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Volumn 197, Issue 14, 2015, Pages 2276-2283

Spore cortex hydrolysis precedes dipicolinic acid release during Clostridium difficile spore germination

Author keywords

[No Author keywords available]

Indexed keywords

BILE ACID; DIPICOLINIC ACID; GLYCINE RECEPTOR; BACTERIAL PROTEIN; CARRIER PROTEIN; CSPC PROTEIN, CLOSTRIDIUM; PICOLINIC ACID DERIVATIVE;

EID: 84932149860     PISSN: 00219193     EISSN: 10985530     Source Type: Journal    
DOI: 10.1128/JB.02575-14     Document Type: Article
Times cited : (79)

References (48)
  • 1
    • 84892894991 scopus 로고    scopus 로고
    • Antibiotic-induced shifts in the mouse gut microbiome and metabolome increase susceptibility to Clostridium difficile infection
    • Theriot CM, Koenigsknecht MJ, Carlson PE, Jr, Hatton GE, Nelson AM, Li B, Huffnagle GB, Li J, Young VB. 2014. Antibiotic-induced shifts in the mouse gut microbiome and metabolome increase susceptibility to Clostridium difficile infection. Nat Commun 5:3114. http://dx.doi.org/10.1038/ncomms4114.
    • (2014) Nat Commun , vol.5 , pp. 3114
    • Theriot, C.M.1    Koenigsknecht, M.J.2    Carlson, P.E.3    Hatton, G.E.4    Nelson, A.M.5    Li, B.6    Huffnagle, G.B.7    Li, J.8    Young, V.B.9
  • 4
    • 34547635096 scopus 로고    scopus 로고
    • Vegetative Clostridium difficile survives in room air on moist surfaces and in gastric contents with reduced acidity: a potential mechanism to explain the association between proton pump inhibitors and C. difficile-associated diarrhea?
    • Jump RLP, Pultz MJ, Donskey CJ. 2007. Vegetative Clostridium difficile survives in room air on moist surfaces and in gastric contents with reduced acidity: a potential mechanism to explain the association between proton pump inhibitors and C. difficile-associated diarrhea?. Antimicrob Agents Chemother 51:2883-2887. http://dx.doi.org/10.1128/AAC.01443-06.
    • (2007) Antimicrob Agents Chemother , vol.51 , pp. 2883-2887
    • Jump, R.L.P.1    Pultz, M.J.2    Donskey, C.J.3
  • 6
    • 84878518519 scopus 로고    scopus 로고
    • Bile acid recognition by the Clostridium difficile Germinant Receptor, CspC, is important for establishing infection
    • Francis MB, Allen CA, Shrestha R, Sorg JA. 2013. Bile acid recognition by the Clostridium difficile Germinant Receptor, CspC, is important for establishing infection. PLoS Pathog 9:e1003356. http://dx.doi.org/10.1371/journal.ppat.1003356.
    • (2013) PLoS Pathog , vol.9
    • Francis, M.B.1    Allen, C.A.2    Shrestha, R.3    Sorg, J.A.4
  • 7
    • 84903612457 scopus 로고    scopus 로고
    • Clostridium difficile spore biology: sporulation, germination, and spore structural proteins
    • Paredes-Sabja D, Shen A, Sorg JA. 2014. Clostridium difficile spore biology: sporulation, germination, and spore structural proteins. Trends Microbiol 22:406-416. http://dx.doi.org/10.1016/j.tim.2014.04.003.
    • (2014) Trends Microbiol , vol.22 , pp. 406-416
    • Paredes-Sabja, D.1    Shen, A.2    Sorg, J.A.3
  • 8
    • 84895725892 scopus 로고    scopus 로고
    • Germination of spores of Bacillus species: what we know and do not know
    • Setlow P. 2014. Germination of spores of Bacillus species: what we know and do not know. J Bacteriol 196:1297-1305. http://dx.doi.org/10.1128/JB.01455-13.
    • (2014) J Bacteriol , vol.196 , pp. 1297-1305
    • Setlow, P.1
  • 9
    • 84876198575 scopus 로고    scopus 로고
    • Molecular kinetics of reviving bacterial spores
    • Segev E, Rosenberg A, Mamou G, Sinai L, Ben-Yehuda S. 2013. Molecular kinetics of reviving bacterial spores. J Bacteriol 195:1875-1882. http://dx.doi.org/10.1128/JB.00093-13.
