A highly neutralizing human monoclonal antibody targeting a novel linear epitope on staphylococcal enterotoxin B

References

• Foster TJ. Immune evasion by Staphylococci. Nat Rev Microbiol. 2005;3(12):948–10. doi:10.1038/nrmicro1289.
   PubMed Web of Science ®Google Scholar
• Bae JS, Da F, Liu R, He L, Lv H, Fisher EL, Rajagopalan G, Li M, Cheung GYC, Otto M. et al. Contribution of staphylococcal enterotoxin B to Staphylococcus aureus systemic infection. J Infect Dis. 2020;223(10):1766–75. doi:10.1093/infdis/jiaa584.
   Web of Science ®Google Scholar
• Sun C, Wang Q, Li W-T, Wen D-N, Chen C-H, Yang X, Shi W, Meng Q-H, Yao K-H, Qian S-Y. et al. Molecular characteristics and antimicrobial susceptibility of Staphylococcus aureus among children with respiratory tract infections in southwest China. World J Pediatr. 2020;16(3):284–92. doi:10.1007/s12519-019-00317-4.
   PubMed Web of Science ®Google Scholar
• Garcia C, Briggs C, Zhang L, Guan L, Gabriel JL, Rogers TJ. Molecular characterization of the putative T-cell receptor cavity of the superantigen staphylococcal enterotoxin B. Immunology. 1998;94(2):160–6. doi:10.1046/j.1365-2567.1998.00493.x.
   PubMed Web of Science ®Google Scholar
• Jardetzky TS, Brown JH, Gorga JC, Stern LJ, Urban RG, Chi Y-I, Stauffacher C, Strominger JL, Wiley DC. Three-dimensional structure of a human class II histocompatibility molecule complexed with superantigen. J Immunol. 2018;201(7):711–8. doi:10.1038/368711a0.
   Web of Science ®Google Scholar
• Wang LM, Zhao YW, Li Z, Guo Y, Jones LL, Kranz DM, Mourad W, Li H. Crystal structure of a complete ternary complex of TCR, superantigen and peptide-MHC. Nature Structural & Molecular Biology. 2007;14(2):169–71. doi:10.1038/nsmb1193.
   PubMed Web of Science ®Google Scholar
• Thammavongsa V, Kim HK, Missiakas D, Schneewind O. Staphylococcal manipulation of host immune responses. Nat Rev Microbiol. 2015;13(9):529–43. doi:10.1038/nrmicro3521.
   PubMed Web of Science ®Google Scholar
• Fraser JD, Proft T. The bacterial superantigen and superantigen-like proteins. Immunol Rev. 2008;225:226–43. doi:10.1111/j.1600-065X.2008.00681.x.
   PubMed Web of Science ®Google Scholar
• Darenberg J, Söderquist B, Normark BH, Norrby‐Teglund A. Differences in potency of intravenous polyspecific immunoglobulin G against streptococcal and staphylococcal superantigens: Implications for therapy of toxic shock syndrome. Clin Infect Dis. 2004;38(6):836–42. doi:10.1086/381979.
   PubMed Web of Science ®Google Scholar
• Kunkl M, Amormino C, Spallotta F, Caristi S, Fiorillo MT, Paiardini A, Kaempfer R, Tuosto L. Bivalent binding of staphylococcal superantigens to the TCR and CD28 triggers inflammatory signals independently of antigen presenting cells. Front Immunol. 2023;14:15. doi:10.3389/fimmu.2023.1170821.
   Web of Science ®Google Scholar
• Benkerroum N. Staphylococcal enterotoxins and enterotoxin-like toxins with special reference to dairy products: An overview. Crit Rev Food Sci Nutr. 2018;58(12):1943–70. doi:10.1080/10408398.2017.1289149.
   PubMed Web of Science ®Google Scholar
• Mantis NJ. Vaccines against the category B toxins: Staphylococcal enterotoxin B, epsilon toxin and ricin. Adv Drug Deliv Rev. 2005;57(9):1424–39. doi:10.1016/j.addr.2005.01.017.
   PubMed Web of Science ®Google Scholar
• Kaempfer R, Arad G, Levy R, Hillman D, Nasie I, Rotfogel Z. CD28: direct and critical receptor for superantigen toxins. Toxins. 2013;5(9):1531–42. doi:10.3390/toxins5091531.
   PubMed Web of Science ®Google Scholar
• Varshney AK, Wang XB, MacIntyre J, Zollner RS, Kelleher K, Kovalenko OV, Pechuan X, Byrne FR, Fries BC. Humanized staphylococcal enterotoxin B (SEB)–specific monoclonal antibodies protect from SEB intoxication and Staphylococcus aureus infections alone or as adjunctive therapy with vancomycin. J Infect Dis. 2014;210(6):973–81. doi:10.1093/infdis/jiu198.
