[논문]Quorum Sensing in Bacillus thuringiensis Is Required for Completion of a Full Infectious Cycle in the Insect

Slamti, Leyla; Perchat, Sté; phane; Huillet, Eugé; nie; Lereclus, Didier

doi:10.3390/toxins6082239

[해외논문] Quorum Sensing in Bacillus thuringiensis Is Required for Completion of a Full Infectious Cycle in the Insect 원문보기

Toxins, v.6 no.8, 2014년, pp.2239 - 2255

Slamti, Leyla , Perchat, Stéphane , Huillet, Eugénie , Lereclus, Didier

Abstract ▼ AI-Helper

Bacterial cell-cell communication or quorum sensing (QS) is a biological process commonly described as allowing bacteria belonging to a same pherotype to coordinate gene expression to cell density. In Gram-positive bacteria, cell-cell communication mainly relies on cytoplasmic sensors regulated by secreted and re-imported signaling peptides. The Bacillus quorum sensors Rap, NprR, and PlcR were previously identified as the first members of a new protein family called RNPP. Except for the Rap proteins, these RNPP regulators are transcription factors that directly regulate gene expression. QS regulates important biological functions in bacteria of the Bacillus cereus group. PlcR was first characterized as the main regulator of virulence in B. thuringiensis and B. cereus. More recently, the PlcR-like regulator PlcRa was characterized for its role in cysteine metabolism and in resistance to oxidative stress. The NprR regulator controls the necrotrophic properties allowing the bacteria to survive in the infected host. The Rap proteins negatively affect sporulation via their interaction with a phosphorelay protein involved in the activation of Spo0A, the master regulator of this differentiation pathway. In this review we aim at providing a complete picture of the QS systems that are sequentially activated during the lifecycle of B. cereus and B. thuringiensis in an insect model of infection.

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참고문헌 (81)

1. Deng C. Peng Q. Song F. Lereclus D. Regulation of cry gene expression in Bacillus thuringiensis Toxins 2014 6 2194 2209 10.3390/toxins6072194 25055802

상세보기
2. Sanahuja G. Banakar R. Twyman R.M. Capell T. Christou P. Bacillus thuringiensis : A century of research, development and commercial applications Plant Biotechnol. J. 2011 9 283 300 10.1111/j.1467-7652.2011.00595.x 21375687

상세보기
3. Sanchis V. From microbial sprays to insect-resistant transgenic plants: History of the biopesticide Bacillus thuringiensis . A review Agron. Sustain. Dev. 2011 31 217 231 10.1051/agro/2010027

상세보기
4. Helgason E. Okstad O.A. Caugant D.A. Johansen H.A. Fouet A. Mock M. Hegna I. Kolsto A.B. Bacillus anthracis , Bacillus cereus , and Bacillus thuringiensis —One species on the basis of genetic evidence Appl. Environ. Microbiol. 2000 66 2627 2630 10.1128/AEM.66.6.2627-2630.2000 10831447

상세보기
5. Stenfors Arnesen L.P. Fagerlund A. Granum P.E. From soil to gut: Bacillus cereus and its food poisoning toxins FEMS Microbiol. Rev. 2008 32 579 606 10.1111/j.1574-6976.2008.00112.x 18422617

상세보기
6. Agata N. Mori M. Ohta M. Suwan S. Ohtani I. Isobe M. A novel dodecadepsipeptide, cereulide, isolated from Bacillus cereus causes vacuole formation in HEp-2 cells FEMS Microbiol. Lett. 1994 121 31 34 8082824

상세보기
7. Ehling-Schulz M. Svensson B. Guinebretiere M.H. Lindback T. Andersson M. Schulz A. Fricker M. Christiansson A. Granum P.E. Martlbauer E. Emetic toxin formation of Bacillus cereus is restricted to a single evolutionary lineage of closely related strains Microbiology 2005 151 183 197 10.1099/mic.0.27607-0 15632437

상세보기
8. Castedo E. Castro A. Martin P. Roda J. Montero C.G. Bacillus cereus prosthetic valve endocarditis Ann. Thorac. Surg. 1999 68 2351 2352 10.1016/S0003-4975(99)01163-7 10617040

