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Journal articles on the topic 'Gbp2'

Author: Grafiati

Published: 6 September 2023

Last updated: 31 July 2025

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1

Clough, Barbara, Ryan Finethy, Rabia T. Khan, et al. "C57BL/6 and 129 inbred mouse strains differ in Gbp2 and Gbp2b expression in response to inflammatory stimuli in vivo." Wellcome Open Research 4 (August 20, 2019): 124. http://dx.doi.org/10.12688/wellcomeopenres.15329.1.

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Background: Infections cause the production of inflammatory cytokines such as Interferon gamma (IFNγ). IFNγ in turn prompts the upregulation of a range of host defence proteins including members of the family of guanylate binding proteins (Gbps). In humans and mice alike, GBPs restrict the intracellular replication of invasive microbes and promote inflammation. To study the physiological functions of Gbp family members, the most commonly chosen in vivo models are mice harbouring loss-of-function mutations in either individual Gbp genes or the entire Gbp gene cluster on mouse chromosome 3. Indi

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Feeley, Eric M., Danielle M. Pilla-Moffett, Erin E. Zwack, et al. "Galectin-3 directs antimicrobial guanylate binding proteins to vacuoles furnished with bacterial secretion systems." Proceedings of the National Academy of Sciences 114, no. 9 (2017): E1698—E1706. http://dx.doi.org/10.1073/pnas.1615771114.

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Many invasive bacteria establish pathogen-containing vacuoles (PVs) as intracellular niches for microbial growth. Immunity to these infections is dependent on the ability of host cells to recognize PVs as targets for host defense. The delivery of several host defense proteins to PVs is controlled by IFN-inducible guanylate binding proteins (GBPs), which themselves dock to PVs through poorly characterized mechanisms. Here, we demonstrate that GBPs detect the presence of bacterial protein secretion systems as “patterns of pathogenesis” associated with PVs. We report that the delivery of GBP2 to

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3

Legewie, Larissa, Jennifer Loschwitz, Nora Steffens, et al. "Biochemical and structural characterization of murine GBP7, a guanylate binding protein with an elongated C-terminal tail." Biochemical Journal 476, no. 21 (2019): 3161–82. http://dx.doi.org/10.1042/bcj20190364.

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Abstract Guanylate-binding proteins (GBPs) constitute a family of interferon-inducible guanosine triphosphatases (GTPases) that are key players in host defense against intracellular pathogens ranging from protozoa to bacteria and viruses. So far, human GBP1 and GBP5 as well as murine GBP2 (mGBP2) have been biochemically characterized in detail. Here, with murine GBP7 (mGBP7), a GBP family member with an unconventional and elongated C-terminus is analyzed. The present study demonstrates that mGBP7 exhibits a concentration-dependent GTPase activity and an apparent GTP turnover number of 20 min−1

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Srinivasachar Badarinarayan, Smitha, Irina Shcherbakova, Simon Langer, et al. "HIV-1 infection activates endogenous retroviral promoters regulating antiviral gene expression." Nucleic Acids Research 48, no. 19 (2020): 10890–908. http://dx.doi.org/10.1093/nar/gkaa832.

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Abstract Although endogenous retroviruses (ERVs) are known to harbor cis-regulatory elements, their role in modulating cellular immune responses remains poorly understood. Using an RNA-seq approach, we show that several members of the ERV9 lineage, particularly LTR12C elements, are activated upon HIV-1 infection of primary CD4+ T cells. Intriguingly, HIV-1-induced ERVs harboring transcription start sites are primarily found in the vicinity of immunity genes. For example, HIV-1 infection activates LTR12C elements upstream of the interferon-inducible genes GBP2 and GBP5 that encode for broad-spe

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Yu, Peifa, Yang Li, Yunlong Li, Zhijiang Miao, Maikel P. Peppelenbosch, and Qiuwei Pan. "Guanylate-binding protein 2 orchestrates innate immune responses against murine norovirus and is antagonized by the viral protein NS7." Journal of Biological Chemistry 295, no. 23 (2020): 8036–47. http://dx.doi.org/10.1074/jbc.ra120.013544.

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Noroviruses are the main causative agents of acute viral gastroenteritis, but the host factors that restrict their replication remain poorly identified. Guanylate-binding proteins (GBPs) are interferon (IFN)-inducible GTPases that exert broad antiviral activity and are important mediators of host defenses against viral infections. Here, we show that both IFN-γ stimulation and murine norovirus (MNV) infection induce GBP2 expression in murine macrophages. Results from loss- and gain-of-function assays indicated that GBP2 is important for IFN-γ–dependent anti-MNV activity in murine macrophages. E

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Liu, Bo, Rongfei Huang, Tingting Fu, et al. "GBP2 as a potential prognostic biomarker in pancreatic adenocarcinoma." PeerJ 9 (May 11, 2021): e11423. http://dx.doi.org/10.7717/peerj.11423.