   PubMed Web of Science ®Google Scholar
• Chen G, Karauzum H, Long H, Carranza D, Holtsberg FW, Howell KA, Abaandou L, Zhang B, Jarvik N, Ye W. et al. Potent neutralization of staphylococcal enterotoxin B in vivo by antibodies that block binding to the T-Cell receptor. J Mol Biol. 2019;431(21):4354–67. doi:10.1016/j.jmb.2019.03.017.
   PubMed Web of Science ®Google Scholar
• Dutta K, Varshney AK, Franklin MC, Goger M, Wang X, Fries BC. Mechanisms mediating enhanced neutralization efficacy of staphylococcal enterotoxin B by combinations of monoclonal antibodies. J Biol Chem. 2015;290(11):6715–30. doi:10.1074/jbc.M114.630715.
   PubMed Web of Science ®Google Scholar
• Liu YY, Song Z, Ge S, Zhang J, Xu L, Yang F, Lu D, Luo P, Gu J, Zou Q. et al. Determining the immunological characteristics of a novel human monoclonal antibody developed against staphylococcal enterotoxin B. Human Vaccines Immunother. 2020;16(7):1708–18. doi:10.1080/21645515.2020.1744362.
   PubMed Web of Science ®Google Scholar
• Miethke T, Wahl C, Heeg K, Echtenacher B, Krammer PH, Wagner H. T cell-mediated lethal shock triggered in mice by the superantigen staphylococcal enterotoxin B: critical role of tumor necrosis factor. J Exp Med. 1992;175(1):91–8. doi:10.1084/jem.175.1.91.
   PubMed Web of Science ®Google Scholar
• Dan N, Setua S, Kashyap VK, Khan S, Jaggi M, Yallapu M, Chauhan S. Antibody-drug conjugates for cancer therapy: chemistry to clinical implications. Pharmaceuticals. 2018;11(2):22. doi:10.3390/ph11020032.
   Web of Science ®Google Scholar
• Swaminathan S, Furey W, Pletcher J, Sax M. Crystal structure of staphylococcal enterotoxin B, a superantigen. Nature. 1992;359(6398):801–6. doi:10.1038/359801a0.
   PubMed Web of Science ®Google Scholar
• Zhao Z, Sun HQ, Wei SS, Li B, Feng Q, Zhu J, Zeng H, Zou Q-M, Wu C. Multiple B-cell epitope vaccine induces a staphylococcus enterotoxin B-specific IgG1 protective response against MRSA infection. Sci Rep. 2015;5(1):12371. doi:10.1038/srep12371.
   PubMedGoogle Scholar
• Soos JM, Johnson HM. Multiple binding sites on the superantigen, staphylococcal enterotoxin B, imparts versatility in binding to MHC class II molecules. Biochem Biophys Res Commun. 1994;201(2):596–602. doi:10.1006/bbrc.1994.1743.
   PubMed Web of Science ®Google Scholar
• Kaempfer R. Bacterial superantigen toxins, CD28, and drug development. Toxins. 2018;10(11):6. doi:10.3390/toxins10110459.
   Web of Science ®Google Scholar
• Deacy AM, Gan SK, Derrick JP. Superantigen recognition and interactions: functions, mechanisms and applications. Front Immunol. 2021;12:731845. doi:10.3389/fimmu.2021.731845.
   PubMed Web of Science ®Google Scholar
• Hu N, Qiao C, Wang J, Wang Z, Li X, Zhou L, Wu J, Zhang D, Feng J, Shen B. et al. Identification of a novel protective human monoclonal antibody, LXY8, that targets the key neutralizing epitopes of staphylococcal enterotoxin B. Biochem Biophys Res Commun. 2021;549:120–7. doi:10.1016/j.bbrc.2021.02.057.
   PubMed Web of Science ®Google Scholar
• Xia T, Liang S, Wang H, Hu S, Sun Y, Yu X, Han J, Li J, Guo S, Dai J. et al. Structural basis for the neutralization and specificity of staphylococcal enterotoxin B against its MHC class II binding site. Mabs-austin. 2014;6(1):119–29. doi:10.4161/mabs.27106.
   PubMed Web of Science ®Google Scholar
• Levy R, Rotfogel Z, Hillman D, Popugailo A, Arad G, Supper E, Osman F, Kaempfer R. Superantigens hyperinduce inflammatory cytokines by enhancing the B7-2/CD28 costimulatory receptor interaction. Proc Natl Acad Sci U S A. 2016;113(42):E6437–e46. doi:10.1073/pnas.1603321113.
