1. Andrades Valtueña, A. et al. The Stone Age plague and its persistence in Eurasia. Curr. Biol. 27, 3683–3691 (2017).

2. Stenseth, N. C. et al. Plague: past, present, and future. PLoS Med. 5, e3 (2008).

3. Benedictow, O. J. The Black Death 1346–1353: The Complete History (Boydell, 2004).

4. Samson, M. et al. Resistance to HIV-1 infection in Caucasian individuals bearing mutant alleles of the CCR-5 chemokine receptor gene. Nature 382, 722–725 (1996).

5. Liu, R. et al. Homozygous defect in HIV-1 coreceptor accounts for resistance of some multiply-exposed individuals to HIV-1 infection. Cell 86, 367–377 (1996).

6. Stephens, J. C. et al. Dating the origin of the CCR5-Δ32 AIDS-resistance allele by the coalescence of haplotypes. Am. J. Hum. Genet. 62, 1507–1515 (1998).

7. Mecsas, J. et al. CCR5 mutation and plague protection. Nature 427, 606 (2004).

8. Elvin, S. J. et al. Ambiguous role of CCR5 in Y. pestis infection. Nature 430, 418 (2004).

9. Galán, J. E., Lara-Tejero, M., Marlovits, T. C. & Wagner, S. Bacterial type III secretion systems: specialized nanomachines for protein delivery into target cells. Annu. Rev. Microbiol. 68, 415–438 (2014).

10. Achtman, M. et al. Yersinia pestis, the cause of plague, is a recently emerged clone of Yersinia pseudotuberculosis. Proc. Natl Acad. Sci. USA 96, 14043–14048 (1999).

11. Cornelis, G. R. The Yersinia deadly kiss. J. Bacteriol. 180, 5495–5504 (1998).

12. Marketon, M. M., DePaolo, R. W., DeBord, K. L., Jabri, B. & Schneewind, O. Plague bacteria target immune cells during infection. Science 309, 1739–1741 (2005).

13. Inglesby, T. V. et al. Plague as a biological weapon: medical and public health management. J. Am. Med. Assoc. 283, 2281–2290 (2000).

14. Quenee, L. E. & Schneewind, O. Plague vaccines and the molecular basis of immunity against Yersinia pestis. Hum. Vaccin. 5, 817–823 (2009).

15. Mitchell, A. et al. Glutathionylation of Yersinia pestis LcrV and its efects on plague pathogenesis. mBio 8, e00646-17 (2017).

16. Collier, R. J. Understanding the mode of action of diphtheria toxin: a perspective on progress during the 20th century. Toxicon 39, 1793–1803 (2001).

17. Boulay, F., Tardif, M., Brouchon, L. & Vignais, P. The human N-formylpeptide receptor. Characterization of two cDNA isolates and evidence for a new subfamily of G-protein-coupled receptors. Biochemistry 29, 11123–11133 (1990).

18. Miettinen, H. M. et al. The ligand binding site of the formyl peptide receptor maps in the transmembrane region. J. Immunol. 159, 4045–4054 (1997).

19. Le, Y., Murphy, P. M. & Wang, J. M. Formyl-peptide receptors revisited. Trends Immunol. 23, 541–548 (2002).

20. Schaffrath, R. & Stark, M. J. Decoding the biosynthesis and function of diphthamide, an enigmatic modification of translation elongation factor 2 (EF2). Microb. Cell 1, 203–205 (2014).

21. Sheahan, K.-L. & Isberg, R. R. Identification of mammalian proteins that collaborate with type III secretion system function: involvement of a chemokine receptor in supporting translocon activity. mBio 6, e02023-14 (2015).

22. Bardoel, B. W. et al. Identification of an immunomodulating metalloprotease of Pseudomonas aeruginosa (IMPa). Cell. Microbiol. 14, 902–913 (2012).

23. Mueller, C. A. et al. The V-antigen of Yersinia forms a distinct structure at the tip of injectisome needles. Science 310, 674–676 (2005).

24. Vacchelli, E. et al. Chemotherapy-induced antitumor immunity requires formyl peptide receptor 1. Science 350, 972–978 (2015).

