期刊
DEVELOPMENTAL AND COMPARATIVE IMMUNOLOGY
卷 67, 期 -, 页码 266-275出版社
ELSEVIER SCI LTD
DOI: 10.1016/j.dci.2016.09.011
关键词
LBP/BPI; Black rockfish; Antibacterial activity; Immune stimulation; Transcriptional regulation
资金
- Ministry of Oceans and Fisheries, Korea
- National Institute of Fisheries Science [R2016001]
Bactericidal permeability-increasing protein (BPD/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 RJLBP that encodes a 474 amino acid protein with a predicted molecular mass of similar to 51.5 kDa. The primary protein sequence of Rfl3PI/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. (C) 2016 Elsevier Ltd. All rights reserved.
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