Top

Published in:

Open Access 13-04-2022 | Interferon | Review

Functional cross-species conservation of guanylate-binding proteins in innate immunity

Authors: Luca Schelle, João Vasco Côrte-Real, Pedro José Esteves, Joana Abrantes, Hanna-Mari Baldauf

Published in: Medical Microbiology and Immunology | Issue 2/2023

Abstract

Guanylate binding proteins (GBPs) represent an evolutionary ancient protein family widely distributed among eukaryotes. They are interferon (IFN)-inducible guanosine triphosphatases that belong to the dynamin superfamily. GBPs are known to have a major role in the cell-autonomous innate immune response against bacterial, parasitic and viral infections and are also involved in inflammasome activation. Evolutionary studies depicted that GBPs present a pattern of gain and loss of genes in each family with several genes pseudogenized and some genes more divergent, indicative for the birth-and-death evolution process. Most species harbor large GBP gene clusters encoding multiple paralogs. Previous functional studies mainly focused on mouse and human GBPs, but more data are becoming available, broadening the understanding of this multifunctional protein family. In this review, we will provide new insights and give a broad overview about GBP evolution, conservation and their roles in all studied species, including plants, invertebrates and vertebrates, revealing how far the described features of GBPs can be transferred to other species.

MacMicking JD (2004) GTP-binding proteins: structure-function relationships. Trends Immunol 25(11):601–609. https://doi.org/10.1016/j.it.2004.08.010CrossRefPubMed

Jimah JR, Hinshaw JE (2019) Structural insights into the mechanism of dynamin superfamily proteins. Trends Cell Biol 29(3):257–273. https://doi.org/10.1016/j.tcb.2018.11.003CrossRefPubMed

Prakash B, Praefcke GJK, Renault L, Wittinghofer A, Herrmann C (2000) Structure of human guanylate-binding protein 1 representing a unique class of GTP-binding proteins. Nature 403(6769):567–571. https://doi.org/10.1038/35000617CrossRefPubMed

Cui W, Braun E, Wang W, Tang J, Zheng Y, Slater B et al (2021) Structural basis for GTP-induced dimerization and antiviral function of guanylate-binding proteins. Proc Natl Acad Sci USA 118(15):1–9. https://doi.org/10.1073/pnas.2022269118CrossRef

Wittinghofer A, Vetter IR (2011) Structure-function relationships of the G domain, a canonical switch motif. Annu Rev Biochem 80:943–971. https://doi.org/10.1146/annurev-biochem-062708-134043 (Epub 2011/06/17)CrossRefPubMed

Britzen-Laurent N, Bauer M, Berton V, Fischer N, Syguda A, Reipschläger S et al (2010) Intracellular trafficking of guanylate-binding proteins is regulated by heterodimerization in a hierarchical manner. PLoS ONE 5(12):e14246. https://doi.org/10.1371/journal.pone.0014246CrossRefPubMedPubMedCentral

Shydlovskyi S, Zienert AY, Ince S, Dovengerds C, Hohendahl A, Dargazanli JM et al (2017) Nucleotide-dependent farnesyl switch orchestrates polymerization and membrane binding of human guanylate-binding protein. Proc Natl Acad Sci USA 114(28):E5559–E5568. https://doi.org/10.1073/pnas.1620959114CrossRefPubMedPubMedCentral

Sistemich L, Dimitrov Stanchev L, Kutsch M, Roux A, Günther Pomorski T, Herrmann C (2021) Structural requirements for membrane binding of human guanylate-binding protein 1. FEBS J 288(13):4098–4114. https://doi.org/10.1111/febs.15703CrossRefPubMed

Sistemich L, Kutsch M, Hämisch B, Zhang P, Shydlovskyi S, Britzen-Laurent N et al (2020) The molecular mechanism of polymer formation of farnesylated human guanylate-binding protein 1. J Mol Biol 432(7):2164–2185. https://doi.org/10.1016/j.jmb.2020.02.009CrossRefPubMed

10.

Ji C, Du S, Li P, Zhu Q, Yang X, Long C et al (2019) Structural mechanism for guanylate-binding proteins (GBPs) targeting by the Shigella E3 ligase IpaH9.8. Plos Pathog 15(6):e1007876. https://doi.org/10.1371/journal.ppat.1007876CrossRefPubMedPubMedCentral

11.