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Background Pancreatic adenocarcinoma (PAAD) is a disease with atypical symptoms, an unfavorable response to therapy, and a poor outcome. Abnormal guanylate-binding proteins (GBPs) play an important role in the host’s defense against viral infection and may be related to carcinogenesis. In this study, we sought to determine the relationship between GBP2 expression and phenotype in patients with PAAD and explored the possible underlying biological mechanism. Method We analyzed the expression of GBP2 in PAAD tissues using a multiple gene expression database and a cohort of 42 PAAD patients. We ev

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Fry, Lucy, Noah Kelner, and Tiffany Weinkopff. "Host guanylate binding proteins participate in parasite control during Leishmania infection." Journal of Immunology 212, no. 1_Supplement (2024): 0466_5420. http://dx.doi.org/10.4049/jimmunol.212.supp.0466.5420.

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Abstract Cutaneous leishmaniasis (CL) is a debilitating neglected tropical disease causing lesions ranging from self-healing to permanent disfigurations. A predominant Th1 response relying on IFNγ production leads to parasite control during CL. Although IFNγ is mainly responsible for activating macrophages to produce NO leading to parasite control, IFNγ can activate other downstream pathways involved in cell autonomous immunity including the activation of guanylate binding proteins (GBPs), a class of interferon-inducible GTPases. GBPs play a role in host defense against some intracellular path

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Gao, Zhenzhen, Zejing Meng, Xiaobing He, et al. "Guanylate-Binding Protein 2 Exerts GTPase-Dependent Anti-Ectromelia Virus Effect." Microorganisms 11, no. 9 (2023): 2258. http://dx.doi.org/10.3390/microorganisms11092258.

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Guanylate-binding proteins (GBPs) are highly expressed interferon-stimulated genes (ISGs) that play significant roles in protecting against invading pathogens. Although their functions in response to RNA viruses have been extensively investigated, there is limited information available regarding their role in DNA viruses, particularly poxviruses. Ectromelia virus (ECTV), a member of the orthopoxvirus genus, is a large double-stranded DNA virus closely related to the monkeypox virus and variola virus. It has been intensively studied as a highly effective model virus. According to the study, GBP

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Ohshima, Jun, Miwa Sasai, Jianfa Liu та ін. "RabGDIα is a negative regulator of interferon-γ–inducible GTPase-dependent cell-autonomous immunity to Toxoplasma gondii". Proceedings of the National Academy of Sciences 112, № 33 (2015): E4581—E4590. http://dx.doi.org/10.1073/pnas.1510031112.

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IFN-γ orchestrates cell-autonomous host defense against various intracellular vacuolar pathogens. IFN-γ–inducible GTPases, such as p47 immunity-related GTPases (IRGs) and p65 guanylate-binding proteins (GBPs), are recruited to pathogen-containing vacuoles, which is important for disruption of the vacuoles, culminating in the cell-autonomous clearance. Although the positive regulation for the proper recruitment of IRGs and GBPs to the vacuoles has been elucidated, the suppressive mechanism is unclear. Here, we show that Rab GDP dissociation inhibitor α (RabGDIα), originally identified as a Rab

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Gao, Zhenzhen, Xiaobing He, Guohua Chen, et al. "The Viral Protein Poly(A) Polymerase Catalytic Subunit Interacts with Guanylate-Binding Proteins 2 to Antagonize the Antiviral Ability of Targeting Ectromelia Virus." International Journal of Molecular Sciences 24, no. 21 (2023): 15750. http://dx.doi.org/10.3390/ijms242115750.

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The recent spread of the monkeypox virus among humans has heightened concerns regarding orthopoxvirus infections. Consequently, conducting a comprehensive study on the immunobiology of the monkeypox virus is imperative for the development of effective therapeutics. Ectromelia virus (ECTV) closely resembles the genetic and disease characteristics of monkeypox virus, making it a valuable research tool for studying orthopoxvirus–host interactions. Guanylate-binding proteins (GBPs), highly expressed interferon-stimulated genes (ISGs), have antagonistic effects against various intracellular pathoge

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You, Ji-Eun, Eun-Ji Kim, Ho Won Kim, Jong-Seok Kim, Kyunggon Kim, and Pyung-Hwan Kim. "Exploring the Role of Guanylate-Binding Protein-2 in Activated Microglia-Mediated Neuroinflammation and Neuronal Damage." Biomedicines 12, no. 5 (2024): 1130. http://dx.doi.org/10.3390/biomedicines12051130.

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Neuron damage by microglia, which act as macrophage cells in the brain, can result in various brain diseases. However, the function of pro-inflammatory or anti-inflammatory microglia in the neurons remains controversial. Guanylate-binding protein-2 (GBP2) is expressed and activated in the microglia in the early phase of the inflammatory response and plays an important role in controlling immune responses. In this study, we evaluated whether GBP2 initially reduces the immune response induced by microglia, and whether microglia induce pro-inflammatory functions in neurons via GBP2 expression. In

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Zhang, Juan, Yu Zhang, Wenshuang Wu, et al. "Guanylate-binding protein 2 regulates Drp1-mediated mitochondrial fission to suppress breast cancer cell invasion." Cell Death & Disease 8, no. 10 (2017): e3151-e3151. http://dx.doi.org/10.1038/cddis.2017.559.

