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DC Field | Value | Language |
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dc.contributor.author | Lee, S. | |
dc.contributor.author | Elvitigala, D. A. S | |
dc.contributor.author | Lee, S. | |
dc.contributor.author | Kim, H. C | |
dc.contributor.author | Park, H. C | |
dc.contributor.author | Lee, J. | |
dc.date.accessioned | 2021-06-06T06:45:56Z | |
dc.date.available | 2021-06-06T06:45:56Z | |
dc.date.issued | 2017 | |
dc.identifier.citation | Lee, 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.uri | http://archive.cmb.ac.lk:8080/xmlui/handle/70130/5306 | - |
dc.description.abstract | 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 (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.iso | en | en_US |
dc.publisher | Elsevier | en_US |
dc.subject | LBP/BPI | en_US |
dc.subject | Black rockfish | en_US |
dc.subject | Antibacterial activity | en_US |
dc.subject | Immune stimulation | en_US |
dc.subject | Transcriptional regulation | en_US |
dc.title | Molecular Characterization of a bactericidal permeability - increasing protein / ilpopolysaccharide - binding protein from black rockfish (sebastes schlegelii) : Deciphering its putative antibacterial role | en_US |
dc.type | Article | en_US |
Appears in Collections: | Department of Basic Sciences & Social Sciences |
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