Chemokines and nanomaterials: interaction for useful immune-applications

Giuseppe Bardi

Exploration of Immunology ›› 2022, Vol. 2 ›› Issue (4) : 637 -647.

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Exploration of Immunology ›› 2022, Vol. 2 ›› Issue (4) :637 -647. DOI: 10.37349/ei.2022.00073
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Chemokines and nanomaterials: interaction for useful immune-applications
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Abstract

Chemokines are homeostatic or inflammatory small proteins regulating immune cell migration and are structurally characterized by cysteine disulfide bridges. Around 50 human chemokines binding almost 20 seven-transmembrane G-protein coupled receptors have been discovered. The finding that two of them were the main human immunodeficiency virus (HIV) co-receptors intensified the research on the binding mechanism to block the viral entrance. Blockade of chemokine/chemokine receptor signaling ultimately modulates cell migration, then immune responses. Particular nanotechnologies can be designed to interfere with chemokine signaling or to exploit the ligand-receptor interaction. Surface chemical modification of nanomaterials with chemokines or specific peptides can find several applications in bio-medicine, from tissue-specific drug delivery to reduced cell migration in pathological conditions. Recent highlights on peculiar chemokine-nanoparticle design and their potential to modulate immune responses will be discussed.

Keywords

Chemokines / nanoparticles / inflammation / chemokine receptors / protein corona

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Giuseppe Bardi. Chemokines and nanomaterials: interaction for useful immune-applications. Exploration of Immunology, 2022, 2 (4) : 637-647 DOI:10.37349/ei.2022.00073

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References

[1]

Baggiolini M. CXCL8-the first chemokine. Front Immunol. 2015; 6: 285.

[2]

Hughes CE, Nibbs RJB. A guide to chemokines and their receptors. FEBS J. 2018; 285: 2944-71.

[3]

Miller MC, Mayo KH. Chemokines from a structural perspective. Int J Mol Sci. 2017; 18: 2088.

[4]

Arimont M, Sun SL, Leurs R, Smit M, De Esch IJP, De Graaf C. Structural analysis of chemokine receptor-ligand interactions. J Med Chem. 2017; 60: 4735-79.

[5]

Kufareva I, Salanga CL, Handel TM. Chemokine and chemokine receptor structure and interactions: implications for therapeutic strategies. Immunol Cell Biol. 2015; 93: 372-83.

[6]

Crump MP, Gong JH, Loetscher P, Rajarathnam K, Amara A, Arenzana-Seisdedos F, et al. Solution structure and basis for functional activity of stromal cell-derived factor-1; dissociation of CXCR4 activation from binding and inhibition of HIV-1. EMBO J. 1997; 16: 6996-7007.

[7]

Laudanna C, Alon R. Right on the spot. Chemokine triggering of integrin-mediated arrest of rolling leukocytes. Thromb Haemost. 2006; 95: 5-11.

[8]

Künze G, Huster D, Samsonov SA. Investigation of the structure of regulatory proteins interacting with glycosaminoglycans by combining NMR spectroscopy and molecular modeling-the beginning of a wonderful friendship. Biol Chem. 2021; 402: 1337-55.

[9]

Hyduk SJ, Cybulsky MI. Role of α4β1 integrins in chemokine-induced monocyte arrest under conditions of shear stress. Microcirculation. 2009; 16: 17-30.

[10]

Tanaka Y. Integrin activation by chemokines: relevance to inflammatory adhesion cascade during T cell migration. Histol Histopathol. 2000; 15: 1169-76.

[11]

Beisser PS, Lavreysen H, Bruggeman CA, Vink C. Chemokines and chemokine receptors encoded by cytomegaloviruses. Curr Top Microbiol Immunol. 2008; 325: 221-42.

[12]

Pontejo SM, Murphy PM, Pease JE. Chemokine subversion by human herpesviruses. J Innate Immun. 2018; 10: 465-78.

[13]

Pontejo SM, Murphy PM. Chemokines encoded by herpesviruses. J Leukoc Biol. 2017; 102: 1199-217.