25. Perretti, M. & D’Acquisto, F. Annexin A1 and glucocorticoids as effectors of the resolution of inflammation. Nat. Rev. Immunol. 9, 62–70 (2009).

26. Postma, B. et al. Chemotaxis inhibitory protein of Staphylococcus aureus binds specifically to the C5a and formylated peptide receptor. J. Immunol. 172, 6994–7001 (2004).

27. Wenzel-Seifert, K., Grünbaum, L. & Seifert, R. Differential inhibition of human neutrophil activation by cyclosporins A, D, and H. Cyclosporin H is a potent and effective inhibitor of formyl peptide-induced superoxide formation. J. Immunol. 147, 1940–1946 (1991).

28. Ligtenberg, K. G., Miller, N. C., Mitchell, A., Plano, G. V. & Schneewind, O. LcrV mutants that abolish Yersinia type III injectisome function. J. Bacteriol. 195, 777–787 (2013).

29. Welkos, S., Friedlander, A., McDowell, D., Weeks, J. & Tobery, S. V antigen of Yersinia pestis inhibits neutrophil chemotaxis. Microb. Pathog. 24, 185–196 (1998).

30. Bartra, S. S., Jackson, M. W., Ross, J. A. & Plano, G. V. Calcium-regulated type III secretion of Yop proteins by an Escherichia coli hha mutant carrying a Yersinia pestis pCD1 virulence plasmid. Infect. Immun. 74, 1381–1386 (2006).

31. Gage, K. L. & Kosoy, M. Y. Natural history of plague: perspectives from more than a century of research. Annu. Rev. Entomol. 50, 505–528 (2005).

32. Hartt, J. K., Barish, G., Murphy, P. M. & Gao, J. L. N-formylpeptides induce two distinct concentration optima for mouse neutrophil chemotaxis by differential interaction with two N-formylpeptide receptor (FPR) subtypes. Molecular characterization of FPR2, a second mouse neutrophil FPR. J. Exp. Med. 190, 741–748 (1999).

33. Stempel, H. et al. Strain-specific loss of formyl peptide receptor 3 in the murine vomeronasal and immune systems. J. Biol. Chem. 291, 9762–9775 (2016).

34. Liu, M. et al. Formylpeptide receptors are critical for rapid neutrophil mobilization in host defense against Listeria monocytogenes. Sci. Rep. 2, 786 (2012).

35. Pechous, R. D., Sivaraman, V., Price, P. A., Stasulli, N. M. & Goldman, W. E. Early host cell targets of Yersinia pestis during primary pneumonic plague. PLoS Pathog. 9, e1003679 (2013).

36. Shannon, J. G. et al. Yersinia pestis subverts the dermal neutrophil response in a mouse model of bubonic plague. mBio 4, e00170-13 (2013).

37. Quenee, L. E., Cornelius, C. A., Ciletti, N. A., Elli, D. & Schneewind, O. Yersinia pestis caf1 variants and the limits of plague vaccine protection. Infect. Immun. 76, 2025–2036 (2008).

38. Sahagun-Ruiz, A. et al. Contrasting evolution of the human leukocyte N-formylpeptide receptor subtypes FPR and FPRL1R. Genes Immun. 2, 335–342 (2001).

39. Håkansson, S., Bergman, T., Vanooteghem, J.-C., Cornelis, G. & Wolf-Watz, H. YopB and YopD constitute a novel class of Yersinia Yop proteins. Infect. Immun. 61, 71–80 (1993).

40. Torruellas, J., Jackson, M. W., Pennock, J. W. & Plano, G. V. The Yersinia pestis type III secretion needle plays a role in the regulation of Yop secretion. Mol. Microbiol. 57, 1719–1733 (2005).

41. Cornelis, G. R. Yersinia type III secretion: send in the effectors. J. Cell Biol. 158, 401–408 (2002).

42. Zhang, Q. et al. Circulating mitochondrial DAMPs cause inflammatory responses to injury. Nature 464, 104–107 (2010).

43. Dorward, D. A. et al. The role of formylated peptides and formyl peptide receptor 1 in governing neutrophil function during acute inflammation. Am. J. Pathol. 185, 1172–1184 (2015).

44. Muto, Y., Guindon, S., Umemura, T., Kőhidai, L. & Ueda, H. Adaptive evolution of formyl peptide receptors in mammals. J. Mol. Evol. 80, 130–141 (2015).