상세보기
9. Chu W.P. Que T.L. Lee W.K. Wong S.N. Meningoencephalitis caused by Bacillus cereus in a neonate Hong Kong Med. J. 2001 7 89 92 11406681
10. Gaur A.H. Patrick C.C. McCullers J.A. Flynn P.M. Pearson T.A. Razzouk B.I. Thompson S.J. Shenep J.L. Bacillus cereus bacteremia and meningitis in immunocompromised children Clin. Infect. Dis. 2001 32 1456 1462 10.1086/320154 11317247

상세보기
11. Bottone E.J. Bacillus cereus , a volatile human pathogen Clin. Microbiol. Rev. 2010 23 382 398 10.1128/CMR.00073-09 20375358

상세보기
12. Gohar M. Faegri K. Perchat S. Ravnum S. Okstad O.A. Gominet M. Kolsto A.B. Lereclus D. The PlcR virulence regulon of Bacillus cereus PLoS One 2008 3 e2793 10.1371/journal.pone.0002793 18665214

상세보기
13. Salamitou S. Ramisse F. Brehelin M. Bourguet D. Gilois N. Gominet M. Hernandez E. Lereclus D. The PlcR regulon is involved in the opportunistic properties of Bacillus thuringiensis and Bacillus cereus in mice and insects Microbiology 2000 146 2825 2832 11065361
14. Callegan M.C. Kane S.T. Cochran D.C. Gilmore M.S. Gominet M. Lereclus D. Relationship of PlcR-regulated factors to Bacillus endophthalmitis virulence Infect. Immun. 2003 71 3116 3124 10.1128/IAI.71.6.3116-3124.2003 12761089

상세보기
15. Dubois T. Faegri K. Perchat S. Lemy C. Buisson C. Nielsen-LeRoux C. Gohar M. Jacques P. Ramarao N. Kolsto A.B. Necrotrophism is a quorum-sensing-regulated lifestyle in Bacillus thuringiensis PLoS Pathog. 2012 8 e1002629 10.1371/journal.ppat.1002629 22511867

상세보기
16. Raymond B. Johnston P.R. Nielsen-LeRoux C. Lereclus D. Crickmore N. Bacillus thuringiensis : An impotent pathogen? Trends Microbiol. 2010 18 189 194 10.1016/j.tim.2010.02.006 20338765

상세보기
17. Olmedo G. Ninfa E.G. Stock J. Youngman P. Novel mutations that alter the regulation of sporulation in Bacillus subtilis . Evidence that phosphorylation of regulatory protein SpoOA controls the initiation of sporulation J. Mol. Biol. 1990 215 359 372 10.1016/S0022-2836(05)80357-2 2121995

상세보기
18. Sonenshein A.L. Control of sporulation initiation in Bacillus subtilis Curr. Opin. Microbiol. 2000 3 561 566 10.1016/S1369-5274(00)00141-7 11121774

상세보기
19. Strauch M. Webb V. Spiegelman G. Hoch J.A. The SpoOA protein of Bacillus subtilis is a repressor of the abrB gene Proc. Natl. Acad. Sci. USA 1990 87 1801 1805 10.1073/pnas.87.5.1801 2106683

상세보기
20. Lereclus D. Agaisse H. Gominet M. Chaufaux J. Overproduction of encapsulated insecticidal crystal proteins in a Bacillus thuringiensis spo0A mutant Biotechnology (N. Y.) 1995 13 67 71 10.1038/nbt0195-67 9634751

상세보기
21. Ng W.L. Bassler B.L. Bacterial quorum-sensing network architectures Annu. Rev. Genet. 2009 43 197 222 10.1146/annurev-genet-102108-134304 19686078

상세보기
22. Rutherford S.T. Bassler B.L. Bacterial quorum sensing: Its role in virulence and possibilities for its control Cold Spring Harb. Perspect. Med. 2012 2 10.1101/cshperspect.a012427
23. Ji G. Beavis R.C. Novick R.P. Cell density control of staphylococcal virulence mediated by an octapeptide pheromone Proc. Natl. Acad. Sci. USA 1995 92 12055 12059 10.1073/pnas.92.26.12055 8618843

상세보기
24. Novick R.P. Geisinger E. Quorum sensing in Staphylococci Ann. Rev. Genet. 2008 42 541 564 10.1146/annurev.genet.42.110807.091640 18713030

상세보기
25. Suzuki A. Mori M. Sakagami Y. Isogai A. Fujino M. Kitada C. Craig R.A. Clewell D.B. Isolation and structure of bacterial sex pheromone, cPD1 Science 1984 226 849 850 6436978

