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D. magna CT448 protease specificity

ABSTRACT: Mass developments of toxin-producing cyanobacteria are frequently observed in freshwater ecosystems due to eutrophication and global warming. These mass developments can partly be attributed to cyanobacterial toxins, such as protease inhibitors (PIs), which inhibit digestive serine proteases of Daphnia, the major herbivore of phytoplankton and cyanobacteria. To date, mechanisms of this inhibition in the gut of the crustacean Daphnia magna are not known. Here, we characterize a single serine protease, chymotrypsin 448 (CT448), which is present in the gut of the crustacean D. magna.

INSTRUMENT(S): maXis

ORGANISM(S): Daphnia Magna

SUBMITTER: Fatih Demir

LAB HEAD: Pitter Florian Huesgen

PROVIDER: PXD010978 | Pride | 2018-10-04

REPOSITORIES: Pride

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Heterologous expression and characterization of a novel serine protease from Daphnia magna: A possible role in susceptibility to toxic cyanobacteria.

Lange Jacqueline J Demir Fatih F Huesgen Pitter F PF Baumann Ulrich U von Elert Eric E Pichlo Christian C

Aquatic toxicology (Amsterdam, Netherlands) 20180926

Mass developments of toxin-producing cyanobacteria are frequently observed in freshwater ecosystems due to eutrophication and global warming. These mass developments can partly be attributed to cyanobacterial toxins, such as protease inhibitors (PIs), which inhibit digestive serine proteases of Daphnia, the major herbivore of phytoplankton and cyanobacteria. To date, mechanisms of this inhibition in the gut of the crustacean Daphnia magna are not known. Here, we characterize a single serine prot ...[more]

PMID: 30384195

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