45. Ye, R. D. et al. International Union of Basic and Clinical Pharmacology. LXXIII. Nomenclature for the formyl peptide receptor (FPR) family. Pharmacol. Rev. 61, 119–161 (2009).

46. Quignon, P., Rimbault, M., Robin, S. & Galibert, F. Genetics of canine olfaction and receptor diversity. Mamm. Genome 23, 132–143 (2012).

47. Perry, R. D. & Fetherston, J. D. Yersinia pestis—etiologic agent of plague. Clin. Microbiol. Rev. 10, 35–66 (1997).

48. Baeten, L. A. et al. Immunological and clinical response of coyotes (Canis latrans) to experimental inoculation with Yersinia pestis. J. Wildl. Dis. 49, 932–939 (2013).

49. Liang, X. Y. et al. FPR1 interacts with CFH, HTRA1 and smoking in exudative age-related macular degeneration and polypoidal choroidal vasculopathy. Eye 28, 1502–1510 (2014).

50. Otani, T. et al. Polymorphisms of the formylpeptide receptor gene (FPR1) and susceptibility to stomach cancer in 1531 consecutive autopsy cases. Biochem. Biophys. Res. Commun. 405, 356–361 (2011).

51. Girard, G. Plague. Annu. Rev. Microbiol. 9, 253–276 (1955).

52. Meyer, K. F., Smith, G., Foster, L., Brookman, M. & Sung, M. H. Live, attenuated Yersinia pestis vaccine: virulent in non-human primates, harmless to guinea pigs. J. Infect. Dis. 129, S85–S120 (1974).

53. Brubaker, R. R. Mutation rate to nonpigmentation in Pasteurella pestis. J. Bacteriol. 98, 1404–1406 (1969).

54. DeBord, K. L. et al. Immunogenicity and protective immunity against bubonic plague and pneumonic plague by immunization of mice with the recombinant V10 antigen, a variant of LcrV. Infect. Immun. 74, 4910–4914 (2006).

55. Higuchi, K. An improved chemically defined culture medium for strain L mouse cells based on growth responses to graded levels of nutrients including iron and zinc ions. J. Cell. Physiol. 75, 65–72 (1970).

56. Doll, J. M. et al. Cat-transmitted fatal pneumonic plague in a person who traveled from Colorado to Arizona. Am. J. Trop. Med. Hyg. 51, 109–114 (1994).

57. Hanahan, D. Studies on transformation of Escherichia coli with plasmids. J. Mol. Biol. 166, 557–580 (1983).

58. Forsberg, A., Bölin, I., Norlander, L. & Wolf-Watz, H. Molecular cloning and expression of calcium-regulated, plasmid-coded proteins of Y. pseudotuberculosis. Microb. Pathog. 2, 123–137 (1987).

59. Ton-That, H. & Schneewind, O. Assembly of pili on the surface of Corynebacterium diphtheriae. Mol. Microbiol. 50, 1429–1438 (2003).

60. Anderson, D. M. & Schneewind, O. A mRNA signal for the type III secretion of Yop proteins by Yersinia enterocolitica. Science 278, 1140–1143 (1997).

61. Sundström, C. & Nilsson, K. Establishment and characterization of a human histiocytic lymphoma cell line (U-937). Int. J. Cancer 17, 565–577 (1976).

62. Gallagher, R. et al. Characterization of the continuous, differentiating myeloid cell line (HL-60) from a patient with acute promyelocytic leukemia. Blood 54, 713–733 (1979).

63. Shalem, O. et al. Genome-scale CRISPR–Cas9 knockout screening in human cells. Science 343, 84–87 (2014).

64. Edgar, R., Domrachev, M. & Lash, A. E. Gene Expression Omnibus: NCBI gene expression and hybridization array data repository. Nucleic Acids Res. 30, 207–210 (2002).

65. Quenee, L. E., Ciletti, N. A., Elli, D., Hermanas, T. M. & Schneewind, O. Prevention of pneumonic plague in mice, rats, guinea pigs and non-human primates with clinical grade rV10, rV10-2 or F1-V vaccines. Vaccine 29, 6572–6583 (2011).