상세보기
26. Kozlowicz B.K. Bae T. Dunny G.M. Enterococcus faecalis pheromone-responsive protein PrgX: Genetic separation of positive autoregulatory functions from those involved in negative regulation of conjugative plasmid transfer Mol. Microbiol. 2004 54 520 532 10.1111/j.1365-2958.2004.04286.x 15469521

상세보기
27. Cook L.C. Federle M.J. Peptide pheromone signaling in Streptococcus and Enterococcus FEMS Microbiol. Rev. 2014 38 473 492 10.1111/1574-6976.12046 24118108

상세보기
28. Perego M. Hoch J.A. Cell-cell communication regulates the effects of protein aspartate phosphatases on the phosphorelay controlling development in Bacillus subtilis Proc. Natl. Acad. Sci. USA 1996 93 1549 1553 10.1073/pnas.93.4.1549 8643670

상세보기
29. Lazazzera B.A. Solomon J.M. Grossman A.D. An exported peptide functions intracellularly to contribute to cell density signaling in Bacillus subtilis Cell 1997 89 917 925 10.1016/S0092-8674(00)80277-9 9200610

상세보기
30. Perego M. Forty years in the making: Understanding the molecular mechanism of peptide regulation in bacterial development PLoS Biol. 2013 11 e1001516 10.1371/journal.pbio.1001516 23526885

상세보기
31. Shi K. Brown C.K. Gu Z.Y. Kozlowicz B.K. Dunny G.M. Ohlendorf D.H. Earhart C.A. Structure of peptide sex pheromone receptor PrgX and PrgX/pheromone complexes and regulation of conjugation in Enterococcus faecalis Proc. Natl. Acad. Sci. USA 2005 102 18596 18601 16339309

상세보기
32. Declerck N. Bouillaut L. Chaix D. Rugani N. Slamti L. Hoh F. Lereclus D. Arold S.T. Structure of PlcR: Insights into virulence regulation and evolution of quorum sensing in Gram-positive bacteria Proc. Natl. Acad. Sci. USA 2007 104 18490 18495 17998541

상세보기
33. Baker M.D. Neiditch M.B. Structural basis of response regulator inhibition by a bacterial anti-activator protein PLoS Biol. 2011 9 e1001226 10.1371/journal.pbio.1001226 22215984

상세보기
34. Gallego del Sol F. Marina A. Structural basis of Rap phosphatase inhibition by Phr peptides PLoS Biol. 2013 11 e1001511 10.1371/journal.pbio.1001511 23526880

상세보기
35. Parashar V. Jeffrey P.D. Neiditch M.B. Conformational change-induced repeat domain expansion regulates Rap phosphatase quorum-sensing signal receptors PLoS Biol. 2013 11 e1001512 10.1371/journal.pbio.1001512 23526881

상세보기
36. Grenha R. Slamti L. Nicaise M. Refes Y. Lereclus D. Nessler S. Structural basis for the activation mechanism of the PlcR virulence regulator by the quorum-sensing signal peptide PapR Proc. Natl. Acad. Sci. USA 2013 110 1047 1052 23277548

상세보기
37. Zouhir S. Perchat S. Nicaise M. Perez J. Guimaraes B. Lereclus D. Nessler S. Peptide-binding dependent conformational changes regulate the transcriptional activity of the quorum-sensor NprR Nucl. Acids Res. 2013 41 7920 7933 10.1093/nar/gkt546 23793817

상세보기
38. Lereclus D. Agaisse H. Gominet M. Salamitou S. Sanchis V. Identification of a Bacillus thuringiensis gene that positively regulates transcription of the phosphatidylinositol-specific phospholipase C gene at the onset of the stationary phase J. Bacteriol. 1996 178 2749 2756 8631661

상세보기
39. Agaisse H. Gominet M. Okstad O.A. Kolsto A.B. Lereclus D. PlcR is a pleiotropic regulator of extracellular virulence factor gene expression in Bacillus thuringiensis Mol. Microbiol. 1999 32 1043 1053 10.1046/j.1365-2958.1999.01419.x 10361306