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Abstract Guanylate-binding protein 2 (GBP2) is a member of the large GTPase superfamily that is strongly induced by interferon-γ (IFN-γ). Although the biochemical characteristics of GBP2 have been reported in detail, its biological function has not been thoroughly elucidated to date. To the best of our knowledge, this study presents the first demonstration that GBP2 inhibits mitochondrial fission and cell metastasis in breast cancer cells both in vitro and in vivo. Our previous work demonstrated that dynamin-related protein 1 (Drp1)-dependent mitochondrial fission has a key role in breast canc

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Wang, Haizhou, Yabo Zhou, Yangyang Zhang, et al. "Subtyping of microsatellite stability colorectal cancer reveals guanylate binding protein 2 (GBP2) as a potential immunotherapeutic target." Journal for ImmunoTherapy of Cancer 10, no. 4 (2022): e004302. http://dx.doi.org/10.1136/jitc-2021-004302.

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BackgroundsProficient-mismatch-repair or microsatellite stability (pMMR/MSS) colorectal cancer (CRC) has limited efficacy for immune checkpoint blockade (ICB) therapy and its underlying mechanism remains unclear. Guanylate binding protein 2 (GBP2) is a member of the GTPase family and is crucial to host immunity against pathogens. However, the correlations between GBP2 and immunosurveillance and immunotherapy for pMMR/MSS CRC have not been reported.MethodsUnsupervised clustering was employed to classify immune class and non-immune class in 1424 pMMR/MSS patients from six independent public data

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14

Ma, Guojian, Jing Huang, Nunu Sun, et al. "Molecular characterization of the porcine GBP1 and GBP2 genes." Molecular Immunology 45, no. 10 (2008): 2797–807. http://dx.doi.org/10.1016/j.molimm.2008.02.007.

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15

Kubo, Yoshinao, Manya Bakatumana Hans, Taisuke Nakamura, and Hideki Hayashi. "The Furin Protease Dependence and Antiviral GBP2 Sensitivity of Murine Leukemia Virus Infection Are Determined by the Amino Acid Sequence at the Envelope Glycoprotein Cleavage Site." International Journal of Molecular Sciences 25, no. 18 (2024): 9987. http://dx.doi.org/10.3390/ijms25189987.

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Host restriction factor GBP2 suppresses the replication of the ecotropic Moloney murine leukemia virus (E-MLV) by inhibiting furin protease, which cleaves the viral envelope glycoprotein (Env) into surface (SU) and transmembrane (TM) subunits. We analyzed the impacts of GBP2 on the infection efficiency mediated by MLV Envs of different strains of ecotropic Moloney, polytropic Friend, amphotropic, and xenotropic MLV-related (XMRV) viruses. Interestingly, the Envs of ecotropic Moloney and polytropic Friend MLV were sensitive to the antiviral activity of GBP2, while XMRV and amphotropic Envs show

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16

Pinheiro, Ana, J. Ricardo Borges, João Vasco Côrte-Real, and Pedro J. Esteves. "Evolution of guanylate binding protein genes shows a remarkable variability within bats (Chiroptera)." Frontiers in Immunology 15 (June 12, 2024): 1329098. https://doi.org/10.5281/zenodo.13435572.

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(Uploaded by Plazi for the Bat Literature Project) Background: GBPs (guanylate binding proteins), an evolutionary ancient protein family, play a key role in the host's innate immune response against bacterial, parasitic and viral infections. In Humans, seven GBP genes have been described (GBP1-7). Despite the interest these proteins have received over the last years, evolutionary studies have only been performed in primates, Tupaia and rodents. These have shown a pattern of gene gain and loss in each family, indicative of the birth-and-death evolution process. Results: In this study, we analys

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Pinheiro, Ana, J. Ricardo Borges, João Vasco Côrte-Real, and Pedro J. Esteves. "Evolution of guanylate binding protein genes shows a remarkable variability within bats (Chiroptera)." Frontiers in Immunology 15 (June 7, 2024): 1329098. https://doi.org/10.5281/zenodo.13435572.

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(Uploaded by Plazi for the Bat Literature Project) Background: GBPs (guanylate binding proteins), an evolutionary ancient protein family, play a key role in the host's innate immune response against bacterial, parasitic and viral infections. In Humans, seven GBP genes have been described (GBP1-7). Despite the interest these proteins have received over the last years, evolutionary studies have only been performed in primates, Tupaia and rodents. These have shown a pattern of gene gain and loss in each family, indicative of the birth-and-death evolution process. Results: In this study, we analys

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Pinheiro, Ana, J. Ricardo Borges, João Vasco Côrte-Real, and Pedro J. Esteves. "Evolution of guanylate binding protein genes shows a remarkable variability within bats (Chiroptera)." Frontiers in Immunology 15 (July 3, 2024): 1329098. https://doi.org/10.5281/zenodo.13435572.

