Proteomic profiles of benthopelagic deep-sea copepods

• Main Authors: Peters, Janna, Renz, Jasmin
• Format: Dataset
• Language: unknown
• Published: 2021
• Subjects: South Atlantic Ocean; Copepods
• Online Access: https://zenodo.org/record/4659288; https://doi.org/10.5061/dryad.8cz8w9gpx

In this study we used in parallel morphological, genetic, and proteomic charac­teristics of specimens of calanoid copepods from the abyssal South Atlantic to test if proteomic fingerprinting by matrix-assisted can accelerate estimating biodiversity. We cross-validated the respective molecular discrimi­nation methods with morphological identifications to establish COI and proteomic reference libraries. This data set includes all information on MALDI-TOF. Funding provided by: DFG initiative 1991 *Crossref Funder Registry ID: Award Number: RE 2808/3-1/2Funding provided by: DFG initiative 1991Crossref Funder Registry ID: Award Number: RE 2808/3-1/2 Calanoid copepods were collected in the benthopelagic boundary layer in the South Atlantic Ocean (14°58.91' S, 29°56.48' W) at a depth of 5139 m using an epibenthic sledge. On board, the samples were immediately fixed in 96% pure undenatured ethanol. Ethanol was exchanged within 24 hours of sampling and samples were constantly cooled for molecular analyses. Copepods were identified to morphospecies where possible (see reference table). In total 259 copepods were cut in half for further molecular analysis to allow for concurrent measurement of molecular genetic analysis and proteomic fingerprinting from the same specimens. Proteomic mass spectra were established using only the cephalosome of the individuals (except for individuals > 4 mm, where only the anterior part of the cephalosome was taken for analysis). The copepod tissue was quickly dried at room temperature. Depending on sample size 5-10 µl matrix solution (α-Cyano-4-hydroxycinnamic acid as saturated solution in 50% acetonitrile, 47.5% LC-MS grade water, and 2.5% trifluoroacetic acid) was added. After at least 10 min extraction 1.2 µl of each sample was added onto the target plate. Protein mass spectra were measured from 2 to 20 kD using a linear-mode MALDI-TOF System (Microflex LT/SH, Bruker Daltonics). Peak intensities were analyzed during random measurement in the range between 2 and 10 kDa using a ...