Proteasome properties of hemocytes differ between the whiteleg shrimp Penaeus vannamei and the brown shrimp Crangon crangon (Crustacea, Decapoda)

Abstract

Crustaceans are intensively farmed in aquaculture facilities where they are vulnerable to parasites, bacteria, or viruses, often severely compromising the rearing success. The ubiquitin-proteasome system (UPS) is crucial for the maintenance of cellular integrity. Analogous to higher vertebrates, the UPS of crustaceans may also play an important role in stress resistance and pathogen defense. We studied the general properties of the proteasome system in the hemocytes of the whiteleg shrimp, Penaeus vannamei, and the European brown shrimp Crangon crangon. The 20S proteasome was the predominant proteasome population in the hemocytes of both species. The specific activities of the trypsin-like (Try-like), chymotrypsinlike (Chy-like), and caspase-like (Cas-like) enzymes of the shrimp proteasome differed between species. P. vannamei exhibited a higher ratio of Try-like to Chy-like activities and Caslike to Chy-like activities than C. crangon. Notably, the Chy-like activity of P. vannamei showed substrate or product inhibition at concentrations of more than 25 mmol L −1 . The K M values ranged from 0.072 mmol L −1 for the Try-like activity of P. vannamei to 0.309 mmol L −1 for the Cas-like activity of C. crangon. Inhibition of the proteasome of P. vannamei by proteasome inhibitors was stronger than in C. crangon. The pH profiles were similar in both species. The Try-like, Chy-like, and Cas-like sites showed the highest activities between pH 7.5 and 8.5. The proteasomes of both species were sensitive against repeated freezing and thawing losing~80-90% of activity. This study forms the basis for future investigations on the shrimp response against infectious diseases, and the role of the UPS therein.

Extracellular Vesicles and Post-Translational Protein Deimination Signatures in Mollusca—The Blue Mussel (Mytilus edulis), Soft Shell Clam (Mya arenaria), Eastern Oyster (Crassostrea virginica) and Atlantic Jacknife Clam (Ensis leei)

“…Ubiquitin extracted from oyster gill has been shown to have antibacterial activity against Gram-positive and Gram-negative bacteria [147]. Antipathogenic pathways mediated by ubiquitin have also been identified in Crustacea [148,149]. Ubiquitin has furthermore been associated with cancer, neurodegenerative and autoimmune diseases [150][151][152], while in Mollusca, ubiquitin has been found to play roles in regulating synaptic strength and growth, using the sea slug (Aplysia) model [153].…”

Orally administered nano-polystyrene caused vitellogenin alteration and oxidative stress in the red swamp crayfish (Procambarus clarkii)

“…Besides, the upregulation of the activating transcription factor 4 (ATF4) (Table S17), illustrated in Section 4.2.2.1, may be linked to the promotion of transcription of genes involved in autophagy (B'Chir et al, 2013), and the resistance to oxidative stress in the unfolded protein response (UPR) directed by PERK (Fusakio et al, 2016;Harding et al, 2003). The alteration of the intracellular protein degradation system has been reported in crustaceans exposed to several stressors (Götze et al, 2017;Hansen et al, 2008;Jiao et al, 2019;Xu et al, 2017;Zhao et al, 2017). Nevertheless, to the best of our knowledge, this is the first investigation reporting such a clear response of the UPS to NPs in Crustacea.…”

Transcriptional Identification of Related Proteins in the Immune System of the Crayfish Procambarus clarkii

“…The other sequence, the ubiquitin-conjugating enzyme E2 UBC9 had a 99% homology and was previously characterized in P. clarkii during a viral infection [ 54 ]. This table also includes 12 elements of the ubiquitin-proteasome system that we identified in Procambarus clarkii and annotated in GenBank; this system is crucial for the maintenance of cellular integrity and may play an important role in stress resistance and shrimp pathogen defense [ 55 ]. In the abdominal nervous cord of P. clarkii , several subunits of proteasomes that integrate the 26S complex as demonstrated in humans have been identified [ 56 ], and five sequences of this system have only been reported in insects.…”