Guanylate-binding protein 5 (GBP5)

Guanylate-binding protein 5 is an interferon-γ-inducible large GTPase with critical roles in innate immunity against viral and bacterial pathogens[1][3][8]. GBP5 undergoes structural changes upon GTP binding, forming dimers that are necessary for its antiviral activity, particularly against HIV-1[1]. The protein exists in several splice variants, including a tumor-specific form missing the CaaX motif required for membrane association, which may alter its function in cancer[3]. GBP5 is highly expressed following stimulation by pro-inflammatory cytokines and is implicated in the regulation of immune signaling, promoting interferon production, and possibly serving as a biomarker for immune activation[7][8]. Structurally, GBP5 contains a globular GTPase domain and an extended helical domain, forming dimers upon activation[1]. Overall, emerging evidence positions GBP5 as a promising therapeutic target and biomarker in infection, immunity, and cancer[7][1][3].

Other names

GBP5hGBP5GTP-binding protein 5

Drugs targeting GTPase activity (putative; not yet established for GBP5 specifically); Modulation of oligomerization and immune pathways (generalizable from family function)