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High-quality SNP calling from olive flounder, Paralichthys olivaceus, in Jeju Island, South Korea
Sukkyoung Lee,Taehyug Jeong,W.K.M. Omeka,D.S. Liyanage,Chaehyeon Lim,Kishanthini Nadarajapillai,H.M.V. Udayantha,W.M. Gayashani Sandamalika,Seong-Rip Oh,David B. Jones,Dean R. Jerry,Jehee Lee 한국수산과학회 양식분과 2021 한국수산과학회 양식분과 학술대회 Vol.2021 No.4
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>