상세보기
40. Gohar M. Okstad O.A. Gilois N. Sanchis V. Kolsto A.B. Lereclus D. Two-dimensional electrophoresis analysis of the extracellular proteome of Bacillus cereus reveals the importance of the PlcR regulon Proteomics 2002 2 784 791 10.1002/1615-9861(200206)2:6 3.0.CO;2-R 12112862

상세보기
41. Slamti L. Lereclus D. A cell-cell signaling peptide activates the PlcR virulence regulon in bacteria of the Bacillus cereus group EMBO J. 2002 21 4550 4559 10.1093/emboj/cdf450 12198157

상세보기
42. Bouillaut L. Perchat S. Arold S. Zorrilla S. Slamti L. Henry C. Gohar M. Declerck N. Lereclus D. Molecular basis for group-specific activation of the virulence regulator PlcR by PapR heptapeptides Nucleic Acids Res. 2008 36 3791 3801 10.1093/nar/gkn149 18492723

상세보기
43. Pomerantsev A.P. Pomerantseva O.M. Camp A.S. Mukkamala R. Goldman S. Leppla S.H. PapR peptide maturation: Role of the NprB protease in Bacillus cereus 569 PlcR/PapR global gene regulation FEMS Immunol. Med. Microbiol. 2009 55 361 377 10.1111/j.1574-695X.2008.00521.x 19159431

상세보기
44. Gominet M. Slamti L. Gilois N. Rose M. Lereclus D. Oligopeptide permease is required for expression of the Bacillus thuringiensis PlcR regulon and for virulence Mol. Microbiol. 2001 40 963 975 10.1046/j.1365-2958.2001.02440.x 11401703

상세보기
45. Slamti L. Lereclus D. Specificity and polymorphism of the PlcR-PapR quorum-sensing system in the Bacillus cereus group J. Bacteriol. 2005 187 1182 1187 10.1128/JB.187.3.1182-1187.2005 15659693

상세보기
46. Frenzel E. Doll V. Pauthner M. Lucking G. Scherer S. Ehling-Schulz M. CodY orchestrates the expression of virulence determinants in emetic Bacillus cereus by impacting key regulatory circuits Mol. Microbiol. 2012 85 67 88 10.1111/j.1365-2958.2012.08090.x 22571587

상세보기
47. Lindback T. Mols M. Basset C. Granum P.E. Kuipers O.P. Kovacs A.T. CodY, a pleiotropic regulator, influences multicellular behaviour and efficient production of virulence factors in Bacillus cereus Environ. Microbiol. 2012 14 2233 2246 10.1111/j.1462-2920.2012.02766.x 22540344

상세보기
48. Sonenshein A.L. CodY, a global regulator of stationary phase and virulence in Gram-positive bacteria Curr. Opin. Microbiol. 2005 8 203 207 10.1016/j.mib.2005.01.001 15802253

상세보기
49. Stenz L. Francois P. Whiteson K. Wolz C. Linder P. Schrenzel J. The CodY pleiotropic repressor controls virulence in gram-positive pathogens FEMS Immunol. Med. Microbiol. 2011 62 123 139 10.1111/j.1574-695X.2011.00812.x 21539625

상세보기
50. Brillard J. Susanna K. Michaud C. Dargaignaratz C. Gohar M. Nielsen-Leroux C. Ramarao N. Kolsto A.B. Nguyen-the C. Lereclus D. The YvfTU two-component system is involved in plcR expression in Bacillus cereus BMC Microbiol. 2008 8 183 10.1186/1471-2180-8-183 18925929

상세보기
51. Lereclus D. Agaisse H. Grandvalet C. Salamitou S. Gominet M. Regulation of toxin and virulence gene transcription in Bacillus thuringiensis Int. J. Med. Microbiol. 2000 290 295 299 10.1016/S1438-4221(00)80024-7 11111901

상세보기
52. Chitlaru T. Gat O. Gozlan Y. Ariel N. Shafferman A. Differential proteomic analysis of the Bacillus anthracis secretome: Distinct plasmid and chromosome CO 2 -dependent cross talk mechanisms modulate extracellular proteolytic activities J. Bacteriol. 2006 188 3551 3571 10.1128/JB.188.10.3551-3571.2006 16672610

상세보기
53. Perchat S. Dubois T. Zouhir S. Gominet M. Poncet S. Lemy C. Aumont-Nicaise M. Deutscher J. Gohar M. Nessler S. A cell-cell communication system regulates protease production during sporulation in bacteria of the Bacillus cereus group Mol. Microbiol. 2011 82 619 633 10.1111/j.1365-2958.2011.07839.x 21958299