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(Uploaded by Plazi for the Bat Literature Project) Background: GBPs (guanylate binding proteins), an evolutionary ancient protein family, play a key role in the host's innate immune response against bacterial, parasitic and viral infections. In Humans, seven GBP genes have been described (GBP1-7). Despite the interest these proteins have received over the last years, evolutionary studies have only been performed in primates, Tupaia and rodents. These have shown a pattern of gene gain and loss in each family, indicative of the birth-and-death evolution process. Results: In this study, we analys

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Pinheiro, Ana, J. Ricardo Borges, João Vasco Côrte-Real, and Pedro J. Esteves. "Evolution of guanylate binding protein genes shows a remarkable variability within bats (Chiroptera)." Frontiers in Immunology 15 (July 10, 2024): 1329098. https://doi.org/10.5281/zenodo.13435572.

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(Uploaded by Plazi for the Bat Literature Project) Background: GBPs (guanylate binding proteins), an evolutionary ancient protein family, play a key role in the host's innate immune response against bacterial, parasitic and viral infections. In Humans, seven GBP genes have been described (GBP1-7). Despite the interest these proteins have received over the last years, evolutionary studies have only been performed in primates, Tupaia and rodents. These have shown a pattern of gene gain and loss in each family, indicative of the birth-and-death evolution process. Results: In this study, we analys

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Pinheiro, Ana, J. Ricardo Borges, João Vasco Côrte-Real, and Pedro J. Esteves. "Evolution of guanylate binding protein genes shows a remarkable variability within bats (Chiroptera)." Frontiers in Immunology 15 (July 17, 2024): 1329098. https://doi.org/10.5281/zenodo.13435572.

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(Uploaded by Plazi for the Bat Literature Project) Background: GBPs (guanylate binding proteins), an evolutionary ancient protein family, play a key role in the host's innate immune response against bacterial, parasitic and viral infections. In Humans, seven GBP genes have been described (GBP1-7). Despite the interest these proteins have received over the last years, evolutionary studies have only been performed in primates, Tupaia and rodents. These have shown a pattern of gene gain and loss in each family, indicative of the birth-and-death evolution process. Results: In this study, we analys

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Cui, Wen, Elisabeth Braun, Wei Wang, et al. "Structural basis for GTP-induced dimerization and antiviral function of guanylate-binding proteins." Proceedings of the National Academy of Sciences 118, no. 15 (2021): e2022269118. http://dx.doi.org/10.1073/pnas.2022269118.

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Guanylate-binding proteins (GBPs) form a family of dynamin-related large GTPases which mediate important innate immune functions. They were proposed to form oligomers upon GTP binding/hydrolysis, but the molecular mechanisms remain elusive. Here, we present crystal structures of C-terminally truncated human GBP5 (hGBP51–486), comprising the large GTPase (LG) and middle (MD) domains, in both its nucleotide-free monomeric and nucleotide-bound dimeric states, together with nucleotide-free full-length human GBP2. Upon GTP-loading, hGBP51–486 forms a closed face-to-face dimer. The MD of hGBP5 under

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Liang, Hai Po H., Edward J. Kerschen, Irene Hernandez, et al. "EPCR-dependent PAR2 activation by the blood coagulation initiation complex regulates LPS-triggered interferon responses in mice." Blood 125, no. 18 (2015): 2845–54. http://dx.doi.org/10.1182/blood-2014-11-610717.

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Abstract Infection and inflammation are invariably associated with activation of the blood coagulation mechanism, secondary to the inflammation-induced expression of the coagulation initiator tissue factor (TF) on innate immune cells. By investigating the role of cell-surface receptors for coagulation factors in mouse endotoxemia, we found that the protein C receptor (ProcR; EPCR) was required for the normal in vivo and in vitro induction of lipopolysaccharide (LPS)-regulated gene expression. In cultured bone marrow–derived myeloid cells and in monocytic RAW264.7 cells, the LPS-induced express

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Zhu, Liangyu, Hanxin Wu, Li Peng, et al. "CD4+ Effective Memory T Cell Markers GBP2 and LAG3 Are Risk Factors for PTB and COVID-19 Infection: A Study Integrating Single-Cell Expression Quantitative Trait Locus and Mendelian Randomization Analyses." International Journal of Molecular Sciences 25, no. 18 (2024): 9971. http://dx.doi.org/10.3390/ijms25189971.

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Observational studies indicate that variations in peripheral blood mononuclear cell (PBMC) subsets are associated with an increased risk of pulmonary tuberculosis (PTB) and coronavirus disease 2019 (COVID-19), but causal validation is lacking. Here, we combined single-cell expression quantitative trait locus (sc-eQTL) and two-sample mendelian randomization (MR) analyses to elucidate the causal relationship between PBMC subsets and the occurrence of PTB and COVID-19 and verified by RT-qPCR. We observed an increase in the CD4+ Effective Memory T Cell (CD4+ TEM) cluster in both PTB and COVID-19 p

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Yu, Shuye, Xiaoting Yu, Lili Sun, et al. "GBP2 enhances glioblastoma invasion through Stat3/fibronectin pathway." Oncogene 39, no. 27 (2020): 5042–55. http://dx.doi.org/10.1038/s41388-020-1348-7.