Tripal P, Bauer M, Naschberger E, Mörtinger T, Hohenadl C, Cornali E et al (2007) Unique features of different members of the human guanylate-binding protein family. J Interferon Cytokine Res 27(1):44–52. https://doi.org/10.1089/jir.2007.0086CrossRefPubMed

12.

Braun E, Hotter D, Koepke L, Zech F, Groß R, Sparrer KMJ et al (2019) Guanylate-binding proteins 2 and 5 exert broad antiviral activity by inhibiting furin-mediated processing of viral envelope proteins. Cell Rep 27(7):2092–104.e10. https://doi.org/10.1016/j.celrep.2019.04.063CrossRefPubMed

13.

Tretina K, Park E-S, Maminska A, MacMicking JD (2019) Interferon-induced guanylate-binding proteins: guardians of host defense in health and disease. J Exp Med 216(3):482–500CrossRefPubMedPubMedCentral

14.

Kutsch M, Coers J (2020) Human guanylate binding proteins: nanomachines orchestrating host defense. FEBS J. https://doi.org/10.1111/febs.15662CrossRefPubMed

15.

Zhang R, Li Z, Tang Y-D, Su C, Zheng C (2021) When human guanylate-binding proteins meet viral infections. J Biomed Sci 28(1):17. https://doi.org/10.1186/s12929-021-00716-8CrossRefPubMedPubMedCentral

16.

Côrte-Real JV, Baldauf H-M, Melo-Ferreira J, Abrantes J, Esteves PJ (2022) Evolution of guanylate binding protein (GBP) genes in muroid rodents (Muridae and Cricetidae) reveals an outstanding pattern of gain and loss. Front Immunol. https://doi.org/10.3389/fimmu.2022.752186CrossRefPubMedPubMedCentral

17.

Côrte-Real JV, Baldauf HM, Abrantes J, Esteves PJ (2021) Evolution of the guanylate binding protein (GBP) genes: emergence of GBP7 genes in primates and further acquisition of a unique GBP3 gene in simians. Mol Immunol 132:79–81. https://doi.org/10.1016/j.molimm.2021.01.025 (Epub 2021/02/08)CrossRefPubMed

18.

Huang S, Meng Q, Maminska A, MacMicking JD (2019) Cell-autonomous immunity by IFN-induced GBPs in animals and plants. Curr Opin Immunol 60:71–80. https://doi.org/10.1016/j.coi.2019.04.017 (Epub 2019/06/09)CrossRefPubMedPubMedCentral

19.

Olszewski MA, Gray J, Vestal DJ (2006) In silico genomic analysis of the human and murine guanylate-binding protein (GBP) gene clusters. J Interferon Cytokine Res 26(5):328–352. https://doi.org/10.1089/jir.2006.26.328 (Epub 2006/05/13)CrossRefPubMed

20.

Li G, Zhang J, Sun Y, Wang H, Wang Y (2009) The evolutionarily dynamic IFN-inducible GTPase proteins play conserved immune functions in vertebrates and cephalochordates. Mol Biol Evol 26(7):1619–1630. https://doi.org/10.1093/molbev/msp074 (Epub 2009/04/17)CrossRefPubMed

21.

Nei M, Gu X, Sitnikova T (1997) Evolution by the birth-and-death process in multigene families of the vertebrate immune system. Proc Natl Acad Sci 94(15):7799–7806. https://doi.org/10.1073/pnas.94.15.7799CrossRefPubMedPubMedCentral

22.

Nei M, Rooney AP (2005) Concerted and birth-and-death evolution of multigene families. Annu Rev Genet 39:121–152. https://doi.org/10.1146/annurev.genet.39.073003.112240CrossRefPubMedPubMedCentral

23.

Wandel MP, Kim B-H, Park E-S, Boyle KB, Nayak K, Lagrange B et al (2020) Guanylate-binding proteins convert cytosolic bacteria into caspase-4 signaling platforms. Nat Immunol. https://doi.org/10.1038/s41590-020-0697-2CrossRefPubMedPubMedCentral

24.