    • (2013) J Bacteriol , vol.195 , pp. 1875-1882
    • Segev, E.1    Rosenberg, A.2    Mamou, G.3    Sinai, L.4    Ben-Yehuda, S.5
  • 10
    • 41549142775 scopus 로고    scopus 로고
    • Bile salts and glycine as cogerminants for Clostridium difficile spores
    • Sorg JA, Sonenshein AL. 2008. Bile salts and glycine as cogerminants for Clostridium difficile spores. J Bacteriol 190:2505-2512. http://dx.doi.org/10.1128/JB.01765-07.
    • (2008) J Bacteriol , vol.190 , pp. 2505-2512
    • Sorg, J.A.1    Sonenshein, A.L.2
  • 11
    • 33244467651 scopus 로고    scopus 로고
    • Bile salt biotransformations by human intestinal bacteria
    • Ridlon JM, Kang D, Hylemon PB. 2006. Bile salt biotransformations by human intestinal bacteria. J Lipid Res 47:241-259. http://dx.doi.org/10.1194/jlr.R500013-JLR200.
    • (2006) J Lipid Res , vol.47 , pp. 241-259
    • Ridlon, J.M.1    Kang, D.2    Hylemon, P.B.3
  • 12
    • 77957337708 scopus 로고    scopus 로고
    • Inhibiting the initiation of Clostridium difficile spore germination using analogs of chenodeoxycholic acid, a bile acid
    • Sorg JA, Sonenshein AL. 2010. Inhibiting the initiation of Clostridium difficile spore germination using analogs of chenodeoxycholic acid, a bile acid. J Bacteriol 192:4983-4990. http://dx.doi.org/10.1128/JB.00610-10.
    • (2010) J Bacteriol , vol.192 , pp. 4983-4990
    • Sorg, J.A.1    Sonenshein, A.L.2
  • 13
    • 63449096364 scopus 로고    scopus 로고
    • Chenodeoxycholate is an inhibitor of Clostridium difficile spore germination
    • Sorg JA, Sonenshein AL. 2009. Chenodeoxycholate is an inhibitor of Clostridium difficile spore germination. J Bacteriol 191:1115-1117. http://dx.doi.org/10.1128/JB.01260-08.
    • (2009) J Bacteriol , vol.191 , pp. 1115-1117
    • Sorg, J.A.1    Sonenshein, A.L.2
  • 14
    • 77955975936 scopus 로고    scopus 로고
    • Kinetic evidence for the presence of putative germination receptors in Clostridium difficile spores
    • Ramirez N, Liggins M, Abel-Santos E. 2010. Kinetic evidence for the presence of putative germination receptors in Clostridium difficile spores. J Bacteriol 192:4215-4222. http://dx.doi.org/10.1128/JB.00488-10.
    • (2010) J Bacteriol , vol.192 , pp. 4215-4222
    • Ramirez, N.1    Liggins, M.2    Abel-Santos, E.3
  • 15
    • 84883621976 scopus 로고    scopus 로고
    • Muricholic acids inhibit Clostridium difficile spore germination and growth
    • Francis MB, Allen CA, Sorg JA. 2013. Muricholic acids inhibit Clostridium difficile spore germination and growth. PLoS One 8:e73653. http://dx.doi.org/10.1371/journal.pone.0073653.
    • (2013) PLoS One , vol.8
    • Francis, M.B.1    Allen, C.A.2    Sorg, J.A.3
  • 16
    • 34547640042 scopus 로고    scopus 로고
    • Structure, assembly, and function of the spore surface layers
    • Henriques AO, Moran CPJ. 2007. Structure, assembly, and function of the spore surface layers. Annu Rev Microbiol 61:555-588. http://dx.doi.org/10.1146/annurev.micro.61.080706.093224.
    • (2007) Annu Rev Microbiol , vol.61 , pp. 555-588
    • Henriques, A.O.1    Moran, C.P.J.2
  • 18
    • 75149112859 scopus 로고    scopus 로고
    • SleC is essential for germination of Clostridium difficile spores in nutrient-rich medium supplemented with the bile salt taurocholate
    • Burns DA, Heap JT, Minton NP. 2010. SleC is essential for germination of Clostridium difficile spores in nutrient-rich medium supplemented with the bile salt taurocholate. J Bacteriol 192:657-664. http://dx.doi.org/10.1128/JB.01209-09.
