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