A new subfamily of penaeidin with an additional serine-rich region from kuruma shrimp (Marsupenaeus japonicus) contributes to antimicrobial and phagocytic activities. (June 2016)

• Record Type: Journal Article
• Authors: An, Ming-Yu; Gao, Jie; Zhao, Xiao-Fan; Wang, Jin-Xing
• Is Part Of: Developmental and comparative immunology. Volume 59(2016)
• Page Start: 186
• Page End: 198
• Publication Date: 2016-06
• Subjects: Penaeidin -- Antimicrobial peptide -- Marsupenaeus japonicus -- Innate immunity -- Antibacterial activity -- Phagocytosis; AMP antimicrobial peptides -- ALF antilipopolysaccharide factors -- Pen penaeidin -- PRR proline-rich region -- CRR cysteine-rich region -- SRR serine-rich region -- ORF open reading frame -- PG peptidoglycan -- LPS lipopolysaccharide -- LTA lipoteichoic acid -- ELISA enzyme-linked immunosorbent assay -- GFP green fluorescent protein -- FITC fluorescein isothiocyanate -- MAC minimal agglutinating concentration; Immunology -- Periodicals; Developmental immunology -- Periodicals; 616.079
• DOI: 10.1016/j.dci.2016.02.001
• Languages: English
• ISSNs: 0145-305X

Abstract

Abstract: Penaeidins are an important family of antimicrobial peptides (AMPs) in penaeid shrimp. To date, five groups of penaeidins have been identified in penaeid shrimp. All are composed of a proline-rich N-terminus and a C-terminus containing six cysteine residues engaged in three disulfide bridges. In this study, a new type of penaeidin from Marsupenaeus japonicus was identified. The full-length penaeidin contains a unique serine-rich region and a penaeidin domain, which consists of a proline-rich region and a cysteine-rich region. Here, we classify all penaeidins into two subfamilies. All reported penaeidins are in subfamily I, and the new penaeidin identified in M. japonicus is designated as Penaeidin subfamily II ( Mj Pen-II). Mj Pen-II was expressed in hemocytes, heart, hepatopancreas, gills, stomach and intestine, and was upregulated after bacterial challenge. A liquid bacteriostatic assay showed that Mj Pen-II had antibacterial activity to some Gram-positive and Gram-negative bacteria. Mj Pen-II could bind to bacteria by binding to polysaccharides on the surface of bacteria, thus promoting bacterial agglutination. The serine-rich region enhanced the agglutination activity of Mj Pen-II. The proline-rich domain had a stronger bacterial-binding activity and polysaccharide-binding activity than the cysteine-rich domain. Mj Pen-II was also found to be involved in the phagocytosis of bacteria and efficiently improved the phagocytosis rate. Therefore, Mj Pen-II eliminates bacteria through direct bacterial inhibition as well as by promoting phagocytosis in shrimp. Highlights: A new subfamily of penaeidin, Mj Pen-II, was identified in Marsupenaeus japonicus . Mj Pen-II had antibacterial activity in vitro . The serine-rich region of Mj Pen-II had binding activity to bacteria. Mj Pen-II inhibited the proliferation of bacteria in vivo . Mj Pen-II was involved in hemocyte phagocytosis.