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Niedelman, Wendy, Joris K. Sprokholt, Barbara Clough, Eva-Maria Frickel, and Jeroen P. J. Saeij. "Cell Death of Gamma Interferon-Stimulated Human Fibroblasts upon Toxoplasma gondii Infection Induces Early Parasite Egress and Limits Parasite Replication." Infection and Immunity 81, no. 12 (2013): 4341–49. http://dx.doi.org/10.1128/iai.00416-13.

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ABSTRACTThe intracellular protozoan parasiteToxoplasma gondiiis a major food-borne illness and opportunistic infection for the immunosuppressed. Resistance toToxoplasmais dependent on gamma interferon (IFN-γ) activation of both hematopoietic and nonhematopoietic cells. Although IFN-γ-induced innate immunity in nonhematopoietic cells has been extensively studied in mice, it remains unclear what resistance mechanisms are relied on in nonhematopoietic human cells. Here, we report an IFN-γ-induced mechanism of resistance toToxoplasmain primary human foreskin fibroblasts (HFFs) that does not depend

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Yu, Shuye, and Ming Li. "CSIG-20. GBP2 ENHANCES GLIOBLASTOMA INVASION THROUGH STAT3/FIBRONECTION PATHWAY." Neuro-Oncology 20, suppl_6 (2018): vi47. http://dx.doi.org/10.1093/neuonc/noy148.186.

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Ahmetoglu, Derin, Haoyi Zheng, Aaron Swart, Hua Zhu, and Ming Li. "Multifaceted Roles of Guanylate-Binding Proteins in Cancer." International Journal of Molecular Sciences 26, no. 12 (2025): 5477. https://doi.org/10.3390/ijms26125477.

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Guanylate-binding proteins (GBPs), encompassing GBP1 through GBP7 in humans, are interferon-inducible large GTPases of the dynamin superfamily, renowned for their pivotal roles in cell-autonomous immunity against intracellular pathogens such as viruses, bacteria, and protozoa. By recognizing pathogen-associated molecular patterns (PAMPs) and danger-associated molecular patterns (DAMPs), GBPs orchestrate lysosomal targeting, regulate inflammatory cascades, and modulate apoptosis to protect host tissues from immune-mediated damage. Beyond their foundational roles in immunity, GBPs exhibit contex

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Lu, Yen-Yun, and Heike Krebber. "Nuclear mRNA Quality Control and Cytoplasmic NMD Are Linked by the Guard Proteins Gbp2 and Hrb1." International Journal of Molecular Sciences 22, no. 20 (2021): 11275. http://dx.doi.org/10.3390/ijms222011275.

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Pre-mRNA splicing is critical for cells, as defects in this process can lead to altered open reading frames and defective proteins, potentially causing neurodegenerative diseases and cancer. Introns are removed in the nucleus and splicing is documented by the addition of exon-junction-complexes (EJCs) at exon-exon boundaries. This “memory” of splicing events is important for the ribosome, which translates the RNAs in the cytoplasm. In case a stop codon was detected before an EJC, translation is blocked and the RNA is eliminated by the nonsense-mediated decay (NMD). In the model organism Saccha

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Kotov, Dmitri I., Jason S. Mitchell, Thomas Pengo, et al. "TCR Affinity Biases Th Cell Differentiation by Regulating CD25, Eef1e1, and Gbp2." Journal of Immunology 202, no. 9 (2019): 2535–45. http://dx.doi.org/10.4049/jimmunol.1801609.

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Martínez-Lumbreras, Santiago, Valerio Taverniti, Silvia Zorrilla, Bertrand Séraphin, and José Manuel Pérez-Cañadillas. "Gbp2 interacts with THO/TREX through a novel type of RRM domain." Nucleic Acids Research 44, no. 1 (2015): 437–48. http://dx.doi.org/10.1093/nar/gkv1303.

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Niu, Pengxia, Sang-Wook Kim, Won-Il Kim, and Kwan-Suk Kim. "Association analyses of DNA polymorphisms in immune-related candidate genes GBP1, GBP2, CD163, and CD169 with porcine growth and meat quality traits." Journal of Biomedical Research 16, no. 2 (2015): 40–46. http://dx.doi.org/10.12729/jbr.2015.16.2.040.

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Qin, Aiping, De-Hua Lai, Weijun Huang та ін. "Bone Marrow-Derived MSCs Stimulated by IFN-γ Inhibited the Growth of ToxoplasmaGondii Via up-Regulation of GBP1". Blood 124, № 21 (2014): 5143. http://dx.doi.org/10.1182/blood.v124.21.5143.5143.