[14]

Berson JF, Long D, Doranz BJ, Rucker J, Jirik FR, Doms RW. A seven-transmembrane domain receptor involved in fusion and entry of T-cell-tropic human immunodeficiency virus type 1 strains. J Virol. 1996; 70: 6288-95.

[15]

Alkhatib G, Combadiere C, Broder CC, Feng Y, Kennedy PE, Murphy PM, et al. CC CKR5: a RANTES, MIP-1α, MIP-1β receptor as a fusion cofactor for macrophage-tropic HIV-1. Science. 1996; 272: 1955-8.

[16]

Feng Y, Broder CC, Kennedy PE, Berger EA. HIV-1 entry cofactor: functional cDNA cloning of a seven-transmembrane, G protein-coupled receptor. Science. 1996; 272: 872-7.

[17]

Bleul CC, Farzan M, Choe H, Parolin C, Clark-Lewis I, Sodroski J, et al. The lymphocyte chemoattractant SDF-1 is a ligand for LESTR/fusin and blocks HIV-1 entry. Nature. 1996; 382: 829-33.

[18]

Oberlin E, Amara A, Bachelerie F, Bessia C, Virelizier JL, Arenzana-Seisdedos F, et al. The CXC chemokine SDF-1 is the ligand for LESTR/fusin and prevents infection by T-cell-line-adapted HIV-1. Nature. 1996; 382: 833-5.

[19]

Broder CC, Dimitrov DS. HIV and the 7-transmembrane domain receptors. Pathobiology. 1996; 64: 171-9.

[20]

Lin G, Baribaud F, Romano J, Doms RW, Hoxie JA. Identification of gp120 binding sites on CXCR4 by using CD4-independent human immunodeficiency virus type 2 Env proteins. J Virol. 2003; 77: 931-42.

[21]

Shaik MM, Peng H, Lu J, Rits-Volloch S, Xu C, Liao M, et al. Structural basis of coreceptor recognition by HIV-1 envelope spike. Nature. 2019; 565: 318-23.

[22]

Bardi G, Sengupta R, Khan MZ, Patel JP, Meucci O. Human immunodeficiency virus gp120-induced apoptosis of human neuroblastoma cells in the absence of CXCR4 internalization. J Neurovirol. 2006; 12: 211-8.

[23]

Smith LK, Babcock IW, Minamide LS, Shaw AE, Bamburg JR, Kuhn TB. Direct interaction of HIV gp120 with neuronal CXCR4 and CCR5 receptors induces cofilin-actin rod pathology via a cellular prion protein- and NOX-dependent mechanism. PLoS One. 2021; 16: e0248309.

[24]

Murakami T, Zhang TY, Koyanagi Y, Tanaka Y, Kim J, Suzuki Y, et al. Inhibitory mechanism of the CXCR4 antagonist T22 against human immunodeficiency virus type 1 infection. J Virol. 1999; 73: 7489-96.

[25]

Kraus S, Kolman T, Yeung A, Deming D. Chemokine receptor antagonists: role in oncology. Curr Oncol Rep. 2021; 23: 131.

[26]

Xiao T, Cai Y, Chen B. HIV-1 entry and membrane fusion inhibitors. Viruses. 2021; 13: 735.

[27]

Lai WY, Mueller A. Latest update on chemokine receptors as therapeutic targets. Biochem Soc Trans. 2021; 49: 1385-95.

[28]

Yang M, Wu E, Tang W, Qian J, Zhan C. Interplay between nanomedicine and protein corona. J Mater Chem B. 2021; 9: 6713-27.

[29]

Kopac T. Protein corona, understanding the nanoparticle-protein interactions and future perspectives: a critical review. Int J Biol Macromol. 2021; 169: 290-301.

[30]

Caracciolo G, Farokhzad OC, Mahmoudi M. Biological identity of nanoparticles in vivo: clinical implications of the protein corona . Trends Biotechnol. 2017; 35: 257-64.

[31]

Fasoli E. Protein corona: Dr. Jekyll and Mr. Hyde of nanomedicine. Biotechnol Appl Biochem. 2021; 68: 1139-52.

