Snapshot of Peptidomics of the Red Tide Forming Species Noctiluca scintillans
The objective of this study was to investigate the peptidome of a red tide forming species Noctiluca scintillans based on mass-spectrometry (MS) analysis. N. scintillans cells were collected at the initiation and peak phases of its bloom. Peptides were extracted by ultrafiltration with cutoff of 10...
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doaj-76e2ae996aa8457cb90140d0938c89922020-11-25T03:44:12ZengFrontiers Media S.A.Frontiers in Marine Science2296-77452020-10-01710.3389/fmars.2020.569807569807Snapshot of Peptidomics of the Red Tide Forming Species Noctiluca scintillansShuwen Zhang0Cheng Li1Shunyan Cheung2Mingming Sun3Shuqun Song4Wang Guo5Cui Guo6Cui Guo7Gongguo Wu8Hongbin Liu9Hongbin Liu10Guangdong Provincial Key Laboratory of Healthy and Safe Aquaculture, College of Life Science, South China Normal University, Guangzhou, ChinaDivision of Life Science, The Hong Kong University of Science and Technology, Kowloon, Hong KongDepartment of Ocean Science, The Hong Kong University of Science and Technology, Kowloon, Hong KongDivision of Life Science, The Hong Kong University of Science and Technology, Kowloon, Hong KongKey Laboratory of Marine Ecology & Environmental Sciences, Institute of Oceanology Chinese Academy of Sciences, Qingdao, ChinaDivision of Life Science, The Hong Kong University of Science and Technology, Kowloon, Hong KongCollege of Marine Life Sciences, Ocean University of China, Qingdao, ChinaInstitute of Evolution and Marine Biodiversity, Ocean University of China, Qingdao, ChinaDivision of Life Science, The Hong Kong University of Science and Technology, Kowloon, Hong KongDepartment of Ocean Science, The Hong Kong University of Science and Technology, Kowloon, Hong KongHong Kong Branch of Southern Marine Science & Engineering Guangdong Laboratory, The Hong Kong University of Science and Technology, Kowloon, Hong KongThe objective of this study was to investigate the peptidome of a red tide forming species Noctiluca scintillans based on mass-spectrometry (MS) analysis. N. scintillans cells were collected at the initiation and peak phases of its bloom. Peptides were extracted by ultrafiltration with cutoff of 10 and 3 kDa in acidic condition. Optimal mass spectra were generated after purification with C18 column. MS analysis and peptide identification was undertaken by Linear Trap Quadropole (LTQ) Velos MS/MS instrument. Using this method, 239 and 332 peptide sequences from the samples collected at the initiation and peak phases of N. scintillans bloom were identified, respectively. These sequences were classified and they were affiliated to 68 and 93 groups of precursor proteins, respectively, at the initiation and peak phases, with a compositional dissimilarity of 49.5%. Meanwhile, majority of the peptides were conjectured to come from contents digested by N. scintillans. Thirty-three groups of precursor proteins were detected at both phases. These peptides involved in various intracellular physiological activities, most of them responsible for functions of digestion activities such as oxidoreductase activity, catalytic activity, hydrolase activity and cofactor/ion binding. The compositions of precursor proteins, molecular weights, functions and cell compartments of the obtained peptides were quite different between two bloom stages. This is the first attempt to study peptidomics of N. scintillans, which provide important information on the functional studies of peptidomics in N. scintillans, especially food digestion and dietary protein utilization, as well as their relationship with bloom development.https://www.frontiersin.org/articles/10.3389/fmars.2020.569807/fullNoctiluca scintillanspeptidomicsmass spectrometryproteinfood digestion |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Shuwen Zhang Cheng Li Shunyan Cheung Mingming Sun Shuqun Song Wang Guo Cui Guo Cui Guo Gongguo Wu Hongbin Liu Hongbin Liu |
spellingShingle |
Shuwen Zhang Cheng Li Shunyan Cheung Mingming Sun Shuqun Song Wang Guo Cui Guo Cui Guo Gongguo Wu Hongbin Liu Hongbin Liu Snapshot of Peptidomics of the Red Tide Forming Species Noctiluca scintillans Frontiers in Marine Science Noctiluca scintillans peptidomics mass spectrometry protein food digestion |
author_facet |
Shuwen Zhang Cheng Li Shunyan Cheung Mingming Sun Shuqun Song Wang Guo Cui Guo Cui Guo Gongguo Wu Hongbin Liu Hongbin Liu |
author_sort |
Shuwen Zhang |
title |
Snapshot of Peptidomics of the Red Tide Forming Species Noctiluca scintillans |
title_short |
Snapshot of Peptidomics of the Red Tide Forming Species Noctiluca scintillans |
title_full |
Snapshot of Peptidomics of the Red Tide Forming Species Noctiluca scintillans |
title_fullStr |
Snapshot of Peptidomics of the Red Tide Forming Species Noctiluca scintillans |
title_full_unstemmed |
Snapshot of Peptidomics of the Red Tide Forming Species Noctiluca scintillans |
title_sort |
snapshot of peptidomics of the red tide forming species noctiluca scintillans |
publisher |
Frontiers Media S.A. |
series |
Frontiers in Marine Science |
issn |
2296-7745 |
publishDate |
2020-10-01 |
description |
The objective of this study was to investigate the peptidome of a red tide forming species Noctiluca scintillans based on mass-spectrometry (MS) analysis. N. scintillans cells were collected at the initiation and peak phases of its bloom. Peptides were extracted by ultrafiltration with cutoff of 10 and 3 kDa in acidic condition. Optimal mass spectra were generated after purification with C18 column. MS analysis and peptide identification was undertaken by Linear Trap Quadropole (LTQ) Velos MS/MS instrument. Using this method, 239 and 332 peptide sequences from the samples collected at the initiation and peak phases of N. scintillans bloom were identified, respectively. These sequences were classified and they were affiliated to 68 and 93 groups of precursor proteins, respectively, at the initiation and peak phases, with a compositional dissimilarity of 49.5%. Meanwhile, majority of the peptides were conjectured to come from contents digested by N. scintillans. Thirty-three groups of precursor proteins were detected at both phases. These peptides involved in various intracellular physiological activities, most of them responsible for functions of digestion activities such as oxidoreductase activity, catalytic activity, hydrolase activity and cofactor/ion binding. The compositions of precursor proteins, molecular weights, functions and cell compartments of the obtained peptides were quite different between two bloom stages. This is the first attempt to study peptidomics of N. scintillans, which provide important information on the functional studies of peptidomics in N. scintillans, especially food digestion and dietary protein utilization, as well as their relationship with bloom development. |
topic |
Noctiluca scintillans peptidomics mass spectrometry protein food digestion |
url |
https://www.frontiersin.org/articles/10.3389/fmars.2020.569807/full |
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