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In molecular biology, the guanylate-binding protein family is a family of GTPases that is induced by interferon (IFN)-gamma . GTPases induced by IFN-gamma (Interferon-inducible GTPase ) are key to the protective immunity against microbial and viral pathogens . These GTPases are classified into three groups: the small 47-KD immunity-related GTPases (IRGs ), the Mx proteins (MX1 , MX2 ), and the large 65- to 67-kd GTPases. Guanylate -binding proteins (GBP) fall into the last class. In humans, there are seven GBPs (hGBP1-7).[ 1] hGBP1 consists of two domains: a compact globular N-terminal domain harbouring the GTPase function, and an alpha-helical finger-like C-terminal domain.[ 2] 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.[ 3]
References
^ Tripal P, Bauer M, Naschberger E, Mortinger T, Hohenadl C, Cornali E, Thurau M, Sturzl M (January 2007). "Unique features of different members of the human guanylate-binding protein family". J. Interferon Cytokine Res . 27 (1): 44–52. doi :10.1089/jir.2007.0086 . PMID 17266443 . ^ Prakash B, Praefcke GJ, Renault L, Wittinghofer A, Herrmann C. Structure of human guanylate-binding protein 1 representing a unique class of GTP-binding proteins. Nature. 2000 Feb 3;403(6769):567-71. http://www.nature.com/nature/journal/v403/n6769/full/403567a0.html
^ Naschberger E, Lubeseder-Martellato C, Meyer N, Gessner R, Kremmer E, Gessner A, Sturzl M (September 2006). "Human guanylate binding protein-1 is a secreted GTPase present in increased concentrations in the cerebrospinal fluid of patients with bacterial meningitis" . Am. J. Pathol . 169 (3): 1088–99. doi :10.2353/ajpath.2006.060244 . PMC 1698817 PMID 16936281 .