    • (2010) J Bacteriol , vol.192 , pp. 657-664
    • Burns, D.A.1    Heap, J.T.2    Minton, N.P.3
  • 19
    • 84891621197 scopus 로고    scopus 로고
    • Functional analysis of SleC from Clostridium difficile: an essential lytic transglycosylase involved in spore germination
    • Gutelius D, Hokeness K, Logan SM, Reid CW. 2014. Functional analysis of SleC from Clostridium difficile: an essential lytic transglycosylase involved in spore germination. Microbiology 160:209-216. http://dx.doi.org/10.1099/mic.0.072454-0.
    • (2014) Microbiology , vol.160 , pp. 209-216
    • Gutelius, D.1    Hokeness, K.2    Logan, S.M.3    Reid, C.W.4
  • 20
    • 84874760766 scopus 로고    scopus 로고
    • Structural and functional analysis of the CspB protease required for Clostridium spore germination
    • Adams CM, Eckenroth BE, Putnam EE, Doublie S, Shen A. 2013. Structural and functional analysis of the CspB protease required for Clostridium spore germination. PLoS Pathog 9:e1003165. http://dx.doi.org/10.1371/journal.ppat.1003165.
    • (2013) PLoS Pathog , vol.9
    • Adams, C.M.1    Eckenroth, B.E.2    Putnam, E.E.3    Doublie, S.4    Shen, A.5
  • 21
    • 33749653115 scopus 로고    scopus 로고
    • Expression of germination-related enzymes, CspA, CspB, CspC, SleC, and SleM, of Clostridium perfringens S40 in the mother cell compartment of sporulating cells
    • Masayama A, Hamasaki K, Urakami K, Shimamoto S, Kato S, Makino S, Yoshimura T, Moriyama M, Moriyama R. 2006. Expression of germination-related enzymes, CspA, CspB, CspC, SleC, and SleM, of Clostridium perfringens S40 in the mother cell compartment of sporulating cells. Genes Genet Syst 81:227-234. http://dx.doi.org/10.1266/ggs.81.227.
    • (2006) Genes Genet Syst , vol.81 , pp. 227-234
    • Masayama, A.1    Hamasaki, K.2    Urakami, K.3    Shimamoto, S.4    Kato, S.5    Makino, S.6    Yoshimura, T.7    Moriyama, M.8    Moriyama, R.9
  • 22
    • 0034981754 scopus 로고    scopus 로고
    • Partial characterization of an enzyme fraction with protease activity which converts the spore peptidoglycan hydrolase (SleC) precursor to an active enzyme during germination of Clostridium perfringens S40 spores and analysis of a gene cluster involved in the activity
    • Shimamoto S, Moriyama R, Sugimoto K, Miyata S, Makino S. 2001. Partial characterization of an enzyme fraction with protease activity which converts the spore peptidoglycan hydrolase (SleC) precursor to an active enzyme during germination of Clostridium perfringens S40 spores and analysis of a gene cluster involved in the activity. J Bacteriol 183:3742-3751. http://dx.doi.org/10.1128/JB.183.12.3742-3751.2001.
    • (2001) J Bacteriol , vol.183 , pp. 3742-3751
    • Shimamoto, S.1    Moriyama, R.2    Sugimoto, K.3    Miyata, S.4    Makino, S.5
  • 23
    • 65249186376 scopus 로고    scopus 로고
    • SleC is essential for cortex peptidoglycan hydrolysis during germination of spores of the pathogenic bacterium Clostridium perfringens
    • Paredes-Sabja D, Setlow P, Sarker MR. 2009. SleC is essential for cortex peptidoglycan hydrolysis during germination of spores of the pathogenic bacterium Clostridium perfringens. J Bacteriol 191:2711-2720. http://dx.doi.org/10.1128/JB.01832-08.
    • (2009) J Bacteriol , vol.191 , pp. 2711-2720
    • Paredes-Sabja, D.1    Setlow, P.2    Sarker, M.R.3
  • 25
    • 34247260039 scopus 로고    scopus 로고
    • Isolation and characterisation of toxin A-negative, toxin B-positive Clostridium difficile in Dublin, Ireland
    • Drudy D, Harnedy N, Fanning S, O'Mahony R, Kyne L. 2007. Isolation and characterisation of toxin A-negative, toxin B-positive Clostridium difficile in Dublin, Ireland. Clin Microbiol Infect 13:298-304. http://dx.doi.org/10.1111/j.1469-0691.2006.01634.x.