Meunier E, Wallet P, Dreier RF, Costanzo S, Anton L, Rühl S et al (2015) Guanylate-binding proteins promote activation of the AIM2 inflammasome during infection with Francisella novicida. Nat Immunol 16(5):476–484. https://doi.org/10.1038/ni.3119 (Epub 2015/03/17)CrossRefPubMedPubMedCentral

25.

Shenoy AR, Wellington DA, Kumar P, Kassa H, Booth CJ, Cresswell P et al (2012) GBP5 promotes NLRP3 inflammasome assembly and immunity in mammals. Science 336(6080):481–485. https://doi.org/10.1126/science.1217141 (Epub 2012/03/31)CrossRefPubMed

26.

Feng M, Zhang Q, Wu W, Chen L, Gu S, Ye Y et al (2021) Inducible guanylate-binding protein 7 facilitates influenza A virus replication by suppressing innate immunity via NF-κB and JAK-STAT signaling pathways. J Virol 95(6):e02038-e2120. https://doi.org/10.1128/JVI.02038-20CrossRefPubMedPubMedCentral

27.

Bentham AR, De la Concepcion JC, Mukhi N, Zdrzałek R, Draeger M, Gorenkin D et al (2020) A molecular roadmap to the plant immune system. J Biol Chem 295(44):14916–14935. https://doi.org/10.1074/jbc.REV120.010852 (Epub 2020/08/21)CrossRefPubMedPubMedCentral

28.

Dangl JL, Horvath DM, Staskawicz BJ (2013) Pivoting the plant immune system from dissection to deployment. Science 341(6147):746–751. https://doi.org/10.1126/science.1236011 (Epub 2013/08/21)CrossRefPubMed

29.

Musseau C, Jorly J, Gadin S, Sørensen I, Deborde C, Bernillon S et al (2020) The tomato guanylate-binding protein SlGBP1 enables fruit tissue differentiation by maintaining endopolyploid cells in a non-proliferative state. Plant Cell 32(10):3188–3205. https://doi.org/10.1105/tpc.20.00245CrossRefPubMedPubMedCentral

30.

Murphy AM, Zhou T, Carr JP (2020) An update on salicylic acid biosynthesis, its induction and potential exploitation by plant viruses. Curr Opin Virol 42:8–17. https://doi.org/10.1016/j.coviro.2020.02.008 (Epub 2020/04/25)CrossRefPubMed

31.

Dong Z, Zheng N, Hu C, Huang X, Chen P, Wu Q et al (2021) Genetic bioengineering of overexpressed guanylate binding protein family BmAtlastin-n enhances silkworm resistance to Nosema bombycis. Int J Biol Macromol 172:223–230. https://doi.org/10.1016/j.ijbiomac.2021.01.021 (Epub 2021/01/17)CrossRefPubMed

32.

Liu T-h, Dong X-l, Pan C-x, Du G-y, Wu Y-f, Yang J-g et al (2016) A newly discovered member of the Atlastin family, BmAtlastin-n, has an antiviral effect against BmNPV in Bombyx mori. Sci Rep 6(1):28946. https://doi.org/10.1038/srep28946CrossRefPubMedPubMedCentral

33.

Robertsen B, Zou J, Secombes C, Leong J-A (2006) Molecular and expression analysis of an interferon-gamma-inducible guanylate-binding protein from rainbow trout (Oncorhynchus mykiss). Dev Comp Immunol 30(11):1023–1033. https://doi.org/10.1016/j.dci.2006.01.003CrossRefPubMed

34.

Cheng YS, Colonno RJ, Yin FH (1983) Interferon induction of fibroblast proteins with guanylate binding activity. J Biol Chem 258(12):7746–7750 (Epub 1983/06/25)CrossRefPubMed

35.

Tyrkalska SD, Candel S, Angosto D, Gómez-Abellán V, Martín-Sánchez F, García-Moreno D et al (2016) Neutrophils mediate Salmonella Typhimurium clearance through the GBP4 inflammasome-dependent production of prostaglandins. Nat Commun 7:12077. https://doi.org/10.1038/ncomms12077 (Epub 2016/07/02)CrossRefPubMedPubMedCentral

36.

