Examinations of GBP-related sequences have shown that zebrafish gbp3 and gbp4 contain an additional function to find (FIIND) and a caspase recruitment (CARD) domains that resemble those found within the inflammasome-related proteins: Apoptosis-associated speck-like protein containing a CARD (PYCARD) and NLR Family Pyrin Domain Containing 1 (NLRP1).

The physiological relevance of the GBP's GDPase activity might yield important insights to elucidate GBP-specific defensive profile versus other INF-induced GTPases(e.g.IRGs).

[7] Evidence has suggested GBPs as important players in a variety of disease conditions ranging from infectious and metabolic inflammatory diseases to cancer,[3][8] In the context of cell protection against bacteria, early efforts conducting loss-function assays revealed a reduced host resistance to several pathogens when lacking GBPs.

[9] More recent studies have indicated that GBPs appear to be an agent that disturbs the structural integrity of bacteria, stimulates inflammasome signaling, forms complexes on pathogen-containing vesicles in infected cells, and fosters autophagy and oxidative mechanisms helping pathogen clearance.

[10][11] Human GBP1 is secreted from cells without the need of a leader peptide, and has been shown to exhibit antiviral activity against Vesicular stomatitis virus and Encephalomyocarditis virus, as well as being able to regulate the inhibition of proliferation and invasion of endothelial cells in response to IFN-gamma.