    • (2007) Clin Microbiol Infect , vol.13 , pp. 298-304
    • Drudy, D.1    Harnedy, N.2    Fanning, S.3    O'Mahony, R.4    Kyne, L.5
  • 29
    • 84872023885 scopus 로고    scopus 로고
    • Both fidaxomicin and vancomycin inhibit outgrowth of Clostridium difficile spores
    • Allen CA, Babakhani F, Sears P, Nguyen L, Sorg JA. 2013. Both fidaxomicin and vancomycin inhibit outgrowth of Clostridium difficile spores. Antimicrob Agents Chemother 57:664-667. http://dx.doi.org/10.1128/AAC.01611-12.
    • (2013) Antimicrob Agents Chemother , vol.57 , pp. 664-667
    • Allen, C.A.1    Babakhani, F.2    Sears, P.3    Nguyen, L.4    Sorg, J.A.5
  • 30
    • 0001864545 scopus 로고
    • Sporulation, germination and outgrowth
    • John Wiley, Chichester, United Kingdom
    • Nicholson WL, Setlow P. 1990. Sporulation, germination and outgrowth, p 391-450. In Molecular biological methods for Bacillus. John Wiley, Chichester, United Kingdom.
    • (1990) Molecular biological methods for Bacillus , pp. 391-450
    • Nicholson, W.L.1    Setlow, P.2
  • 31
    • 0032723232 scopus 로고    scopus 로고
    • Dipicolinic acid (DPA) assay revisited and appraised for spore detection
    • Hindle AA, Hall EA. 1999. Dipicolinic acid (DPA) assay revisited and appraised for spore detection. Analyst 124:1599-1604. http://dx.doi.org/10.1039/a906846e.
    • (1999) Analyst , vol.124 , pp. 1599-1604
    • Hindle, A.A.1    Hall, E.A.2
  • 32
    • 70349421685 scopus 로고    scopus 로고
    • The protease CspB is essential for initiation of cortex hydrolysis and dipicolinic acid (DPA) release during germination of spores of Clostridium perfringens type A food poisoning isolates
    • Paredes-Sabja D, Setlow P, Sarker MR. 2009. The protease CspB is essential for initiation of cortex hydrolysis and dipicolinic acid (DPA) release during germination of spores of Clostridium perfringens type A food poisoning isolates. Microbiology 155:3464-3472. http://dx.doi.org/10.1099/mic.0.030965-0.
    • (2009) Microbiology , vol.155 , pp. 3464-3472
    • Paredes-Sabja, D.1    Setlow, P.2    Sarker, M.R.3
  • 33
    • 77957009247 scopus 로고
    • Enzymes that degrade bacterial cell walls
    • Ghuysen J-M, Tipper DJ, Strominger JL. 1966. Enzymes that degrade bacterial cell walls. Methods Enzymol 8:685-699. http://dx.doi.org/10.1016/0076-6879(66)08124-2.
    • (1966) Methods Enzymol , vol.8 , pp. 685-699
    • Ghuysen, J.-M.1    Tipper, D.J.2    Strominger, J.L.3
  • 34
    • 79952502699 scopus 로고    scopus 로고
    • Combination of Raman tweezers and quantitative differential interference contrast microscopy for measurement of dynamics and heterogeneity during the germination of individual bacterial spores
    • Zhang P, Kong L, Wang G, Setlow P, Li YQ. 2010. Combination of Raman tweezers and quantitative differential interference contrast microscopy for measurement of dynamics and heterogeneity during the germination of individual bacterial spores. J Biomed Optics 15:056010. http://dx.doi.org/10.1117/1.3494567.
    • (2010) J Biomed Optics , vol.15
    • Zhang, P.1    Kong, L.2    Wang, G.3    Setlow, P.4    Li, Y.Q.5
  • 35
    • 22144452584 scopus 로고    scopus 로고
    • Assessment of heat resistance of bacterial spores from food product isolates by fluorescence monitoring of dipicolinic acid release
    • Kort R, O'Brien AC, van Stokkum IH, Oomes SJ, Crielaard W, Hellingwerf KJ, Brul S. 2005. Assessment of heat resistance of bacterial spores from food product isolates by fluorescence monitoring of dipicolinic acid release. Appl Environ Microbiol 71:3556-3564. http://dx.doi.org/10.1128/AEM.71.7.3556-3564.2005.
