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Here, we show that the human protein GBP1 acts as a cytosolic "glue trap," capturing cytosolic Gram-negative bacteria through a unique protein motif and preventing disseminated infections in cell culture models. To escape from this GBP1-mediated host defense, Shigella employs a virulence factor that prevents or dislodges the association of GBP1 with cytosolic bacteria.
Results show that GBP1 is overexpressed in triple-negative breast cancer (TNBC), under the control of EGFR (show EGFR Proteins) and selectively affects the growth of TNBC cell lines.
These findings confirm the involvement of caspase-1 (show CASP1 Proteins) in non-classical secretion mechanisms and open novel perspectives for the extracellular function of secreted GBP-1.
Taken together, these results provide a new understanding of the antiviral mechanism of human GBP1, which possesses potent anti-Kaposi's sarcoma-associated herpesvirus activity, and suggest the critical role of viral RTA (show RBM9 Proteins) in the evasion of the innate immune response during primary infection by Kaposi's sarcoma-associated herpesvirus.
Elevated hGBP-1 RNA in ovarian tumors correlates with shorter recurrence-free survival. hGBP-1 does not confer paclitaxel resistance on MCF-7 and TMX2-28 breast cancer cells.
In insulitic islets from living patients with recent-onset T1D, most of the overexpressed ISGs, including GBP1, TLR3 (show TLR3 Proteins), OAS1 (show OAS1 Proteins), EIF2AK2 (show EIF2AK2 Proteins), HLA-E (show HLAE Proteins), IFI6 (show IFI6 Proteins), and STAT1 (show STAT1 Proteins), showed higher expression in the islet core compared with the peri (show PLIN1 Proteins)-islet area containing the surrounding immune cells
the study not only highlights the importance of hGBP1 tetramer in stimulated GMP (show NT5C2 Proteins) formation, but also demonstrates its role in the antiviral activity against hepatitis C virus.
GBP1 expression is elevated in human Glioblastoma multiforme tumors and positively correlates with EGFRvIII status in Glioblastoma multiforme specimens, and its expression is inversely correlated with the survival rate of Glioblastoma multiforme patients. Taken together, these results reveal that GBP1 may serve as a potential therapeutic target for Glioblastoma multiforme with EGFRvIII mutation.
GBP1 promotes lymph node metastasis and has a positive correlation with EGFR (show EGFR Proteins) expression in esophageal squamous cell carcinoma.
Molecular dynamics studies showed that only GTP (show AK3 Proteins) decreases the formation of the GBP1:PIM1 (show PIM1 Proteins) complex through an allosteric mechanism, outlining the rational for the identification of new compounds potentially able to revert resistance to paclitaxel.
GBP1 is associated with resistance against porcine reproductive and respiratory syndrome infection and efficient T cell activation in pigs.
Allele A in GBP1, the unfavourable allele, is associated with higher PRRSV viremia levels and lower weight gain following infection
cDNA sequences were cloned and the genomic structure of porcine GBP1 (poGBP1) and GBP2 (show GBP2 Proteins) (poGBP2), was analyzed.
Guanylate binding protein expression is induced by interferon. Guanylate binding proteins are characterized by their ability to specifically bind guanine nucleotides (GMP, GDP, and GTP) and are distinguished from the GTP-binding proteins by the presence of 2 binding motifs rather than 3.
, GTP-binding protein 1
, guanine nucleotide-binding protein 1
, guanylate binding protein 1, interferon-inducible, 67kDa
, interferon-induced guanylate-binding protein 1
, guanylate binding protein 1, interferon-inducible