Jin T, Huang M, Smith P, Jiang J, Xiao TS (2013) Structure of the caspase-recruitment domain from a zebrafish guanylate-binding protein. Acta Crystallogr Sect F Struct Biol Cryst Commun 69(Pt 8):855–860. https://doi.org/10.1107/S1744309113015558 (Epub 2013/07/27)CrossRefPubMedPubMedCentral

37.

Valera-Pérez A, Tyrkalska SD, Viana C, Rojas-Fernández A, Pelegrín P, García-Moreno D et al (2019) WDR90 is a new component of the NLRC4 inflammasome involved in Salmonella Typhimurium resistance. Dev Comp Immunol 100:103428. https://doi.org/10.1016/j.dci.2019.103428CrossRefPubMed

38.

Zou Z, Meng Z, Ma C, Liang D, Sun R, Lan K (2017) Guanylate-binding protein 1 inhibits nuclear delivery of Kaposi’s sarcoma-associated herpesvirus virions by disrupting formation of actin filament. J Virol 91(16):e00632-e717CrossRefPubMedPubMedCentral

39.

Glitscher M, Himmelsbach K, Woytinek K, Schollmeier A, Johne R, Praefcke GJK et al (2021) Identification of the interferon-inducible GTPase GBP1 as major restriction factor for the hepatitis E virus. J Virol. https://doi.org/10.1128/jvi.01564-20 (Epub 2021/01/22)CrossRefPubMedPubMedCentral

40.

Itsui Y, Sakamoto N, Kakinuma S, Nakagawa M, Sekine-Osajima Y, Tasaka-Fujita M et al (2009) Antiviral effects of the interferon-induced protein guanylate binding protein 1 and its interaction with the hepatitis C virus NS5B protein. Hepatology 50(6):1727–1737. https://doi.org/10.1002/hep.23195CrossRefPubMed

41.

Zhu Z, Shi Z, Yan W, Wei J, Shao D, Deng X et al (2013) Nonstructural protein 1 of influenza A virus interacts with human guanylate-binding protein 1 to antagonize antiviral activity. PLoS One 8(2):e55920. https://doi.org/10.1371/journal.pone.0055920 (Epub 2013/02/14)CrossRefPubMedPubMedCentral

42.

Anderson SL, Carton JM, Lou J, Xing L, Rubin BY (1999) Interferon-induced guanylate binding protein-1 (GBP-1) mediates an antiviral effect against vesicular stomatitis virus and encephalomyocarditis virus. Virology 256(1):8–14. https://doi.org/10.1006/viro.1999.9614 (Epub 1999/03/24)CrossRefPubMed

43.

Pan W, Zuo X, Feng T, Shi X, Dai J (2012) Guanylate-binding protein 1 participates in cellular antiviral response to dengue virus. Virol J 9:292. https://doi.org/10.1186/1743-422x-9-292 (Epub 2012/11/29)CrossRefPubMedPubMedCentral

44.

Nordmann A, Wixler L, Boergeling Y, Wixler V, Ludwig S (2012) A new splice variant of the human guanylate-binding protein 3 mediates anti-influenza activity through inhibition of viral transcription and replication. FASEB J 26(3):1290–1300. https://doi.org/10.1096/fj.11-189886CrossRefPubMed

45.

Krapp C, Hotter D, Gawanbacht A, McLaren Paul J, Kluge Silvia F, Stürzel Christina M et al (2016) Guanylate binding protein (GBP) 5 is an interferon-inducible inhibitor of HIV-1 infectivity. Cell Host Microbe 19(4):504–514. https://doi.org/10.1016/j.chom.2016.02.019CrossRefPubMed

46.

Srinivasachar Badarinarayan S, Shcherbakova I, Langer S, Koepke L, Preising A, Hotter D et al (2020) HIV-1 infection activates endogenous retroviral promoters regulating antiviral gene expression. Nucleic Acids Res 48(19):10890–10908. https://doi.org/10.1093/nar/gkaa832CrossRefPubMedPubMedCentral

47.