    • (2005) Appl Environ Microbiol , vol.71 , pp. 3556-3564
    • Kort, R.1    O'Brien, A.C.2    van Stokkum, I.H.3    Oomes, S.J.4    Crielaard, W.5    Hellingwerf, K.J.6    Brul, S.7
  • 36
    • 69949107820 scopus 로고    scopus 로고
    • Superdormant spores of Bacillus species have elevated wet-heat resistance and temperature requirements for heat activation
    • Ghosh S, Zhang P, Li YQ, Setlow P. 2009. Superdormant spores of Bacillus species have elevated wet-heat resistance and temperature requirements for heat activation. J Bacteriol 191:5584-5591. http://dx.doi.org/10.1128/JB.00736-09.
    • (2009) J Bacteriol , vol.191 , pp. 5584-5591
    • Ghosh, S.1    Zhang, P.2    Li, Y.Q.3    Setlow, P.4
  • 37
    • 84857472906 scopus 로고    scopus 로고
    • Spores of Clostridium difficile clinical isolates display a diverse germination response to bile salts
    • Heeg D, Burns DA, Cartman ST, Minton NP. 2012. Spores of Clostridium difficile clinical isolates display a diverse germination response to bile salts. PLoS One 7:e32381. http://dx.doi.org/10.1371/journal.pone.0032381.
    • (2012) PLoS One , vol.7
    • Heeg, D.1    Burns, D.A.2    Cartman, S.T.3    Minton, N.P.4
  • 38
    • 84922748691 scopus 로고    scopus 로고
    • Variation in germination of Clostridium difficile clinical isolates correlates to disease severity
    • Carlson PE, Jr, Kaiser AM, McColm SA, Bauer JM, Young VB, Aronoff DM, Hanna PC. 2015. Variation in germination of Clostridium difficile clinical isolates correlates to disease severity. Anaerobe 33:64-70. http://dx.doi.org/10.1016/j.anaerobe.2015.02.003.
    • (2015) Anaerobe , vol.33 , pp. 64-70
    • Carlson, P.E.1    Kaiser, A.M.2    McColm, S.A.3    Bauer, J.M.4    Young, V.B.5    Aronoff, D.M.6    Hanna, P.C.7
  • 39
    • 0020084325 scopus 로고
    • Use of sodium taurocholate to enhance spore recovery on a medium selective for Clostridium difficile
    • Wilson KH, Kennedy MJ, Fekety FR. 1982. Use of sodium taurocholate to enhance spore recovery on a medium selective for Clostridium difficile. J Clin Microbiol 15:443-446.
    • (1982) J Clin Microbiol , vol.15 , pp. 443-446
    • Wilson, K.H.1    Kennedy, M.J.2    Fekety, F.R.3
  • 40
    • 0016147148 scopus 로고
    • (Sodium taurocholate, a germination factor for anaerobic bacterial spores "in vitro" and "in vivo"
    • (Author's translation.)
    • Railbaud P, Ducluzeau R, Muller MC, Sacquet E. 1974. (Sodium taurocholate, a germination factor for anaerobic bacterial spores "in vitro" and "in vivo." Ann Microbiol 125B:381-391. (Author's translation.).
    • (1974) Ann Microbiol , vol.125B , pp. 381-391
    • Railbaud, P.1    Ducluzeau, R.2    Muller, M.C.3    Sacquet, E.4
  • 41
    • 38949090419 scopus 로고    scopus 로고
    • Clostridium perfringens spore germination: characterization of germinants and their receptors
    • Paredes-Sabja D, Torres JA, Setlow P, Sarker MR. 2008. Clostridium perfringens spore germination: characterization of germinants and their receptors. J Bacteriol 190:1190-1201. http://dx.doi.org/10.1128/JB.01748-07.