[32]

Li H, Wang Y, Tang Q, Yin D, Tang C, He E, et al. The protein corona and its effects on nanoparticle-based drug delivery systems. Acta Biomater. 2021; 129: 57-72.

[33]

Cagliani R, Gatto F, Bardi G. Protein adsorption: a feasible method for nanoparticle functionalization? Materials (Basel). 2019; 12: 1991.

[34]

Digiacomo L, Pozzi D, Palchetti S, Zingoni A, Caracciolo G. Impact of the protein corona on nanomaterial immune response and targeting ability. Wiley Interdiscip Rev Nanomed Nanobiotechnol. 2020; 12: e1615.

[35]

Batt J, Milward M, Chapple I, Grant M, Roberts H, Addison O. TiO2 nanoparticles can selectively bind CXCL8 impacting on neutrophil chemotaxis . Eur Cells Mater. 2018; 35: 13-24.

[36]

Jafari S, Mahyad B, Hashemzadeh H, Janfaza S, Gholikhani T, Tayebi L. Biomedical applications of TiO2 nanostructures: recent advances . Int J Nanomedicine. 2020; 15: 3447-70.

[37]

Zheng Y, Pescatore N, Gogotsi Y, Dyatkin B, Ingavle G, Mochalin V, et al. Rapid adsorption of proinflammatory cytokines by graphene nanoplatelets and their composites for extracorporeal detoxification. J Nanomater. 2018: 2018: 6274072.

[38]

Bruce L, Lyngstadaas SP, inventor; Prophy Med AB, assignee. Selective chemokine modulation. United States patent US 8784845B2. 2014 Jul 22.

[39]

Pisani A, Pompa PP, Bardi G. Potential applications of nanomaterials to quench the cytokine storm in coronavirus disease 19. Front Bioeng Biotechnol. 2020; 8: 906.

[40]

Kocbach A, Totlandsdal AI, Låg M, Refsnes M, Schwarze PE. Differential binding of cytokines to environmentally relevant particles: a possible source for misinterpretation of in vitro results? Toxicol Lett. 2008; 176: 131-7.

[41]

Li S, Pettersson US, Hoorelbeke B, Kolaczkowska E, Schelfhout K, Martens E, et al. Interference with glycosaminoglycan-ghemokine interactions with a probe to alter leukocyte recruitment and inflammation in vivo . PLoS One. 2014; 9: e104107.

[42]

Guryanov I, Cipriani S, Fiorucci S, Zashikhina N, Marchianò S, Scarpelli P, et al. Nanotraps with biomimetic surface as decoys for chemokines. Nanomedicine. 2017; 13: 2575-85.

[43]

Pisani A, Bardi G. Immunology of biodegradable nanoparticles: a brief overview on a wide growing field. Explor Immunol. 2021; 1: 48-60.

[44]

Gatto F, Bardi G. Metallic nanoparticles: general research approaches to immunological characterization. Nanomaterials (Basel). 2018; 8: 753.

[45]

Ramadi KB, Mohamed YA, Al-Sbiei A, Almarzooqi S, Bashir G, Al Dhanhani A, et al. Acute systemic exposure to silver-based nanoparticles induces hepatotoxicity and NLRP3-dependent inflammation. Nanotoxicology. 2016; 10: 1061-74.

[46]

Wu QH, Jin RR, Feng T, Liu L, Yang L, Tao YH, et al. Iron oxide nanoparticles and induced autophagy in human monocytes. Int J Nanomedicine. 2017; 12: 3993-4005.

[47]

Petrick L, Rosenblat M, Paland N, Aviram M. Silicon dioxide nanoparticles increase macrophage atherogenicity: stimulation of cellular cytotoxicity, oxidative stress, and triglycerides accumulation. Environ Toxicol. 2016; 31: 713-23.

[48]

Paino IMM, Zucolotto V. Poly (vinyl alcohol)-coated silver nanoparticles: activation of neutrophils and nanotoxicology effects in human hepatocarcinoma and mononuclear cells. Environ Toxicol Pharmacol. 2015; 39: 614-21.

