Target intelligence / Profile preview

BPI fold-containing family B member 3 (BPIFB3)

Target
BPIFB3
Molecular classification
Lipid-binding protein, BPI fold-containing protein, Other
01

Overview

BPI fold-containing family B member 3 (BPIFB3) is a lipid-binding protein localized predominantly in the endoplasmic reticulum (ER), where it plays a key role in regulating ER membrane morphology, autophagy (especially reticulophagy), and membrane remodeling. It facilitates replication of flaviviruses such as Dengue virus and Zika virus but restricts enteroviruses like coxsackievirus B. BPIFB3 is part of the BPI fold-containing protein family, which shares structural homology with antimicrobial proteins involved in the innate immune response, though BPIFB3 itself does not exhibit classical secreted antimicrobial activity. Its molecular function appears to center on controlling intracellular membrane dynamics, impacting the availability of membranes for viral replication, and influencing vesicle trafficking and cell defense mechanisms against infection and structural stress. BPIFB3’s expression is low under normal conditions, but its depletion causes pronounced effects on ER structure and cell autophagy, suggesting a tightly regulated and essential physiological role[1][2][3].

Other names
BPI fold-containing family B member 3BPIFB3C20orf185LPLUNC3RYA3ligand-binding protein RYA3Long palate, lung and nasal epithelium carcinoma-associated protein 3
02

Mechanism of action

Drugs targeting BPIFB3 would likely modulate cellular autophagy pathways or ER membrane morphology to affect viral replication rates[1][2].

03

Biological functions

Regulation of autophagyRegulation of endoplasmic reticulum (ER) morphologyHost factor in viral replication (flaviviruses, enteroviruses)Innate immune responsePossible odorant or ligand binding
04

Disease associations

Infection (especially flavivirus and enterovirus host factor)Cancer (associated name in carcinoma tissues)InflammationMidface dysplasiaAdenoiditis
05

Safety considerations

Disrupting BPIFB3 may affect normal ER morphology, autophagy, and potentially increase susceptibility to certain viral infections[1].

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