Li Z, Qu X, Liu X, Huan C, Wang H, Zhao Z et al (2020) GBP5 is an interferon-induced inhibitor of respiratory syncytial virus. J Virol 94(21):e01407-e1420. https://doi.org/10.1128/JVI.01407-20CrossRefPubMedPubMedCentral

48.

Feng J, Cao Z, Wang L, Wan Y, Peng N, Wang Q et al (2017) Inducible GBP5 mediates the antiviral response via interferon-related pathways during influenza A virus infection. J Innate Immun 9(4):419–435CrossRefPubMedPubMedCentral

49.

Ma G, Huang J, Sun N, Liu X, Zhu M, Wu Z et al (2008) Molecular characterization of the porcine GBP1 and GBP2 genes. Mol Immunol 45(10):2797–2807. https://doi.org/10.1016/j.molimm.2008.02.007CrossRefPubMed

50.

Li LF, Yu J, Li Y, Wang J, Li S, Zhang L et al (2016) Guanylate-binding protein 1, an interferon-induced GTPase, exerts an antiviral activity against classical swine fever virus depending on its GTPase activity. J Virol 90(9):4412–4426. https://doi.org/10.1128/JVI.02718-15 (Epub 20160414)CrossRefPubMedPubMedCentral

51.

Kommadath A, Bao H, Choi I, Reecy JM, Koltes JE, Fritz-Waters E et al (2017) Genetic architecture of gene expression underlying variation in host response to porcine reproductive and respiratory syndrome virus infection. Sci Rep 7:46203. https://doi.org/10.1038/srep46203 (Epub 20170410)CrossRefPubMedPubMedCentral

52.

Khatun A, Nazki S, Jeong CG, Gu S, Mattoo SUS, Lee SI et al (2020) Effect of polymorphisms in porcine guanylate-binding proteins on host resistance to PRRSV infection in experimentally challenged pigs. Vet Res 51(1):14. https://doi.org/10.1186/s13567-020-00745-5 (Epub 20200219)CrossRefPubMedPubMedCentral

53.

Koltes JE, Fritz-Waters E, Eisley CJ, Choi I, Bao H, Kommadath A et al (2015) Identification of a putative quantitative trait nucleotide in guanylate binding protein 5 for host response to PRRS virus infection. BMC Genom 16:412. https://doi.org/10.1186/s12864-015-1635-9 (Epub 20150528)CrossRef

54.

Gol S, Estany J, Fraile LJ, Pena RN (2015) Expression profiling of the GBP1 gene as a candidate gene for porcine reproductive and respiratory syndrome resistance. Anim Genet 46(6):599–606. https://doi.org/10.1111/age.12347 (Epub 20150911)CrossRefPubMed

55.

Gu T, Yu D, Fan Y, Wu Y, Yao YL, Xu L et al (2019) Molecular identification and antiviral function of the guanylate-binding protein (GBP) genes in the Chinese tree shrew (Tupaia belangeri chinesis). Dev Comp Immunol 96:27–36. https://doi.org/10.1016/j.dci.2019.02.014 (Epub 2019/03/01)CrossRefPubMed

56.

Wehner M, Herrmann C (2010) Biochemical properties of the human guanylate binding protein 5 and a tumor-specific truncated splice variant. FEBS J 277(7):1597–1605. https://doi.org/10.1111/j.1742-4658.2010.07586.x (Epub 2010/02/26)CrossRefPubMed

57.

Nantais DE, Schwemmle M, Stickney JT, Vestal DJ, Buss JE (1996) Prenylation of an interferon-gamma-induced GTP-binding protein: the human guanylate binding protein, huGBP1. J Leukoc Biol 60(3):423–431. https://doi.org/10.1002/jlb.60.3.423 (Epub 1996/09/01)CrossRefPubMed

58.

Modiano N, Lu YE, Cresswell P (2005) Golgi targeting of human guanylate-binding protein-1 requires nucleotide binding, isoprenylation, and an IFN-gamma-inducible cofactor. Proc Natl Acad Sci USA 102(24):8680–8685. https://doi.org/10.1073/pnas.0503227102 (Epub 2005/06/03)CrossRefPubMedPubMedCentral

59.