[49]

Abdelhalim MAK, Jarrar BM. Histological alterations in the liver of rats induced by different gold nanoparticle sizes, doses and exposure duration. J Nanobiotechnology. 2012; 10: 5.

[50]

Blanpain C, Libert F, Vassart G, Parmentier M. CCR5 and HIV infection. Recept Channels. 2002; 8: 19-31.

[51]

De Silva E, Stumpf MPH. HIV and the CCR5-Delta32 resistance allele. FEMS Microbiol Lett. 2004; 241: 1-12.

[52]

Hütter G, Bodor J, Ledger S, Boyd M, Millington M, Tsie M, et al. CCR5 targeted cell therapy for HIV and prevention of viral escape. Viruses. 2015; 7: 4186-203.

[53]

Barmania F, Pepper MS. C-C chemokine receptor type five (CCR5): an emerging target for the control of HIV infection. Appl Transl Genom. 2013; 2: 3-16.

[54]

Proudfoot AEI, Power CA, Schwarz MK. Anti-chemokine small molecule drugs: a promising future? Expert Opin Investig Drugs. 2010; 19: 345-55.

[55]

Griffith JW, Sokol CL, Luster AD . Chemokines and chemokine receptors: positioning cells for host defense and immunity. Annu Rev Immunol. 2014; 32: 659-702.

[56]

Wang Y, Xie Y, Oupický D. Potential of CXCR4/CXCL12 chemokine axis in cancer drug delivery. Curr Pharmacol Rep. 2016; 2: 1-10.

[57]

Ratajczak MZ, Zuba-Surma E, Kucia M, Reca R, Wojakowski W, Ratajczak J. The pleiotropic effects of the SDF-1-CXCR4 axis in organogenesis, regeneration and tumorigenesis. Leukemia. 2006; 20: 1915-24.

[58]

Teicher BA, Fricker SP. CXCL12 (SDF-1)/CXCR4 pathway in cancer. Clin Cancer Res. 2010; 16: 2927-31.

[59]

Unzueta U, Céspedes MV, Ferrer-Miralles N, Casanova I, Cedano J, Corchero JL, et al. Intracellular CXCR4+ cell targeting with T22-empowered protein-only nanoparticles . Int J Nanomedicine. 2012; 7: 4533-44.

[60]

de la Torre C, Casanova I, Acosta G, Coll C, Moreno MJ, Albericio F, et al. Gated mesoporous silica nanoparticles using a double-role circular peptide for the controlled and target-preferential release of doxorubicin in CXCR4-expresing lymphoma cells. Adv Funct Mater. 2015; 25: 687-95.

[61]

Díƴaz R, Pallarès V, Cano-Garrido O, Serna N, Sánchez-Garcíƴa L, Falgàs A, et al. Selective CXCR4+ cancer cell targeting and potent antineoplastic effect by a nanostructured version of recombinant ricin . Small. 2018; 14: e1800665.

[62]

Céspedes MV, Unzueta U, ÁƵ lamo P, Gallardo A, Sala R, Casanova I, et al. Cancer-specific uptake of a liganded protein nanocarrier targeting aggressive CXCR4+ colorectal cancer models . Nanomedicine. 2016; 12: 1987-96.

[63]

Falgàs A, Pallarès V, Unzueta U, Céspedes MV, Arroyo-Solera I, Moreno MJ, et al. A CXCR4-targeted nanocarrier achieves highly selective tumor uptake in diffuse large B-cell lymphoma mouse models. Haematologica. 2020; 105: 741-53.

[64]

Falgàs A, Pallarès V, Serna N, Sánchez-Garcíƴa L, Sierra J, Gallardo A, et al. Selective delivery of T22-PE24-H6 to CXCR4+ diffuse large B-cell lymphoma cells leads to wide therapeutic index in a disseminated mouse model . Theranostics. 2020; 10: 5169-80.

[65]

Pallarès V, Unzueta U, Falgàs A, Sánchez-Garciá L, Serna N, Gallardo A, et al. An Auristatin nanoconjugate targeting CXCR4+ leukemic cells blocks acute myeloid leukemia dissemination. J Hematol Oncol. 2020; 13: 36.