    • (2008) J Bacteriol , vol.190 , pp. 1190-1201
    • Paredes-Sabja, D.1    Torres, J.A.2    Setlow, P.3    Sarker, M.R.4
  • 42
    • 70349416523 scopus 로고    scopus 로고
    • Inorganic phosphate and sodium ions are cogerminants for spores of Clostridium perfringens type A food poisoning-related isolates
    • Paredes-Sabja D, Udompijitkul P, Sarker MR. 2009. Inorganic phosphate and sodium ions are cogerminants for spores of Clostridium perfringens type A food poisoning-related isolates. Appl Environ Microbiol 75: 6299-6305. http://dx.doi.org/10.1128/AEM.00822-09.
    • (2009) Appl Environ Microbiol , vol.75 , pp. 6299-6305
    • Paredes-Sabja, D.1    Udompijitkul, P.2    Sarker, M.R.3
  • 43
    • 67349152920 scopus 로고    scopus 로고
    • Levels and localization of mechanosensitive channel proteins in Bacillus subtilis
    • Wahome PG, Cowan AE, Setlow B, Setlow P. 2009. Levels and localization of mechanosensitive channel proteins in Bacillus subtilis. Arch Microbiol 191:403-414. http://dx.doi.org/10.1007/s00203-009-0465-z.
    • (2009) Arch Microbiol , vol.191 , pp. 403-414
    • Wahome, P.G.1    Cowan, A.E.2    Setlow, B.3    Setlow, P.4
  • 44
    • 33750740748 scopus 로고    scopus 로고
    • The synthesis and role of the mechanosensitive channel of large conductance in growth and differentiation of Bacillus subtilis
    • Wahome PG, Setlow P. 2006. The synthesis and role of the mechanosensitive channel of large conductance in growth and differentiation of Bacillus subtilis. Arch Microbiol 186:377-383. http://dx.doi.org/10.1007/s00203-006-0152-2.
    • (2006) Arch Microbiol , vol.186 , pp. 377-383
    • Wahome, P.G.1    Setlow, P.2
  • 45
    • 36349035531 scopus 로고    scopus 로고
    • Growth, osmotic downshock resistance and differentiation of Bacillus subtilis strains lacking mechanosensitive channels
    • Wahome PG, Setlow P. 2008. Growth, osmotic downshock resistance and differentiation of Bacillus subtilis strains lacking mechanosensitive channels. Arch Microbiol 189:49-58.
    • (2008) Arch Microbiol , vol.189 , pp. 49-58
    • Wahome, P.G.1    Setlow, P.2
  • 46
    • 33947369915 scopus 로고    scopus 로고
    • Role of SpoVA proteins in release of dipicolinic acid during germination of Bacillus subtilis spores triggered by dodecylamine or lysozyme
    • Vepachedu VR, Setlow P. 2007. Role of SpoVA proteins in release of dipicolinic acid during germination of Bacillus subtilis spores triggered by dodecylamine or lysozyme. J Bacteriol 189:1565-1572. http://dx.doi.org/10.1128/JB.01613-06.
    • (2007) J Bacteriol , vol.189 , pp. 1565-1572
    • Vepachedu, V.R.1    Setlow, P.2
  • 47
    • 84861213261 scopus 로고    scopus 로고
    • Role of a SpoVA protein in dipicolinic acid uptake into developing spores of Bacillus subtilis
    • Li Y, Davis A, Korza G, Zhang P, Li YQ, Setlow B, Setlow P, Hao B. 2012. Role of a SpoVA protein in dipicolinic acid uptake into developing spores of Bacillus subtilis. J Bacteriol 194:1875-1884. http://dx.doi.org/10.1128/JB.00062-12.
    • (2012) J Bacteriol , vol.194 , pp. 1875-1884
    • Li, Y.1    Davis, A.2    Korza, G.3    Zhang, P.4    Li, Y.Q.5    Setlow, B.6    Setlow, P.7    Hao, B.8
  • 48
    • 84899902629 scopus 로고    scopus 로고
    • Bacillus subtilis spore protein SpoVAC functions as a mechanosensitive channel
    • Velasquez J, Schuurman-Wolters G, Birkner JP, Abee T, Poolman B. 2014. Bacillus subtilis spore protein SpoVAC functions as a mechanosensitive channel. Mol Microbiol 92:813-823. http://dx.doi.org/10.1111/mmi.12591.
    • (2014) Mol Microbiol , vol.92 , pp. 813-823
    • Velasquez, J.1    Schuurman-Wolters, G.2    Birkner, J.P.3    Abee, T.4    Poolman, B.5


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