On the wave of the crustin antimicrobial peptide family: From sequence diversity to function

• Published in: Fish and shellfish immunology reports Vol. 3; p. 100069
• Main Authors: Barreto, Cairé, Matos, Gabriel M, Rosa, Rafael D
• Format: Journal Article
• Language: English
• Published: Elsevier Ltd 01.12.2022; Elsevier
• Subjects: 11.5-kDa peptide; Carcinin; Crustacean; Host defense peptide (HDP); Invertebrate immunity; Whey four disulfide core domain (WFDC); Carcinin; Invertebrate immunity; Whey four disulfide core domain (WFDC); 11.5-kDa peptide; Crustacean; Host defense peptide (HDP)
• ISSN: 2667-0119; 2667-0119
• DOI: 10.1016/j.fsirep.2022.100069

•Crustins represent the largest and most diverse AMP family found in crustaceans.•Crustins exhibit several biological functions beyond their antimicrobial properties.•Three crustin classification systems are currently recognized. Crustins represent the largest and most diverse family of antimicrobial peptides (AMPs) found in crustaceans. They are classically defined as disulfide-rich peptides/polypeptides holding a typical Whey Acidic Protein (WAP) domain at the C-terminal end. This WAP domain has eight cysteine residues forming a tightly packed structure, the four-disulfide core (4DSC) motif, that is also found in other proteins displaying protease inhibitory properties. Crustins are highly diverse in terms of primary structure, size and biochemical features, thus exhibiting a series of biological functions beyond their antimicrobial properties. In order to better categorize the distinct crustin members, different classification systems have been proposed. In this review, we discuss the current classification systems and explore the biological implication of the impressive molecular diversity of this unique AMP family. We also summarize the recent findings on the role of these effectors in crustacean immunity and homeostasis as well as in host-microbe interactions.