Ngo CC, Man SM (2017) Mechanisms and functions of guanylate-binding proteins and related interferon-inducible GTPases: roles in intracellular lysis of pathogens. Cell Microbiol 19(12):e12791. https://doi.org/10.1111/cmi.12791CrossRef

60.

Santos JC, Broz P (2018) Sensing of invading pathogens by GBPs: at the crossroads between cell-autonomous and innate immunity. J Leukoc Biol 104(4):729–735. https://doi.org/10.1002/jlb.4mr0118-038r (Epub 2018/07/19)CrossRefPubMed

61.

Mostafavi S, Yoshida H, Moodley D, LeBoité H, Rothamel K, Raj T et al (2016) Parsing the interferon transcriptional network and its disease associations. Cell 164(3):564–578. https://doi.org/10.1016/j.cell.2015.12.032 (Epub 2016/01/30)CrossRefPubMedPubMedCentral

62.

Degrandi D, Konermann C, Beuter-Gunia C, Kresse A, Würthner J, Kurig S et al (2007) Extensive characterization of IFN-induced GTPases mGBP1 to mGBP10 involved in host defense. J Immunol 179(11):7729–7740. https://doi.org/10.4049/jimmunol.179.11.7729CrossRefPubMed

63.

Kim BH, Shenoy AR, Kumar P, Das R, Tiwari S, MacMicking JD (2011) A family of IFN-γ-inducible 65-kD GTPases protects against bacterial infection. Science 332(6030):717–721. https://doi.org/10.1126/science.1201711CrossRefPubMed

64.

Gu T, Yu D, Xu L, Yao YL, Zheng X, Yao YG (2021) Tupaia guanylate-binding protein 1 interacts with vesicular stomatitis virus phosphoprotein and represses primary transcription of the viral genome. Cytokine 138:155388. https://doi.org/10.1016/j.cyto.2020.155388 (Epub 2020/12/04)CrossRefPubMed

65.

Gu T, Yu D, Xu L, Yao Y-L, Yao Y-G (2021) Tupaia GBP1 interacts with STING to initiate autophagy and restrict herpes simplex virus type 1 infection. J Immunol 207(11):2673. https://doi.org/10.4049/jimmunol.2100325CrossRefPubMed

66.

Li R, Zanin M, Xia X, Yang Z (2018) The tree shrew as a model for infectious diseases research. J Thorac Dis 10(Suppl 19):S2272–S2279. https://doi.org/10.21037/jtd.2017.12.121 (Epub 2018/08/18)CrossRefPubMedPubMedCentral

67.

Xu L, Yu DD, Ma YH, Yao YL, Luo RH, Feng XL et al (2020) COVID-19-like symptoms observed in Chinese tree shrews infected with SARS-CoV-2. Zool Res 41(5):517–526. https://doi.org/10.24272/j.issn.2095-8137.2020.053 (Epub 2020/07/24)CrossRefPubMedPubMedCentral

68.

Carter CC, Gorbacheva VY, Vestal DJ (2005) Inhibition of VSV and EMCV replication by the interferon-induced GTPase, mGBP-2: differential requirement for wild-type GTP binding domain. Arch Virol 150(6):1213–1220. https://doi.org/10.1007/s00705-004-0489-2 (Epub 2005/02/18)CrossRefPubMed

69.

Yu P, Li Y, Li Y, Miao Z, Peppelenbosch MP, Pan Q (2020) Guanylate-binding protein 2 orchestrates innate immune responses against murine norovirus and is antagonized by the viral protein NS7. J Biol Chem 295(23):8036–8047. https://doi.org/10.1074/jbc.RA120.013544 (Epub 2020/04/30)CrossRefPubMedPubMedCentral

70.

Degrandi D, Kravets E, Konermann C, Beuter-Gunia C, Klümpers V, Lahme S et al (2013) Murine guanylate binding protein 2 (mGBP2) controls Toxoplasma gondii replication. Proc Natl Acad Sci USA 110(1):294–299. https://doi.org/10.1073/pnas.1205635110 (Epub 2012/12/19)CrossRefPubMed

71.

