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Lee, Seongdo,Elvitigala, Don Anushka Sandaruwan,Lee, Sukkyoung,Kim, Hyun Chul,Park, Hae-Chul,Lee, Jehee Elsevier 2017 Developmental and comparative immunology Vol.67 No.-
<P><B>Abstract</B></P> <P>Bactericidal permeability-increasing protein (BPI)/lipopolysaccharide (LPS) binding proteins (LBPs) are well-known proteins that play an indispensable role in host antimicrobial defense. Herein, we report a homolog of BPI/LBP from black rockfish (<I>Sebastes schlegelii</I>) (designated as RfBPI/LBP) and characterize its structural and functional features at the molecular level. We identified the putative complete open reading frame (1422 bp) of <I>RfLBP</I> that encodes a 474 amino acid protein with a predicted molecular mass of ∼51.5 kDa. The primary protein sequence of RfBPI/LBP contains domain features of BPI/LBP family proteins and shares significant sequence consistency with its homologs. Our phylogenetic analysis clearly demonstrated the vertebrate ancestral origin of RfBPI/LBP, further reinforcing its evolutionary relationship with teleostean homologs. Recombinant RfBPI/LBP demonstrated <I>in vitro</I> LPS-binding activity and antibacterial activity against <I>Escherichia coli</I>, but not against <I>Streptococcus iniae</I>. Moreover, <I>RfBPI/LBP</I> exhibited temporal transcriptional activation against pathogens and pathogen-associated molecular patterns. Collectively, our findings suggest that RfBPI/LBP plays an essential role in host antimicrobial defense, plausibly through selective eradication of invading bacteria.</P> <P><B>Highlights</B></P> <P> <UL> <LI> Homolog of BPI/LBP was identified from black rockfish (RfBPI/LBP). </LI> <LI> Rf RfBPI/LBP resembled typical domain architecture of its homologues. </LI> <LI> Recombinant RfBPI/LBP showed selective antibacterial and LPS binding activity. </LI> <LI> <I>RfBPI/LBP</I> was ubiquitously expressed in tissues under physiological conditions. </LI> <LI> Transcriptional level of <I>RfBPI/LBP</I> was modulated under pathogenic stress. </LI> </UL> </P>
Lee, Jehee,Munasinghe, Helani,Song, Choon Bok 한국수산학회 2003 Fisheries and Aquatic Sciences Vol.6 No.3
Isolation and cloning of seven-band grouper (Epirzephelus septenzfusciatus) growth hormone cDNA from pituitary gland revealed an open reading frame of 612 bp coding for a pre-growth hormone of 204 amino acids with a 17 amino acid putative signal peptide. Deduced amino acid sequence showed that there was one ossible N-glycosylation site at Asn^(184) and four cysteine residues (Cys^(52), Cys^(160), Cys^(177), Cys^(185) on the same positions as in some other species where they were involved in the stabilization of the tertiary structure. The seven-band grouper growth hormone (sbgGH) presented a 99.5% amino acid sequence identity with the growth hormone of Epinephelus coioides and contained the conserved hormone domain region. Comparison of growth hormone sequences from evolutionarily diverse species revealed 25 amino acid residues conserved in jawless fishes to modern mammals. It also revealed an evolutionary trend to retain the same polypeptide sequence even in the distantly related animals while allowing alterations to occur in polypeptides of the closely related species. In order to create a recombinant system to produce high levels of the growth hormone, it was expressed in Escherichia coli (BL21) cells. The gel analysis revealed theoretically expected molecular weights for both mature and pre-sbgGHs.