title: A Diverse Family of Host-Defense Peptides (Piscidins) Exhibit Specialized Anti-Bacterial and Anti-Protozoal Activities in Fishes.
abstract: Conventional antibiotics and other chemical-based drugs are currently one of the most common methods used to control disease-related mortality in animal agriculture. Use of the innate immune system to decrease disease related mortalities is a novel alternative to conventional drugs. One component of the innate immune system is the host-defense peptides, also known as antimicrobial peptides. Host-defense peptides are typically small, amphipathic, α-helical peptides with a broad-spectrum of action against viral, bacterial, fungal, and/or protozoal pathogens. Piscidins are host-defense peptides first discovered in the hybrid striped bass (white bass, Morone chrysops, x striped bass, M. saxatilis). In this paper we identify four new piscidin isoforms in the hybrid striped bass and describe their tissue distributions. We also determine the progenitor species of origin of each piscidin (orthology) and propose a revised nomenclature for this newly described piscidin family based on a three class system. The Class I piscidins (22 amino acids in length; striped bass and white bass piscidin 1 and piscidin 3) show broad-spectrum activity against bacteria and ciliated protozoans, while the Class III piscidins (55 amino acids in length; striped bass and white bass piscidin 6 and striped bass piscidin 7) primarily show anti-protozoal activity. The Class II piscidins (44-46 amino acids in length; striped bass and white bass piscidin 4 and white bass piscidin 5) have a level of activity against bacteria and protozoans intermediate to Classes I and III. Knowledge of piscidin function and activity may help in the future development of disease-resistant lines of striped bass and white bass that could be used to produce superior hybrids for aquaculture.
authors.affiliation: Department of Applied Ecology, North Carolina State University, Raleigh, North Carolina, United States of America.
authors.forename: Scott A
authors.initials: SA
authors.lastname: Salger
authors.affiliation: Department of Applied Ecology, North Carolina State University, Raleigh, North Carolina, United States of America.
authors.forename: Katherine R
authors.initials: KR
authors.lastname: Cassady
authors.affiliation: Department of Applied Ecology, North Carolina State University, Raleigh, North Carolina, United States of America.
authors.forename: Benjamin J
authors.initials: BJ
authors.lastname: Reading
authors.affiliation: Department of Clinical Sciences, North Carolina State University, College of Veterinary Medicine, Raleigh, North Carolina, United States of America.
authors.forename: Edward J
authors.initials: EJ
authors.lastname: Noga
mesh_terms: D000595:Amino Acid Sequence / Q000235:genetics; D000818:Animals; D000900:Anti-Bacterial Agents / Q000276:immunology; D023181:Antimicrobial Cationic Peptides / Q000235:genetics* / Q000276:immunology; D060467:Disease Resistance / Q000235:genetics* / Q000276:immunology; D029941:Fish Proteins / Q000235:genetics* / Q000276:immunology; D005399:Fishes / Q000276:immunology / Q000382:microbiology / Q000469:parasitology; D015870:Gene Expression; D007113:Immunity, Innate; D016415:Sequence Alignment
chemical_list: D000900:Anti-Bacterial Agents; D023181:Antimicrobial Cationic Peptides; D029941:Fish Proteins; C449802:moronecidin protein, Morone saxatilis