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Last update 08 May 2025

BPI

Last update 08 May 2025

Basic Info

Synonyms

bactericidal permeability increasing protein, Bactericidal permeability-increasing protein, BPI

+ [2]

Introduction

The cytotoxic action of BPI is limited to many species of Gram-negative bacteria; this specificity may be explained by a strong affinity of the very basic N-terminal half for the negatively charged lipopolysaccharides that are unique to the Gram-negative bacterial outer envelope. Has antibacterial activity against the Gram-negative bacterium P.aeruginosa, this activity is inhibited by LPS from P.aeruginosa.

Drugs associated with BPI

CN118252914

Patent Mining

Target

BPI

Mechanism-

Active Org.

China-Japan Friendship Hospital

Originator Org.

China-Japan Friendship Hospital

Active Indication

Infectious Diseases [+3]

Inactive Indication-

Drug Highest PhaseDiscovery

First Approval Ctry. / Loc.-

First Approval Date20 Jan 1800

100 Clinical Results associated with BPI

100 Translational Medicine associated with BPI

0 Patents (Medical) associated with BPI

642

Literatures (Medical) associated with BPI

01 May 2025·Archives of Microbiology

Chimeric hBPI23-Fcγ protein shows bactericidal activity against drug-resistant Gram-negative bacteria and protects mice from lethal challenge

Article

Author: Huang, Chaoben ; Kong, Qingli ; Zhang, Xulong ; An, Yunqing ; Cao, Bin ; Ma, Tianxiao ; Wang, Yang ; Zhang, Qi

The antimicrobial peptides, such as host immune system-derived human bactericidal/permeability-increasing protein (hBPI), are the potential drugs for antibiotic-resistant Gram-negative bacterial infection. However, whether the purified chimeric hBPI₂₃-Fcγ protein has bactericidal activity against drug-resistant Gram-negative bacteria (GNB) and the relevant mechanisms have not been fully elucidated. In this study, the chimeric hBPI₂₃-Fcγ protein, which consisting of the functional N terminus of BPI and Fcγ1, were expressed and purified in a lab-scale. The chimeric hBPI₂₃-Fcγ protein showed longer half-life up to 148.2 min in vivo. The hBPI₂₃-Fcγ protein also showed significant bactericidal activity against standard and clinically isolated drug-resistant Acinetobacter baumannii (A. baumannii) and Escherichia coli (E. coli). In addition, the hBPI₂₃-Fcγ protein markedly decreased biofilm formation, neutralized bacterial lipopolysaccharides (endotoxin) and enhanced the opsonization of phagocytes, as well as significantly improved the survival rate of minimal lethal dose (MLD) of drug-resistant E. coli -infected mice. These results indicate that the BPI₂₃-Fcγ protein protected mice from drug-resistant GNB infection not only by direct bactericidal effect, but also by promoting opsonophagocytosis of macrophages. In conclusion, the chimeric BPI₂₃-Fcγ protein may be as a promising candidate of non-antibiotic biological agent for drug-resistant GNB infection.

01 Dec 2024·IBRO Neuroscience Reports

Identifying signature genes and their associations with immune cell infiltration in spinal cord injury

Article

Author: Zhao, Yingjie ; Chang, Su’e ; Chang, Su'e ; Lv, Meng ; Gao, Zhengchao

BackgroundEarly detection of spinal cord injury (SCI) is conducive to improving patient outcomes. In addition, many studies have revealed the role of immune cells in the progression or treatment of SCI. The objective of this study was to identify the early signature genes and clarify how they are related to immune cell infiltration in SCI.MethodsWe analysed and identified early signature genes associated with SCI via bioinformatics analysis of the GSE151371 dataset from the GEO database. These genes were subsequently verified in the GSE33886 dataset and qRT-PCR. Finally, the CIBERSORT algorithm was used to examine the immune cell infiltration in SCI and its relationship with signature genes.ResultsSeven SCI-related signature genes, including ARG1, RETN, BPI, GGH, CCNB1, HIST1H2AC, and HIST1H2BJ, were identified, and their expression was verified via an external validation cohort and qRT-PCR. Moreover, the ROC curves revealed the diagnostic value of these genes. In addition, on the basis of immune cell infiltration analysis, plasma cells, M0 macrophages, activated CD4+ memory T cells, γδ T cells, naive CD4+ T cells, and resting CD4+ memory T cells may participate in the progression of SCI.ConclusionThis study identified seven early signature genes of SCI that may serve as biomarkers for the early diagnosis of SCI and contribute to our understanding of immune changes during the pathology of SCI.

01 Nov 2024·Fish & Shellfish Immunology

A novel LPS binding /bactericidal permeability-increasing protein (LBP/BPI) from the scallop Argopecten purpuratus plays an essential role in host resistance to Vibrio infection

Article

Author: Borregales, Yurubí ; Rojas, Rodrigo ; Ramírez, Felipe ; Valenzuela, Cristian ; Farlora, Rodolfo ; Jorquera, Antonia ; Muñoz-Cerro, Katherine ; Schmitt, Paulina ; Montecinos, Camila ; Guzmán, Fanny ; González, Roxana ; Brokordt, Katherina ; Santelices, Max ; Mercado, Luis

Lipopolysaccharide binding proteins (LBPs) and bactericidal permeability increasing proteins (BPIs) play significant roles in the immune response of vertebrates against bacterial pathogens. These soluble proteins produced by immune cells, specifically interact with and bind to bacterial lipopolysaccharides (LPS), with BPIs also displaying antibacterial activity. In Argopecten purpuratus scallop larvae resistant to Vibrio bivalvicida VPAP30, we identified a significant overexpression of a transcript displaying molecular features of an LBP/BPI protein, both before and after infection. Therefore, in the present work we aimed to understand the role of this novel LBP/BPI, named ApLBP/BPI3, in the scallop resistance to this Vibrio. The ApLBP/BPI3 open reading frame encodes a putative protein of 506 amino acids, with a molecular weight 56.78 kDa. The protein contains a C-terminal domain of 403-amino acid that, after theorical cleavage, displays a soluble form of 44.99 kDa, featuring two BPI/LBP/CETP domains, an apolar binding pocket, a single disulfide bond and a BPI dimerization interface. Phylogenetic analysis reveals high similarity between ApLBP/BPI3 and other mollusk LBP/BPI proteins. Aplbp/bpi3 transcripts were constitutively and highly expressed in hemocytes, gills, mantle, and digestive gland tissues, and were induced following VPAP30 infection in scallop larvae and adult hemocytes. We characterized ApLBP/BPI3 protein using a polyclonal antibody against a synthetic peptide. ApLBP/BPI3 was secreted to the media by infected cultured hemocytes, detected by ELISA. ApLBP/BPI3 was spotted inside non-infected hemocytes, bound to the cell wall of V. bivalvicida after in vitro hemocyte infection, and coating the gills and mantle epithelial barriers before and after an in vivo immune challenge, with stronger detection after VPAP30 injection, detected by immunofluorescence. Infected scallop larvae showed increased ApLBP/BPI3 levels, with slightly higher production in resistant larvae, determined by Western blot. Finally, silencing the Aplbp/bpi3 transcript through RNA interference and and subsequently infecting scallop juveniles with an LD50 of V. bivalvicida resulted in 100 % mortality. Altogether, results demonstrate the essential role of this immune effector in the resistance of A. purpuratus.

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