Cerqueira DM, Gomes MTR, Silva ALN, Rungue M, Assis NRG, Guimarães ES et al (2018) Guanylate-binding protein 5 licenses caspase-11 for Gasdermin-D mediated host resistance to Brucella abortus infection. PLoS Pathog 14(12):e1007519-e. https://doi.org/10.1371/journal.ppat.1007519CrossRef

72.

Corsetti PP, de Almeida LA, Gonçalves ANA, Gomes MTR, Guimarães ES, Marques JT et al (2018) miR-181a-5p regulates TNF-α and miR-21a-5p influences gualynate-binding protein 5 and IL-10 expression in macrophages affecting host control of Brucella abortus infection. Front Immunol 9:1331. https://doi.org/10.3389/fimmu.2018.01331 (Epub 2018/06/27)CrossRefPubMedPubMedCentral

73.

Man SM, Karki R, Malireddi RK, Neale G, Vogel P, Yamamoto M et al (2015) The transcription factor IRF1 and guanylate-binding proteins target activation of the AIM2 inflammasome by Francisella infection. Nat Immunol 16(5):467–475. https://doi.org/10.1038/ni.3118 (Epub 2015/03/17)CrossRefPubMedPubMedCentral

74.

Place DE, Malireddi RKS, Kim J, Vogel P, Yamamoto M, Kanneganti T-D (2021) Osteoclast fusion and bone loss are restricted by interferon inducible guanylate binding proteins. Nat Commun 12(1):496. https://doi.org/10.1038/s41467-020-20807-8CrossRefPubMedPubMedCentral

75.

Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H et al (2000) The protein data bank. Nucleic Acids Res 28(1):235–242. https://doi.org/10.1093/nar/28.1.235 (Epub 1999/12/11)CrossRefPubMedPubMedCentral

76.

Sehnal D, Bittrich S, Deshpande M, Svobodová R, Berka K, Bazgier V et al (2021) Mol* Viewer: modern web app for 3D visualization and analysis of large biomolecular structures. Nucleic Acids Res 49(W1):W431–W437. https://doi.org/10.1093/nar/gkab314CrossRefPubMedPubMedCentral

Title: Functional cross-species conservation of guanylate-binding proteins in innate immunity
Authors: Luca Schelle
João Vasco Côrte-Real
Pedro José Esteves
Joana Abrantes
Hanna-Mari Baldauf
Publication date: 13-04-2022
Publisher: Springer Berlin Heidelberg
Keywords: Interferon
Listeria Monocytogenes
Published in: Medical Microbiology and Immunology / Issue 2/2023
Print ISSN: 0300-8584
Electronic ISSN: 1432-1831
DOI: https://doi.org/10.1007/s00430-022-00736-7

Live Webinar | 27-06-2024 | 18:00 (CEST)

Keynote webinar | Spotlight on medication adherence

Reserve your place

Live: Thursday 27th June 2024, 18:00-19:30 (CEST)

WHO estimates that half of all patients worldwide are non-adherent to their prescribed medication. The consequences of poor adherence can be catastrophic, on both the individual and population level.

Join our expert panel to discover why you need to understand the drivers of non-adherence in your patients, and how you can optimize medication adherence in your clinics to drastically improve patient outcomes.

Prof. Kevin Dolgin

Prof. Florian Limbourg

Prof. Anoop Chauhan

Developed by: Springer Medicine

Obesity Clinical Trial Summary

At a glance: The STEP trials

A round-up of the STEP phase 3 clinical trials evaluating semaglutide for weight loss in people with overweight or obesity.

Developed by: Springer Medicine

Keynote webinar | Spotlight on medication adherence

Springer Medicine

Abstract

Please log in to get access to this content

Other articles of this Issue 2/2023

Immune complexes as culprits of immunopathology in severe COVID-19

Mouse models in COVID-19 research: analyzing the adaptive immune response

HIV-1 restriction by SERINC5

Editorial on special issue on “Immunobiology of Viral Infections”

Interferon antagonists encoded by SARS-CoV-2 at a glance

Cytomegalovirus immune evasion sets the functional avidity threshold for protection by CD8 T cells

Keynote webinar | Spotlight on medication adherence

Live: Thursday 27th June 2024, 18:00-19:30 (CEST)

At a glance: The STEP trials