:00Zhttps://doi.org/10.1038/s41598-021-98548-xhttps://doaj.org/toc/2045-2322Abstract Coral reefs across the globe are threatened by warming oceans. The last few years have seen the worst mass coral bleaching events recorded, with more than one quarter of all reefs irreversibly impacted. Considering the widespread devastation, we need to increase our efforts to understanding the physiological and metabolic shifts underlying the breakdown of this important symbiotic ecosystem. Here, we investigated the proteome (PRIDE accession # PXD011668) of both host and symbionts of the reef-building coral Acropora millepora exposed to ambient (~ 28 °C) and elevated temperature (~ 32 °C for 2 days, following a five-day incremental increase) and explored associated biomolecular changes in the symbiont, with the aim of gaining new insights into the mechanisms underpinning the collapse of the coral symbiosis. We identified 1,230 unique proteins (774 host and 456 symbiont) in the control and thermally stressed corals, of which 107 significantly increased and 125 decreased in abundance under elevated temperature relative to the control. Proteins involved in oxidative stress and proteolysis constituted 29% of the host proteins that increased in abundance, with evidence of impairment to endoplasmic reticulum and cytoskeletal regulation proteins. In the symbiont, we detected a decrease in proteins responsible for photosynthesis and energy production (33% of proteins decreased in abundance), yet minimal signs of oxidative stress or proteolysis. Lipid stores increased > twofold despite reduction in photosynthesis, suggesting reduced translocation of carbon to the host. There were significant changes in proteins related to symbiotic state, including proteins linked to nitrogen metabolism in the host and the V-ATPase (-0.6 fold change) known to control symbiosome acidity. These results highlight key differences in host and symbiont proteomic adjustments under elevated temperature and identify two key proteins directly involved in bilateral nutrient exchange as potential indicators of symbiosis breakdown.K. PetrouB. L. NunnM. P. PadulaD. J. MillerD. A. NielsenNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 11, Iss 1, Pp 1-16 (2021)
institution DOAJ
collection DOAJ
language EN
topic Medicine
R
Science
Q
spellingShingle Medicine
R
Science
Q
K. Petrou
B. L. Nunn
M. P. Padula
D. J. Miller
D. A. Nielsen
Broad scale proteomic analysis of heat-destabilised symbiosis in the hard coral Acropora millepora
description Abstract Coral reefs across the globe are threatened by warming oceans. The last few years have seen the worst mass coral bleaching events recorded, with more than one quarter of all reefs irreversibly impacted. Considering the widespread devastation, we need to increase our efforts to understanding the physiological and metabolic shifts underlying the breakdown of this important symbiotic ecosystem. Here, we investigated the proteome (PRIDE accession # PXD011668) of both host and symbionts of the reef-building coral Acropora millepora exposed to ambient (~ 28 °C) and elevated temperature (~ 32 °C for 2 days, following a five-day incremental increase) and explored associated biomolecular changes in the symbiont, with the aim of gaining new insights into the mechanisms underpinning the collapse of the coral symbiosis. We identified 1,230 unique proteins (774 host and 456 symbiont) in the control and thermally stressed corals, of which 107 significantly increased and 125 decreased in abundance under elevated temperature relative to the control. Proteins involved in oxidative stress and proteolysis constituted 29% of the host proteins that increased in abundance, with evidence of impairment to endoplasmic reticulum and cytoskeletal regulation proteins. In the symbiont, we detected a decrease in proteins responsible for photosynthesis and energy production (33% of proteins decreased in abundance), yet minimal signs of oxidative stress or proteolysis. Lipid stores increased > twofold despite reduction in photosynthesis, suggesting reduced translocation of carbon to the host. There were significant changes in proteins related to symbiotic state, including proteins linked to nitrogen metabolism in the host and the V-ATPase (-0.6 fold change) known to control symbiosome acidity. These results highlight key differences in host and symbiont proteomic adjustments under elevated temperature and identify two key proteins directly involved in bilateral nutrient exchange as potential indicators of symbiosis breakdown.
format article
author K. Petrou
B. L. Nunn
M. P. Padula
D. J. Miller
D. A. Nielsen
author_facet K. Petrou
B. L. Nunn
M. P. Padula
D. J. Miller
D. A. Nielsen
author_sort K. Petrou
title Broad scale proteomic analysis of heat-destabilised symbiosis in the hard coral Acropora millepora
title_short Broad scale proteomic analysis of heat-destabilised symbiosis in the hard coral Acropora millepora
title_full Broad scale proteomic analysis of heat-destabilised symbiosis in the hard coral Acropora millepora
title_fullStr Broad scale proteomic analysis of heat-destabilised symbiosis in the hard coral Acropora millepora
title_full_unstemmed Broad scale proteomic analysis of heat-destabilised symbiosis in the hard coral Acropora millepora
title_sort broad scale proteomic analysis of heat-destabilised symbiosis in the hard coral acropora millepora
publisher Nature Portfolio
publishDate 2021
url https://doaj.org/article/7985aae22b5741aa9bb5977c63ac9aca
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AT blnunn broadscaleproteomicanalysisofheatdestabilisedsymbiosisinthehardcoralacroporamillepora
AT mppadula broadscaleproteomicanalysisofheatdestabilisedsymbiosisinthehardcoralacroporamillepora
AT djmiller broadscaleproteomicanalysisofheatdestabilisedsymbiosisinthehardcoralacroporamillepora
AT danielsen broadscaleproteomicanalysisofheatdestabilisedsymbiosisinthehardcoralacroporamillepora
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