ABSTRACT
Crustins are cysteine-rich cationic antimicrobial peptides (AMPs) found in decapod crustaceans. Six novel crustin genes (Paj-CrusIc, Id, Ie, If, IIb and IIc) were identified in the morotoge shrimp, Pandalopsis japonica. Deduced amino acid sequences of isolated Paj-Crus genes ranged from 99 to 178 amino acid residues (10.6-17.8 kDa). Sequence analysis of nine isolated Paj-Crus genes and 100 different crustins from various decapod crustaceans revealed that a splice site and KXXXCP motif within the WAP domain may be the main criteria for classifying type I and II crustins, suggesting that the two types of crustin genes may have been generated by different processes. We also identified three intron-less crustin I genes (Paj-Crus Id, Ie and If) for the first time, which may have been generated by gene duplication. The tissue distribution profiles showed that Paj-CrusI genes were expressed predominantly in the gill and epidermis, whereas Paj-CrusII genes were expressed ubiquitously, suggesting that the two types of crustins may play different roles in various tissues or under different physiological conditions. Differing from previous results, hemocyte-specific crustin was not isolated from Pandalopsis japonica. This study showed that both types of crustin genes (types I and II) exist in decapod crustaceans and their primary structure and expression profiles differ from each other, suggesting that they may play different biological roles. This will help to extend our knowledge of the crustacean innate immune response, which will provide important basic information of shrimp immunity against various pathogens.
Subject(s)
Antimicrobial Cationic Peptides/genetics , Arthropod Proteins/genetics , Pandalidae/genetics , Amino Acid Sequence , Animals , Antimicrobial Cationic Peptides/chemistry , Antimicrobial Cationic Peptides/metabolism , Arthropod Proteins/chemistry , Arthropod Proteins/metabolism , Base Sequence , Cloning, Molecular , DNA, Complementary/genetics , DNA, Complementary/metabolism , Gene Expression Regulation , Models, Molecular , Molecular Sequence Data , Organ Specificity , Pandalidae/chemistry , Pandalidae/metabolism , Polymerase Chain Reaction , Protein Structure, Tertiary , RNA, Messenger/genetics , RNA, Messenger/metabolism , Sequence AlignmentABSTRACT
The entire mitochondrial genome sequence of Sphyraena pinguis collected from Korean water was determined by the Next Generation Sequencing (NGS) technology. Its total length was 16,620 bps in length, which possessed the canonical 37 genes in the eukaryotes. Unusual start codon was exclusively found in COX1(GTG), while incomplete stop codons (TA-/T-) were identified in ATP6, COX2, ND3, ND4, and Cyt b. A phylogenetic analysis with currently identified full mitogenomes in Perciformes, S. pinguis was most closely related to S. barracuda (76.87%) and S. jello (76.84%). This mitogenome sequence would explain the evolution of genus Sphyraena.
ABSTRACT
The complete mitochondrial genome of Odontobutis platycephala collected from a native Korean river was determined by the bioinformatics assembly of the next-generation sequencing (NGS) reads. The circular mitogenome was 17,590 bp length which harbored canonical 13 protein-coding genes, 22 tRNAs, and 2 rRNAs, which was identical to those of family Odontobutidae. Twenty-eight genes were located on H strand, whereas remaining nine genes were on L strand. Except for COX1 gene (GTG), other 12 protein-coding genes were predicted typical start codons (ATG). Among the currently known mitogenome sequences, O. platycephala showed highest identity (96.98%) to Korean haplotype of O. platycephala (NC010199).
ABSTRACT
As in all other oviparous animals, lipoprotein receptors play a critical role in lipid metabolism and reproduction in decapod crustaceans. Four full-length cDNAs encoding lipoprotein receptors (Paj-VgR, Paj-LpR1, Paj-LpR2A, and Paj-LpR2B) were identified from Pandalopsis japonica through a combination of EST screening and PCR-based cloning. Paj-LpR1 appears to be the first crustacean ortholog of insect lipophorin receptors, and its two paralogs, Paj-LpR2A and Paj-LpR2B, exhibited similar structural characteristics. Several transcriptional isoforms were also identified for all three Paj-LpRs. Each expression pattern was unique, suggesting different physiological roles for these proteins. Paj-VgR is an ortholog of vitellogenin (Vg) receptors from other decapod crustaceans. A phylogenetic analysis of lipoproteins and their receptors suggested that the nomenclature of Vgs from decapod crustaceans may need to be changed. A PCR-based transcriptional analysis showed that Paj-VgR and Paj-LpR2B are expressed almost exclusively in the ovary, whereas Paj-LpR1 and Paj-LpR2A are expressed in multiple tissues. The various transcriptional isoforms of the three Paj-LpRs exhibited unique tissue distribution profiles. A transcriptional analysis of each receptor using tissues with different GSI values showed that the change in transcription of Paj-VgRs, Paj-LpR2A and Paj-LpR1 was not as significant as that of Vgs during maturation. However, the transcriptional levels of Paj-LpR2B decreased in ovary at maturation, suggesting that their transcriptional regulation is involved in reproduction.