Molecular characterization of a bactericidal permeability-increasing protein/lipopolysaccharide-binding protein from black rockfish (Sebastes schlegelii): Deciphering its putative antibacterial role

Seongdo Lee, Don Anushka Sandaruwan Elvitigala, Sukkyoung Lee, Hyun Chul Kim, Hae Chul Park, Jehee Lee

Research output: Contribution to journalArticle

2 Citations (Scopus)


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.

Original languageEnglish
Pages (from-to)266-275
Number of pages10
JournalDevelopmental and Comparative Immunology
Publication statusPublished - 2017 Feb 1



  • Antibacterial activity
  • Black rockfish
  • Immune stimulation
  • Transcriptional regulation

ASJC Scopus subject areas

  • Immunology
  • Developmental Biology

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