title: Hemerythrin-related antimicrobial peptide, msHemerycin, purified from the body of the Lugworm, Marphysa sanguinea.
abstract: A ∼1.7 kDa antimicrobial peptide was purified from the acidified body extract of the Lugworm, Marphysa sanguinea, by preparative acid-urea-polyacrylamide gel electrophoresis and C18 reversed-phase high performance liquid chromatography (HPLC). The identified peptide is composed of 14 amino acids with the N-terminal acetylation. Comparison of the identified amino acid sequences and molecular weight of this peptide with those of other known proteins or peptides revealed that this peptide had high identity to the N-terminus of hemerythrin of marine invertebrates and named the msHemerycin. The full-length hemerythrin cDNA of Lugworm was contained 1027-bp, including a 5'-untranslated region (UTR) of 60-bp, a 3'-UTR of 595-bp, and an open reading frame of 372-bp encoding 123 amino acids including the msHemerycin at the N-terminus. Tissue distribution of the msHemerycin mRNA suggests that it is constitutively expressed as a non-tissue-specific manner, however, a relatively higher expression level was observed in muscle (6.8-fold) and brain (6.3-fold), and the lowest level in digestive gland. The secondary structural prediction and homology modeling studies indicate that the msHemerycin might form an unordered structure and might act via unconventional mechanism. Our results suggest that the msHemerycin might be an innate immune component related to the host defenses in the Lugworm. This is the first report on the antimicrobial function of the peptide derived from the N-terminus of hemerythrin in the Lugworm, Marphysa sanguinea.
authors: Department of Food Science and Biotechnology, Kunsan National University, Kunsan 54150, South Korea. Electronic address: jungkileun@kunsan.ac.kr.
authors: Jung-Kil
authors: JK
authors: Seo
authors: Biotechnology Research Division, Aquaculture Industry Department, National Institute of Fisheries Science, Busan 46083, South Korea.
authors: Bo-Hye
authors: BH
authors: Nam
authors: Department of Biotechnology, Pukyong National University, Busan 48513, South Korea.
authors: Hye-Jin
authors: HJ
authors: Go
authors: Department of Food Science and Biotechnology, Kunsan National University, Kunsan 54150, South Korea.
authors: Minkyeong
authors: M
authors: Jeong
authors: Department of Marine Biotechnology, Kunsan National University, Kunsan 54150, South Korea.
authors: Ki-Young
authors: KY
authors: Lee
authors: Department of Marine Aquaculture and Aquatic Sciences, Kunsan National University, Kunsan 54150, South Korea.
authors: Sang-Man
authors: SM
authors: Cho
authors: Department of Chemistry, Kunsan National University, Kunsan 54150, South Korea.
authors: In-Ah
authors: IA
authors: Lee
authors: Department of Biotechnology, Pukyong National University, Busan 48513, South Korea. Electronic address: ngpark@pknu.ac.kr.
authors: Nam Gyu
authors: NG
authors: Park
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D000890:Anti-Infective Agents / Q000737:chemistry / Q000378:metabolism; D023181:Antimicrobial Cationic Peptides / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism; D001483:Base Sequence; D003001:Cloning, Molecular; D018076:DNA, Complementary / Q000235:genetics / Q000378:metabolism; D004591:Electrophoresis, Polyacrylamide Gel; D006422:Hemerythrin / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism; D011077:Polychaeta / Q000235:genetics* / Q000378:metabolism; D017433:Protein Structure, Secondary; D012333:RNA, Messenger / Q000235:genetics / Q000378:metabolism; D016415:Sequence Alignment; D014018:Tissue Distribution
chemical_list: D000890:Anti-Infective Agents; D023181:Antimicrobial Cationic Peptides; D018076:DNA, Complementary; D006422:Hemerythrin; D012333:RNA, Messenger
keywords: Antimicrobial activity; Innate immunity; Marphysa sanguinea; The Lugworm; The hemerythrin; Tissue distribution; cDNA