상세보기
54. Dubois T. Perchat S. Verplaetse E. Gominet M. Lemy C. Aumont-Nicaise M. Grenha R. Nessler S. Lereclus D. Activity of the Bacillus thuringiensis NprR-NprX cell-cell communication system is co-ordinated to the physiological stage through a complex transcriptional regulation Mol. Microbiol. 2013 88 48 63 10.1111/mmi.12168 23388036

상세보기
55. Dubois T. Etude du systeème de communication cellulaire NprR-NprX au sein du groupe Bacillus cereus Ph.D. Thesis AgroParisTech Jouy-en-Josas, France 5 3 2012 (In French)
56. Jiang M. Shao W. Perego M. Hoch J.A. Multiple histidine kinases regulate entry into stationary phase and sporulation in Bacillus subtilis Mol. Microbiol. 2000 38 535 542 10.1046/j.1365-2958.2000.02148.x 11069677

상세보기
57. Burbulys D. Trach K.A. Hoch J.A. Initiation of sporulation in Bacillus subtilis is controlled by a multicomponent phosphorelay Cell 1991 64 545 552 10.1016/0092-8674(91)90238-T 1846779

상세보기
58. Perego M. Glaser P. Hoch J.A. Aspartyl-phosphate phosphatases deactivate the response regulator components of the sporulation signal transduction system in Bacillus subtilis Mol. Microbiol. 1996 19 1151 1157 10.1111/j.1365-2958.1996.tb02460.x 8730857

상세보기
59. Fujita M. Losick R. Evidence that entry into sporulation in Bacillus subtilis is governed by a gradual increase in the level and activity of the master regulator Spo0A Genes Dev. 2005 19 2236 2244 10.1101/gad.1335705 16166384

상세보기
60. Core L. Perego M. TPR-mediated interaction of RapC with ComA inhibits response regulator-DNA binding for competence development in Bacillus subtilis Mol. Microbiol. 2003 49 1509 1522 10.1046/j.1365-2958.2003.03659.x 12950917

상세보기
61. Ishikawa S. Core L. Perego M. Biochemical characterization of aspartyl phosphate phosphatase interaction with a phosphorylated response regulator and its inhibition by a pentapeptide J. Biol. Chem. 2002 277 20483 20489 10.1074/jbc.M201086200 11923303

상세보기
62. Stephenson S. Mueller C. Jiang M. Perego M. Molecular analysis of Phr peptide processing in Bacillus subtilis J. Bacteriol. 2003 185 4861 4871 10.1128/JB.185.16.4861-4871.2003 12897006

상세보기
63. Lanigan-Gerdes S. Dooley A.N. Faull K.F. Lazazzera B.A. Identification of subtilisin, Epr and Vpr as enzymes that produce CSF, an extracellular signalling peptide of Bacillus subtilis Mol. Microbiol. 2007 65 1321 1333 10.1111/j.1365-2958.2007.05869.x 17666034

상세보기
64. Perego M. A peptide export-import control circuit modulating bacterial development regulates protein phosphatases of the phosphorelay Proc. Natl. Acad. Sci. USA 1997 94 8612 8617 10.1073/pnas.94.16.8612 9238025

상세보기
65. Perego M. Brannigan J.A. Pentapeptide regulation of aspartyl-phosphate phosphatases Peptides 2001 22 1541 1547 10.1016/S0196-9781(01)00490-9 11587783

상세보기
66. Mueller J.P. Bukusoglu G. Sonenshein A.L. Transcriptional regulation of Bacillus subtilis glucose starvation-inducible genes: Control of gsiA by the ComP-ComA signal transduction system J. Bacteriol. 1992 174 4361 4373 1378051
67. Molle V. Nakaura Y. Shivers R.P. Yamaguchi H. Losick R. Fujita Y. Sonenshein A.L. Additional targets of the Bacillus subtilis global regulator CodY identified by chromatin immunoprecipitation and genome-wide transcript analysis J. Bacteriol. 2003 185 1911 1922 10.1128/JB.185.6.1911-1922.2003 12618455

상세보기
68. McQuade R.S. Comella N. Grossman A.D. Control of a family of phosphatase regulatory genes(phr) by the alternate sigma factor sigma-H of Bacillus subtilis J. Bacteriol. 2001 183 4905 4909 10.1128/JB.183.16.4905-4909.2001 11466295