[66]

Rioja-Blanco E, Gallardo A, Arroyo-Solera I, ÁƵlamo P, Casanova I, Unzueta U, et al. A novel CXCR4-targeted diphtheria toxin nanoparticle inhibits invasion and metastatic dissemination in a head and neck squamous cell carcinoma mouse model. Pharmaceutics. 2022; 14: 887.

[67]

Sala R, Rioja-Blanco E, Serna N, Sánchez-Garcíƴa L, ÁƵ lamo P, Alba-Castellón L, et al. GSDMD-dependent pyroptotic induction by a multivalent CXCR4-targeted nanotoxin blocks colorectal cancer metastases. Drug Deliv. 2022; 29: 1384-97.

[68]

Pallarès V, Núñez Y, Sánchez-Garcíƴa L, Falgàs A, Serna N, Unzueta U, et al. Antineoplastic effect of a diphtheria toxin-based nanoparticle targeting acute myeloid leukemia cells overexpressing CXCR4. J Controlled Release. 2021; 335: 117-29.

[69]

Cano-Garrido O, ÁƵ lamo P, Sánchez-Garcíƴa L, Falgàs A, Sánchez-Chardi A, Serna N, et al. Biparatopic protein nanoparticles for the precision therapy of CXCR4+ cancers . Cancers (Basel). 2021; 13: 2929.

[70]

Falgàs A, Garcia-León A, Núñez Y, Serna N, Sánchez-Garcia L, Unzueta U, et al. A diphtheria toxin-based nanoparticle achieves specific cytotoxic effect on CXCR4+ lymphoma cells without toxicity in immunocompromised and immunocompetent mice . Biomed Pharmacother. 2022; 150: 112940.

[71]

Chittasupho C, Lirdprapamongkol K, Kewsuwan P, Sarisuta N. Targeted delivery of doxorubicin to A549 lung cancer cells by CXCR4 antagonist conjugated PLGA nanoparticles. Eur J pharm Biopharm. 2014; 88: 529-38.

[72]

Wang RT, Zhi XY, Yao SY, Zhang Y. LFC131 peptide-conjugated polymeric nanoparticles for the effective delivery of docetaxel in CXCR4 overexpressed lung cancer cells. Colloids Surf B Biointerfaces. 2015; 133: 43-50.

[73]

Zheng N, Liu W, Li B, Nie H, Liu J, Cheng Y, et al. Co-delivery of sorafenib and metapristone encapsulated by CXCR4-targeted PLGA-PEG nanoparticles overcomes hepatocellular carcinoma resistance to sorafenib. J Exp Clin Cancer Res. 2019; 38: 232.

[74]

Egorova A, Shubina A, Sokolov D, Selkov S, Baranov V, Kiselev A. CXCR4-targeted modular peptide carriers for efficient anti-VEGF siRNA delivery. Int J Pharm. 2016; 515: 431-40.

[75]

Egorova A, Kiselev A, Hakli M, Ruponen M, Baranov V, Urtti A. Chemokine-derived peptides as carriers for gene delivery to CXCR4 expressing cells. J Gene Med. 2009; 11: 772-81.

[76]

Lee IH, Palombo MS, Zhang X, Szekely Z, Sinko PJ. Design and evaluation of a CXCR4 targeting peptide 4DV3 as an HIV entry inhibitor and a ligand for targeted drug delivery. Eur J Pharm Biopharm. 2019; 138: 11-22.

[77]

Liu Y, Woodard PK. Chemokine receptors: key for molecular imaging of inflammation in atherosclerosis. J Nucl Cardiol. 2019; 26: 1179-81.

[78]

Detering L, Abdilla A, Luehmann HP, Williams JW, Huang LH, Sultan D, et al. CC chemokine receptor 5 targeted nanoparticles imaging the progression and regression of atherosclerosis using positron emission tomography/computed tomography. Mol Pharm. 2021; 18: 1386-96.

[79]

Luehmann HP, Pressly ED, Detering L, Wang C, Pierce R, Woodard PK, et al. PET/CT imaging of chemokine receptor CCR5 in vascular injury model using targeted nanoparticle. J Nucl Med. 2014; 55: 629-34.