   PubMed Web of Science ®Google Scholar
• Leder L, Llera A, Lavoie PM, Lebedeva MI, Li H, Sékaly R-P, Bohach GA, Gahr PJ, Schlievert PM, Karjalainen K. et al. A mutational analysis of the binding of staphylococcal enterotoxins B and C3 to the T cell receptor β chain and major histocompatibility complex class II. J Exp Med. 1998;187(6):823–33. doi:10.1084/jem.187.6.823.
   PubMed Web of Science ®Google Scholar
• Hu DL, Nakane A. Mechanisms of staphylococcal enterotoxin-induced emesis. Eur J Pharmacol. 2014;722:95–107. doi:10.1016/j.ejphar.2013.08.050.
   PubMed Web of Science ®Google Scholar
• Deacy AM, Gan SKE, Derrick JP. Superantigen recognition and interactions: functions, mechanisms and applications. Front Immunol. 2021;12:16. doi:10.3389/fimmu.2021.731845.
   Web of Science ®Google Scholar
• Di Stefano A, Paulesu L, Niccolai N, Scarselli M, Soldani P, Neri P. Identification of critical residues of staphylococcal enterotoxin B for lymphomonocyte proliferation and cytokine production. J Pept Res. 1998;52(2):130–6. doi:10.1111/j.1399-3011.1998.tb01367.x.
   PubMedGoogle Scholar
• Kaempfer R, Popugailo A, Levy R, Arad G, Hillman D, Rotfogel Z. Bacterial superantigen toxins induce a lethal cytokine storm by enhancing B7-2/CD28 costimulatory receptor engagement, a critical immune checkpoint. Recept & Clin Invest. 2017;4(1):e1500. doi:10.14800/rci.1500.
   PubMedGoogle Scholar
• Vidlak D, Mariani MM, Aldrich A, Liu S, Kielian T. Roles of toll-like receptor 2 (TLR2) and superantigens on adaptive immune responses during CNS staphylococcal infection. Brain Behav Immun. 2011;25(5):905–14. doi:10.1016/j.bbi.2010.09.016.
   PubMed Web of Science ®Google Scholar
• Martens K, Seys SF, Alpizar YA, Schrijvers R, Bullens DMA, Breynaert C, Lebeer S, Steelant B. Staphylococcus aureus enterotoxin B disrupts nasal epithelial barrier integrity. Clin Exp Allergy. 2021;51(1):87–98. doi:10.1111/cea.13760.
   PubMed Web of Science ®Google Scholar
• Schlievert PM, Cahill MP, Hostager BS, Brosnahan AJ, Klingelhutz AJ, Gourronc FA, Bishop GA, Leung DYM. Staphylococcal superantigens stimulate epithelial cells through CD40 to produce chemokines. mBio. 2019;10(2):11. doi:10.1128/mBio.00214-19.
   Web of Science ®Google Scholar
• Lamphear JG, Stevens KR, Rich RR. Intercellular adhesion molecule-1 and leukocyte function-associated antigen-3 provide costimulation for superantigen-induced T lymphocyte proliferation in the absence of a specific presenting molecule. J Immunol. 1998;160(2):615–23. doi:10.4049/jimmunol.160.2.615.
   PubMed Web of Science ®Google Scholar
• Kunkl M, Amormino C, Caristi S, Tedeschi V, Fiorillo MT, Levy R, Popugailo A, Kaempfer R, Tuosto L. Binding of staphylococcal enterotoxin B (SEB) to B7 receptors triggers TCR- and CD28-mediated inflammatory signals in the absence of MHC class II molecules. Front Immunol. 2021;12:16. doi:10.3389/fimmu.2021.723689.
   Web of Science ®Google Scholar
• Truant SN, Redolfi DM, Sarratea MB, Malchiodi EL, Fernández MM. Superantigens, a paradox of the immune response. Toxins. 2022;14(11):30. doi:10.3390/toxins14110800.
   PubMed Web of Science ®Google Scholar
• Shaler CR, Choi J, Rudak PT, Memarnejadian A, Szabo PA, Tun-Abraham ME, Rossjohn J, Corbett AJ, McCluskey J, McCormick JK. et al. MAIT cells launch a rapid, robust and distinct hyperinflammatory response to bacterial superantigens and quickly acquire an anergic phenotype that impedes their cognate antimicrobial function: Defining a novel mechanism of superantigen-induced immunopathology and immunosuppression. PLOS Biol. 2017;15(6):35. doi:10.1371/journal.pbio.2001930.
   Web of Science ®Google Scholar
• Lee J, Park N, Park JY, Kaplan BLF, Pruett SB, Park JW, Park YH, Seo KS. Induction of immunosuppressive CD8+CD25+FOXP3+Regulatory T cells by suboptimal stimulation with staphylococcal enterotoxin C1. J Immunol. 2018;200(2):669–80. doi:10.4049/jimmunol.1602109.
   PubMed Web of Science ®Google Scholar