상세보기
69. Stephenson K. Hoch J.A. Evolution of signalling in the sporulation phosphorelay Mol. Microbiol. 2002 46 297 304 10.1046/j.1365-2958.2002.03186.x 12406209

상세보기
70. Tzeng Y.L. Hoch J.A. Molecular recognition in signal transduction: The interaction surfaces of the Spo0F response regulator with its cognate phosphorelay proteins revealed by alanine scanning mutagenesis J. Mol. Biol. 1997 272 200 212 10.1006/jmbi.1997.1226 9299348

상세보기
71. Zapf J. Sen U. Madhusudan Hoch J.A. Varughese K.I. A transient interaction between two phosphorelay proteins trapped in a crystal lattice reveals the mechanism of molecular recognition and phosphotransfer in signal transduction Structure 2000 8 851 862 10.1016/S0969-2126(00)00174-X 10997904

상세보기
72. Brunsing R.L. La Clair C. Tang S. Chiang C. Hancock L.E. Perego M. Hoch J.A. Characterization of sporulation histidine kinases of Bacillus anthracis J. Bacteriol. 2005 187 6972 6981 10.1128/JB.187.20.6972-6981.2005 16199567

상세보기
73. Bongiorni C. Stoessel R. Shoemaker D. Perego M. Rap phosphatase of virulence plasmid pXO1 inhibits Bacillus anthracis sporulation J. Bacteriol. 2006 188 487 498 10.1128/JB.188.2.487-498.2006 16385039

상세보기
74. Petersen T.N. Brunak S. von Heijne G. Nielsen H. SignalP 4.0: Discriminating signal peptides from transmembrane regions Nat. Methods 2011 8 785 786 10.1038/nmeth.1701 21959131

상세보기
75. Kall L. Krogh A. Sonnhammer E.L. Advantages of combined transmembrane topology and signal peptide prediction—The Phobius web server Nucl. Acids Res. 2007 35 W429 W432 10.1093/nar/gkm256 17483518

상세보기
76. Huillet E. Tempelaars M.H. Andre-Leroux G. Wanapaisan P. Bridoux L. Makhzami S. Panbangred W. Martin-Verstraete I. Abee T. Lereclus D. PlcRa, a new quorum-sensing regulator from Bacillus cereus , plays a role in oxidative stress responses and cysteine metabolism in stationary phase PLoS One 2012 7 e51047 23239999

상세보기
77. Tanous C. Soutourina O. Raynal B. Hullo M.F. Mervelet P. Gilles A.M. Noirot P. Danchin A. England P. Martin-Verstraete I. The CymR regulator in complex with the enzyme CysK controls cysteine metabolism in Bacillus subtilis J. Biol. Chem. 2008 283 35551 35560 10.1074/jbc.M805951200 18974048

상세보기
78. Zuber P. Management of oxidative stress in Bacillus Annu. Rev. Microbiol. 2009 63 575 597 10.1146/annurev.micro.091208.073241 19575568

상세보기
79. Mols M. Abee T. Primary and secondary oxidative stress in Bacillus Environ. Microbiol. 2011 13 1387 1394 10.1111/j.1462-2920.2011.02433.x 21352461

상세보기
80. Newton G.L. Rawat M. La Clair J.J. Jothivasan V.K. Budiarto T. Hamilton C.J. Claiborne A. Helmann J.D. Fahey R.C. Bacillithiol is an antioxidant thiol produced in Bacilli Nat. Chem. Biol. 2009 5 625 627 10.1038/nchembio.189 19578333

상세보기
81. Nicely N.I. Parsonage D. Paige C. Newton G.L. Fahey R.C. Leonardi R. Jackowski S. Mallett T.C. Claiborne A. Structure of the type III pantothenate kinase from Bacillus anthracis at 2.0 A resolution: Implications for coenzyme A-dependent redox biology Biochemistry 2007 46 3234 3245 10.1021/bi062299p 17323930

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용어 설명: PCR은 세균 특이성이 있는 primer를 이용하여 적은 수의 세균이 있을지라도 쉽게 검출할 수 있는 유용한 방법이며, 이를 이용하여 구강 내 치면세균막이나 타액에서 직접 세균을 검출할 수 있게 되었다[8].

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