[80]

Woodard PK, Liu Y, Pressly ED, Luehmann HP, Detering L, Sultan DE, et al. Design and modular construction of a polymeric nanoparticle for targeted atherosclerosis positron emission tomography imaging: a story of 25% (64)Cu-CANF-comb. Pharm Res. 2016; 33: 2400-10.

[81]

Wei L, Petryk J, Gaudet C, Kamkar M, Gan W, Duan Y, et al. Development of an inflammation imaging tracer,111In-DOTA-DAPTA, targeting chemokine receptor CCR5 and preliminary evaluation in an ApoE-/- atherosclerosis mouse model . J Nucl Cardiol. 2019; 26: 1169-78.

[82]

Gao DY, Lin TT, Sung YC, Liu YC, Chiang WH, Chang CC, et al. CXCR4-targeted lipid-coated PLGA nanoparticles deliver sorafenib and overcome acquired drug resistance in liver cancer. Biomaterials. 2015; 67: 194-203.

[83]

Liu JY, Chiang T, Liu CH, Chern GG, Lin TT, Gao DY, et al. Delivery of siRNA using CXCR4-targeted nanoparticles modulates tumor microenvironment and achieves a potent antitumor response in liver cancer. Mol Ther. 2015; 23: 1772-82.

[84]

Cashen AF, Nervi B, DiPersio J. AMD3100: CXCR4 antagonist and rapid stem cell-mobilizing agent. Future Oncol. 2007; 3: 19-27.

[85]

De Clercq E. Mozobil® (plerixafor, AMD3100), 10 years after its approval by the US Food and Drug Administration . Antivir Chem Chemother. 2019; 27: 2040206619829382.

[86]

De Clercq E. AMD3100/CXCR4 inhibitor. Front Immunol. 2015; 6: 276.

[87]

Guo P, You JO, Yang J, Jia D, Moses MA, Auguste DT. Inhibiting metastatic breast cancer cell migration via the synergy of targeted, pH-triggered siRNA delivery and chemokine axis blockade. Mol Pharm. 2014; 11: 755-65.

[88]

Guo P, You JO, Yang J, Moses MA, Auguste DT. Using breast cancer cell CXCR4 surface expression to predict liposome binding and cytotoxicity. Biomaterials. 2012; 33: 8104-10.

[89]

Cagliani R, Gatto F, Cibecchini G, Marotta R, Catalano F, Sanchez-Moreno P, et al. CXCL5 modified nanoparticle surface improves CXCR2+ cell selective internalization . Cells. 2020; 9: 56.

[90]

Pisani A, Donno R, Gennari A, Cibecchini G, Catalano F, Marotta R, et al. CXCL12-PLGA/pluronic nanoparticle internalization abrogates CXCR4-mediated cell migration. Nanomaterials (Basel). 2020; 10: 2304.

[91]

Xiong J, Feng JL, Qiu L, Gao Z, Li P, Pang L, et al. SDF-1-loaded PLGA nanoparticles for the targeted photoacoustic imaging and photothermal therapy of metastatic lymph nodes in tongue squamous cell carcinoma. Int J Pharm. 2019; 554: 93-104.

[92]

Xu J, Wang J, Qiu J, Liu H, Wang Y, Cui Y, et al. Nanoparticles retard immune cells recruitment in vivo by inhibiting chemokine expression . Biomaterials. 2021; 265: 120392.

[93]

Gamucci O, Bardi G. Cerium dioxide nanoparticles selectively up-regulate C-C chemokine receptor 2 and CD16 expression on human monocytes. ENTL. 2014; 5: 1.

[94]

Popova TG, Teunis A, Magni R, Luchini A, Espina V, Liotta LA, et al. Chemokine-releasing nanoparticles for manipulation of lymph node microenvironment. Nanomaterials (Basel). 2015; 5: 298-320.

[95]

Popova TG, Teunis A, Espina V, Liotta LA, Popov SG. Chemokine-releasing microparticles improve bacterial clearance and survival of anthrax spore-challenged mice. PLoS One. 2016; 11: e0163163.

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