Please use this identifier to cite or link to this item: http://archive.cmb.ac.lk:8080/xmlui/handle/70130/5306
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dc.contributor.authorLee, S.
dc.contributor.authorElvitigala, D. A. S
dc.contributor.authorLee, S.
dc.contributor.authorKim, H. C
dc.contributor.authorPark, H. C
dc.contributor.authorLee, J.
dc.date.accessioned2021-06-06T06:45:56Z
dc.date.available2021-06-06T06:45:56Z
dc.date.issued2017
dc.identifier.citationLee, S., Elvitigala, D. A. S., Lee, S., Kim, H. C., Park, H. C., & Lee, J. (2017). Molecular characterization of a bactericidal permeability-increasing protein/lipopolysaccharide-binding protein from black rockfish (Sebastes schlegelii): Deciphering its putative antibacterial role. Developmental & Comparative Immunology, 67, 266-275.en_US
dc.identifier.urihttp://archive.cmb.ac.lk:8080/xmlui/handle/70130/5306-
dc.description.abstractBactericidal 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 (Sebastes schlegelii) (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 RfLBP 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 in vitro LPS-binding activity and antibacterial activity against Escherichia coli, but not against Streptococcus iniae. Moreover, RfBPI/LBP 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
dc.language.isoenen_US
dc.publisherElsevieren_US
dc.subjectLBP/BPIen_US
dc.subjectBlack rockfishen_US
dc.subjectAntibacterial activityen_US
dc.subjectImmune stimulationen_US
dc.subjectTranscriptional regulationen_US
dc.titleMolecular Characterization of a bactericidal permeability - increasing protein / ilpopolysaccharide - binding protein from black rockfish (sebastes schlegelii) : Deciphering its putative antibacterial roleen_US
dc.typeArticleen_US
Appears in Collections:Department of Basic Sciences & Social Sciences

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