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Abstract Background Mesenchymal stromal cells (MSCs) are a heterogeneous cell population endowed with multi-lineage differentiation potential and extensive immunomodulatory properties. MSCs have been successfully used for prevention and treatment of immune disorders such as graft-versus-host disease. Emerging preclinical studies suggest that MSCs might also protect against infectious challenge. Aims This study aimed to rule out the potential mechanism of human MSCs against Toxoplasma gondii (T. gondii). Methods Human bone marrow-derived MSCs (hMSCs) were pretreated for 24h with a series of con

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Zhao, Xiaoyu, Bocheng Yin, and Sarah E. Ewald. "Cell death effectors are recruited to Toxoplasma gondii parasite vacuoles targeted by interferon-inducible GTPases in infected dendritic cells." Journal of Immunology 206, no. 1_Supplement (2021): 110.04. http://dx.doi.org/10.4049/jimmunol.206.supp.110.04.

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Abstract Toxoplasma gondii is an obligate intracellular pathogen whose ability to grow and evade cell autonomous immunity depends on the parasitophorous vacuole membrane (PVM). The PVM forms from the host plasma membrane during invasion and is maintained by parasite effectors. Interferon-inducible GTPases (IIGs) are central in parasite clearance, however, the precise mechanism linking IIG attack of the PVM, parasite killing and inflammatory host cell death is not clear. To identify host and parasite proteins recruited to the PVM, we used Automated Spatially Targeted Optical Micro Proteomics (A

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Huang, Zhijian, Yunyun Han, and Xiaoting Qiu. "Abstract P2-04-26: Predicting the prognosis and immunotherapeutic response of triple-negative breast cancer by constructing a prognostic model based on CD8T cell-related immune genes." Clinical Cancer Research 31, no. 12_Supplement (2025): P2–04–26—P2–04–26. https://doi.org/10.1158/1557-3265.sabcs24-p2-04-26.

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Abstract Background: triple-negative breast cancer (TNBC) posed significant challenges in terms of treatment efficacy. CD8+ T cells, pivotal immune cells, can be effectively analyzed for gene expression differentials across diverse cell populations owing to the rapid advancements in sequencing technology. Leveraging these genes, our objective was to develop a prognostic model that accurately predicted the prognosis of TNBC patients and their responsiveness to immunotherapy. Methods: The sampl e information and clinical data of triple-negative breast cancer (TNBC) were sourced from the TCGA dat

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Zakharova, M. V., A. V. Dyomina, A. A. Kovalenko, O. E. Zubareva, A. M. Ischenko, and A. V. Zaitsev. "Anakinra Promotes M2 Microglia Activation during the Latent Phase of the Lithium-Pilocarpine Model of Temporal Lobe Epilepsy." Российский физиологический журнал им И М Сеченова 110, no. 3 (2024): 424–44. http://dx.doi.org/10.31857/s0869813924030074.

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Astrocytes and microglia and their polarization are thought to contribute to the progression of epilepsy. One of the processes affecting polarization is neuroinflammation, which plays an important role in epileptogenesis. However, the specific mechanisms of its involvement in shifting the pro- and anti-inflammatory reactivation of astro- and microglia have not been clarified. In this study, we examined the effect of 7-day interleukin-1 receptor antagonist (anakinra) administration on glial cell polarization during the latent phase of the lithium-pilocarpine model in 7-week-old male Wistar rats

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Tarhoni, I., C. Fhied, J. A. Borgia, M. J. Fidler, M. Batus, and P. Bonomi. "Novel Autoantibodies Biomarkers Panel to Prognosticate the Clinical Outcomes in Advanced-stage NSCLC Patients Receiving Anti PD-1/PD-L1 Immunotherapy." American Journal of Clinical Pathology 154, Supplement_1 (2020): S142. http://dx.doi.org/10.1093/ajcp/aqaa161.311.

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Abstract Introduction/Objective Lung cancer is the leading cause of cancer-related deaths worldwide, with a majority of cases detected at a non-resectable advanced stage. Current anti PD-1/-L1 therapy has reformed cancer treatment strategies with remarkable clinical outcomes in non-small cell lung cancer (NSCLC). However, the overall response rate is still marginal, demonstrating the need for biomarkers predictive of response. The objective of this study is to develop a serum based panel to prognosticate clinical response in advanced NSCLC patients receiving anti PD-1/-L1 therapy. Methods Pool

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Mori, Gentaro, Hodaka Sasaki, Yasushi Makabe, Masao Yoshinari, and Yasutomo Yajima. "The genes Scgb1a1, Lpo and Gbp2 characteristically expressed in peri-implant epithelium of rats." Clinical Oral Implants Research 27, no. 12 (2015): e190-e198. http://dx.doi.org/10.1111/clr.12601.

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Querl, Luisa, and Heike Krebber. "Defenders of the Transcriptome: Guard Protein-Mediated mRNA Quality Control in Saccharomyces cerevisiae." International Journal of Molecular Sciences 25, no. 19 (2024): 10241. http://dx.doi.org/10.3390/ijms251910241.

