Near-future ocean acidification does not alter the lipid content and fatty acid composition of adult Antarctic krill.

Euphausia superba (Antarctic krill) is a keystone species in the Southern Ocean, but little is known about how it will respond to climate change. Ocean acidification, caused by sequestration of carbon dioxide into ocean surface waters (pCO2), alters the lipid biochemistry of some organisms. This can have cascading effects up the food chain. In a year-long laboratory experiment adult krill were exposed to ambient seawater pCO2 levels (400 µatm), elevated pCO2 levels mimicking near-future ocean acidification (1000, 1500 and 2000 µatm) and an extreme pCO2 level (4000 µatm). Total lipid mass (mg g-1 DM) of krill was unaffected by near-future pCO2. Fatty acid composition (%) and fatty acid ratios associated with immune responses and cell membrane fluidity were also unaffected by near-future pCO2, apart from an increase in 18:3n-3/18:2n-6 ratios in krill in 1500 µatm pCO2 in winter and spring. Extreme pCO2 had no effect on krill lipid biochemistry during summer. During winter and spring, krill in extreme pCO2 had elevated levels of 18:2n-6 (up to 1.2% increase), 20:4n-6 (up to 0.8% increase), lower 18:3n-3/18:2n-6 and 20:5n-3/20:4n-6 ratios, and showed evidence of increased membrane fluidity (up to three-fold increase in phospholipid/sterol ratios). These results indicate that the lipid biochemistry of adult krill is robust to near-future ocean acidification.

A thioredoxin from antarctic microcrustacean (Euphausia superba): Cloning and functional characterization.

Thioredoxins, with a dithiol/disulfide active site (CGPC) are major highly conserved and ubiquitous proteins that are involved in protecting organisms against various oxidative stresses. In the present study, a novel thioredoxin gene was identified in antarctic microcrustacean, Euphausia superba (designated as EsTrx1). The full-length cDNA sequences of EsTrx1 was of 621 bp, containing a 5' untranslated region (UTR) of 45 bp, a 3' UTR of 276 bp and an open reading frame (ORF) of 303 bp encoding a putative protein of 100 amino acids. The predicted molecular weight of EsTrx1 was 11.08 kDa and the theoretical isoelectric point was 4.51. Multiple sequence alignment indicated that the EsTrx1 possessed conserved CGPC redox-active site. EsTrx1 shared 68.6% similarity with the Chinese mitten crab (Eriocheir sinensis) Trx1. The predicted three-dimensional structure of EsTrx1 consisted of a central core of a four-stranded ß-sheet and four flanking α-helices. The high similarity of EsTrx1 with Trx1s from other animals together with the phylogenetic analysis indicated that EsTrx1 could be a novel member of Trx1 sub-family. In order to elucidate its biological functions, the recombinant EsTrx1 was constructed and expressed in Escherichia coli BL21 (DE3). Experiments demonstrated that the rEsTrx1 fusion protein possessed the expected redox activity in enzymatic analysis, and be more potent than GSH in antioxidant capacity. These results together indicated that EsTrx1 could be involved in the oxidative stress response of E. superba.

Identification of tropomyosins as major allergens in antarctic krill and mantis shrimp and their amino acid sequence characteristics.

Tropomyosin represents a major allergen of decapod crustaceans such as shrimps and crabs, and its highly conserved amino acid sequence (>90% identity) is a molecular basis of the immunoglobulin E (IgE) cross-reactivity among decapods. At present, however, little information is available about allergens in edible crustaceans other than decapods. In this study, the major allergen in two species of edible crustaceans, Antarctic krill Euphausia superba and mantis shrimp Oratosquilla oratoria that are taxonomically distinct from decapods, was demonstrated to be tropomyosin by IgE-immunoblotting using patient sera. The cross-reactivity of the tropomyosins from both species with decapod tropomyosins was also confirmed by inhibition IgE immunoblotting. Sequences of the tropomyosins from both species were determined by complementary deoxyribonucleic acid cloning. The mantis shrimp tropomyosin has high sequence identity (>90% identity) with decapod tropomyosins, especially with fast-type tropomyosins. On the other hand, the Antarctic krill tropomyosin is characterized by diverse alterations in region 13-42, the amino acid sequence of which is highly conserved for decapod tropomyosins, and hence, it shares somewhat lower sequence identity (82.4-89.8% identity) with decapod tropomyosins than the mantis shrimp tropomyosin. Quantification by enzyme-linked immunosorbent assay revealed that Antarctic krill contains tropomyosin at almost the same level as decapods, suggesting that its allergenicity is equivalent to decapods. However, mantis shrimp was assumed to be substantially not allergenic because of the extremely low content of tropomyosin.