[Problem] To provide a nucleic acid expected to be useful for treating crustacean allergy.

[Means to be solved] Provided is a nucleic acid comprising a nucleotide sequence encoding a chimeric protein, wherein the nucleic acid comprises a nucleotide sequence encoding a signal peptide, a nucleotide sequence encoding an intra-organelle stabilizing domain of LAMP, a nucleotide sequence encoding an allergen domain comprising Lit v 1, Lit v 4, and Lit v 3, a nucleotide sequence encoding a transmembrane domain and a nucleotide sequence encoding an endosomal/lysosomal targeting domain of LAMP in this order.

Disclosed is a mussel adhesive protein including at least one photocaged 3,4-dihydroxyphenylalanine derivative residue including a protecting group on at least one hydroxyl residue of its catechol moiety. The photocaged 3,4-dihydroxyphenylalanine derivative residue replaces a naturally occurring amino acid and the protecting group can be cleaved from the 3,4-dihydroxyphenylalanine derivative residue by irradiation with UV light.

Isolated proteins from caligid copepods, polynucleotides encoding the same, and antigens and vaccines comprising the same, in particular for the treatment or prevention of caligid copepod infection in fish. Proteins are peroxiredoxin-2 (Prx-2), fructose bisphosphate aldolase (FBP); enolase, transitionally-controlled tumour protein homolog (TCTP) and triosephosphate isomerase (TIM).

A biologically active non-lipid extract comprising of an isolated molecular weight fraction of <10 kDa or <1 kDa derived from New Zealand green-lipped mussels (Perna canaliculus). The extract exhibits biological activity selected from one or more of antihypertensive activity, antioxidant activity, antimicrobial activity, antiviral activity, and antiparasitic activity. The extract includes a plurality of biologically active substances selected from the group having free amino acids; peptides; cryptides; sugars and/or sugar-containing compounds including nucleosides and their derivatives; carbohydrates including glycoconjugates such as glycosides, glycosylamines, glycoproteins, glycopeptides, peptidoglycans; nitrogen-containing compounds including purines; phenolic compounds; minerals; metabolites.

Provided is an antimicrobial peptide Sparamosin from Scylla paramamosain. The Sparamosin mature peptide and its functional domain Sparamosin.sub.26-54 were synthesized by solid-phase synthesis with a purity of over 95%. Both Sparamosin and Sparamosin.sub.26-54 exhibit strong antimicrobial activity. More importantly, Sparamosin.sub.26-54 has strong antifungal activity and could inhibit the growth of a variety of yeasts and filamentous fungi. Based on the potent antimicrobial activities of Sparamosin and Sparamosin.sub.26-54, both peptides could be developed as alternatives for conventional antibiotics, antimicrobial agents, feed additives in aquaculture and livestock, preservatives, and mold inhibitors.

Luciferases which are different from those known heretofore have been desired. A luciferase mutant comprising an amino acid sequence in which at least one amino acid selected from the group consisting of valine at the position of 44, alanine at the position of 54 and tyrosine at the position of 138 is substituted with other amino acid(s) in the amino acid sequence of SEQ ID NO: 2.

Described herein are proteins and fragments thereof that can be capable of binding or otherwise interacting with a Vibrio species toxin. The Vibrio toxin binding proteins and fragments thereof can be included in a formulation, such as a feed formulation, that can be used to treat and/or prevent Vibrio spp. disease or a symptom thereof, such as AHPND. Also described herein are AHPND susceptibility signatures that can be useful for identification of susceptible and/or resistant/tolerant organisms.

Disclosed herein is a protein-based, genetically-encoded bioluminescent sensor that can report changes in intracellular ATP in live cells. This sensor is built from the NanoLuc luciferase (Promega) and mScarlet red fluorescent protein (DOI: 10.1038/nmeth.4074) in a novel platform that provides a much more quantitative optical signal for measurements. Analytical Chemistry demonstrates its characterization and that it can be used to image ATP differences in live cells under the skin of mice. This new sensor can be very useful for research purposes in cancer biology to measure cell health and chemotherapeutic drug efficacy for example in animal models of tumors or in cell-based screening.

Antimicrobial peptides of general formula X.sub.0X.sub.1X.sub.2C X.sub.3X.sub.4X.sub.5CX.sub.6X.sub.7X.sub.8X.sub.9CYX.sub.10X.sub.11CX.sub.12X.sub.13 are provided. Also provided are certain formulations containing these peptides and methods of using these peptides for treating skin infections in an animal in need thereof.

Provided herein are compositions and methods for the assembly of a bioluminescent complex from two or more non-luminescent (e.g., substantially non-luminescent) peptide and/or polypeptide units. In particular, bioluminescent activity is conferred upon a non-luminescent polypeptide via structural complementation with another, complementary non-luminescent peptide.