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Cell survival depends on precise gene expression, which is controlled sequentially. The guard proteins surveil mRNAs from their synthesis in the nucleus to their translation in the cytoplasm. Although the proteins within this group share many similarities, they play distinct roles in controlling nuclear mRNA maturation and cytoplasmic translation by supporting the degradation of faulty transcripts. Notably, this group is continuously expanding, currently including the RNA-binding proteins Npl3, Gbp2, Hrb1, Hrp1, and Nab2 in Saccharomyces cerevisiae. Some of the human serine–arginine (SR) splic

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Roy, Sayantan, Bing Wang, Yuan Tian, and Qian Yin. "Structural and biochemical characterization of an interferon-inducible GTPase, human guanylate binding protein 2 (GBP2)." Acta Crystallographica Section A Foundations and Advances 78, a1 (2022): a36. http://dx.doi.org/10.1107/s2053273322099636.

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Rahvar, Farzaneh, Mahdieh Salimi, and Hossein Mozdarani. "Study of GBP2 Gene Expression and Its Promoter Methylation Pattern in Tumors of Breast Cancer Patients." Multidisciplinary Cancer Investigation 1, Supplementary 1 (2017): 0. http://dx.doi.org/10.21859/mci-supp-04.

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Côrte-Real, João Vasco, Hanna-Mari Baldauf, José Melo-Ferreira, Joana Abrantes, and Pedro José Esteves. "Evolution of Guanylate Binding Protein (GBP) Genes in Muroid Rodents (Muridae and Cricetidae) Reveals an Outstanding Pattern of Gain and Loss." Frontiers in Immunology 13 (February 9, 2022). http://dx.doi.org/10.3389/fimmu.2022.752186.

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Guanylate binding proteins (GBPs) are paramount in the host immunity by providing defense against invading pathogens. Multigene families related to the immune system usually show that the duplicated genes can either undergo deletion, gain new functions, or become non-functional. Here, we show that in muroids, the Gbp genes followed an unusual pattern of gain and loss of genes. Muroids present a high diversity and plasticity regarding Gbp synteny, with most species presenting two Gbp gene clusters. The phylogenetic analyses revealed seven different Gbps groups. Three of them clustered with GBP2

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Place, David E., R. K. Subbarao Malireddi, Jieun Kim, Peter Vogel, Masahiro Yamamoto, and Thirumala-Devi Kanneganti. "Osteoclast fusion and bone loss are restricted by interferon inducible guanylate binding proteins." Nature Communications 12, no. 1 (2021). http://dx.doi.org/10.1038/s41467-020-20807-8.

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AbstractChronic inflammation during many diseases is associated with bone loss. While interferons (IFNs) are often inhibitory to osteoclast formation, the complex role that IFN and interferon-stimulated genes (ISGs) play in osteoimmunology during inflammatory diseases is still poorly understood. We show that mice deficient in IFN signaling components including IFN alpha and beta receptor 1 (IFNAR1), interferon regulatory factor 1 (IRF1), IRF9, and STAT1 each have reduced bone density and increased osteoclastogenesis compared to wild type mice. The IFN-inducible guanylate-binding proteins (GBPs

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Valeva, Stanimira V., Manon Degabriel, Fanny Michal, et al. "Comparative study of GBP recruitment on two cytosol-dwelling pathogens, Francisella novicida and Shigella flexneri highlights differences in GBP repertoire and in GBP1 motif requirements." Pathogens and Disease, April 3, 2023. http://dx.doi.org/10.1093/femspd/ftad005.

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Abstract Guanylate-Binding Proteins are interferon-inducible GTPases that play a key role in cell autonomous responses against intracellular pathogens. Despite sharing high sequence similarity, subtle differences among GBPs translate into functional divergences that are still largely not understood. A key GBP feature is the formation of supramolecular GBP complexes on the bacterial surface. Such complexes are observed when GBP1 binds lipopolysaccharide (LPS) from Shigella and Salmonella and further recruits GBP2-4. Here, we compared GBP recruitment on two cytosol-dwelling pathogens, Francisell

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Dickinson, Mary S., Miriam Kutsch, Linda Sistemich, et al. "LPS-aggregating proteins GBP1 and GBP2 are each sufficient to enhance caspase-4 activation both in cellulo and in vitro." Proceedings of the National Academy of Sciences 120, no. 15 (2023). http://dx.doi.org/10.1073/pnas.2216028120.

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The gamma-interferon (IFNγ)-inducible guanylate-binding proteins (GBPs) promote host defense against gram-negative cytosolic bacteria in part through the induction of an inflammatory cell death pathway called pyroptosis. To activate pyroptosis, GBPs facilitate sensing of the gram-negative bacterial outer membrane component lipopolysaccharide (LPS) by the noncanonical caspase-4 inflammasome. There are seven human GBP paralogs, and it is unclear how each GBP contributes to LPS sensing and pyroptosis induction. GBP1 forms a multimeric microcapsule on the surface of cytosolic bacteria through dire

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Marinho, Fabio V., Camila Brito, Ana Carolina V. S. C. de Araujo, and Sergio C. Oliveira. "Guanylate-binding protein-5 is involved in inflammasome activation by bacterial DNA but only the cooperation of multiple GBPs accounts for control of Brucella abortus infection." Frontiers in Immunology 15 (February 8, 2024). http://dx.doi.org/10.3389/fimmu.2024.1341464.

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IntroductionGuanylate-binding proteins (GBPs) are produced in response to pro-inflammatory signals, mainly interferons. The most studied cluster of GBPs in mice is on chromosome 3. It comprises the genes for GBP1-to-3, GBP5 and GBP7. In humans, all GBPs are present in a single cluster on chromosome 1. Brucella abortus is a Gram-negative bacterium known to cause brucellosis, a debilitating disease that affects both humans and animals. Our group demonstrated previously that GBPs present on murine chromosome 3 (GBPchr3) is important to disrupt Brucella-containing vacuole and GBP5 itself is import

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Luo, Yongyang, Hanyong Jin, Je Hyeong Kim, and Jeehyeon Bae. "Guanylate-binding proteins induce apoptosis of leukemia cells by regulating MCL-1 and BAK." Oncogenesis 10, no. 7 (2021). http://dx.doi.org/10.1038/s41389-021-00341-y.

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AbstractInterferon-inducible guanylate-binding proteins (GBPs) are well-known for mediating host-defense mechanisms against cellular pathogens. Emerging evidence suggests that GBPs are also implicated in tumorigenesis; however, their underlying molecular mechanism is still unknown. In this study, we identified that GBP1 and GBP2 interact with MCL-1, the key prosurvival member of the BCL-2 family, via its BH3 domain. GBPs induce caspase-dependent apoptosis in chronic myeloid leukemia (CML) and acute myeloid leukemia (AML) cells, where the proapoptotic BCL-2 member, BAK, is an indispensable medi

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Goers, Lisa, Kyungsub Kim, Teagan C. Stedman, et al. "Shigella IpaH9.8 limits GBP1-dependent LPS release from intracytosolic bacteria to suppress caspase-4 activation." Proceedings of the National Academy of Sciences 120, no. 15 (2023). http://dx.doi.org/10.1073/pnas.2218469120.

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Pyroptosis is an inflammatory form of cell death induced upon recognition of invading microbes. During an infection, pyroptosis is enhanced in interferon-gamma-exposed cells via the actions of members of the guanylate-binding protein (GBP) family. GBPs promote caspase-4 (CASP4) activation by enhancing its interactions with lipopolysaccharide (LPS), a component of the outer envelope of Gram-negative bacteria. Once activated, CASP4 promotes the formation of noncanonical inflammasomes, signaling platforms that mediate pyroptosis. To establish an infection, intracellular bacterial pathogens, like

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Fisch, Daniel, Barbara Clough, Rabia Khan, Lyn Healy, and Eva-Maria Frickel. "Toxoplasma-proximal and distal control by GBPs in human macrophages." Pathogens and Disease 79, no. 9 (2021). http://dx.doi.org/10.1093/femspd/ftab058.

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ABSTRACT Human guanylate binding proteins (GBPs) are key players of interferon–gamma (IFNγ)-induced cell intrinsic defense mechanisms targeting intracellular pathogens. In this study, we combine the well-established Toxoplasmagondii infection model with three in vitro macrophage culture systems to delineate the contribution of individual GBP family members to control this apicomplexan parasite. Use of high-throughput imaging assays and genome engineering allowed us to define a role for GBP1, 2 and 5 in parasite infection control. While GBP1 performs a pathogen-proximal, parasiticidal and growt

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Schelle, Luca, João Vasco Côrte-Real, Sharmeen Fayyaz, et al. "Evolutionary and functional characterization of lagomorph guanylate-binding proteins: a story of gain and loss and shedding light on expression, localization and innate immunity-related functions." Frontiers in Immunology 15 (January 29, 2024). http://dx.doi.org/10.3389/fimmu.2024.1303089.

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Guanylate binding proteins (GBPs) are an evolutionarily ancient family of proteins that are widely distributed among eukaryotes. They belong to the dynamin superfamily of GTPases, and their expression can be partially induced by interferons (IFNs). GBPs are involved in the cell-autonomous innate immune response against bacterial, parasitic and viral infections. Evolutionary studies have shown that GBPs exhibit a pattern of gene gain and loss events, indicative for the birth-and-death model of evolution. Most species harbor large GBP gene clusters that encode multiple paralogs. Previous functio

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Kohler, Kristin M., Miriam Kutsch, Anthony S. Piro, Graham D. Wallace, Jörn Coers, and Matthew F. Barber. "A Rapidly Evolving Polybasic Motif Modulates Bacterial Detection by Guanylate Binding Proteins." mBio 11, no. 3 (2020). http://dx.doi.org/10.1128/mbio.00340-20.

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ABSTRACT Cell-autonomous immunity relies on the rapid detection of invasive pathogens by host proteins. Guanylate binding proteins (GBPs) have emerged as key mediators of vertebrate immune defense through their ability to recognize a diverse array of intracellular pathogens and pathogen-containing cellular compartments. Human and mouse GBPs have been shown to target distinct groups of microbes, although the molecular determinants of pathogen specificity remain unclear. We show that rapid diversification of a C-terminal polybasic motif (PBM) in primate GBPs controls recognition of the model cyt

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