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Infection and Immunity
Volumn 83, Issue 4, 2015, Pages 1339-1346
Type IV pilus glycosylation mediates resistance of Pseudomonas aeruginosa to opsonic activities of the pulmonary surfactant protein A
Author keywords

[No Author keywords available]
Indexed keywords

MANNOSE BINDING LECTIN 2; O ANTIGEN; OPSONIN; PILIN; SURFACTANT PROTEIN A; SURFACTANT PROTEIN D; GLYCOSYLTRANSFERASE; MANNOSE BINDING LECTIN; O ANTIGEN, PSEUDOMONAS;
EID: 84925355236     PISSN: 00199567     EISSN: 10985522     Source Type: Journal    
DOI: 10.1128/IAI.02874-14     Document Type: Article
Times cited : (28)
References (56)
  • 2
    • 68649125562 scopus 로고    scopus 로고
    • The relevance of the polymicrobial nature of airway infection in the acute and chronic management of patients with cystic fibrosis
    • Sibley CD, Parkins MD, Rabin HR, Surette MG. 2009. The relevance of the polymicrobial nature of airway infection in the acute and chronic management of patients with cystic fibrosis. Curr Opin Investig Drugs 10:787-794.
    • (2009) Curr Opin Investig Drugs , vol.10 , pp. 787-794
    • Sibley, C.D.1    Parkins, M.D.2    Rabin, H.R.3    Surette, M.G.4
  • 3
    • 77649255036 scopus 로고    scopus 로고
    • Respiratory infection in noncystic fibrosis bronchiectasis
    • Zoumot Z, Wilson R. 2010. Respiratory infection in noncystic fibrosis bronchiectasis. Curr Opin Infect Dis 23:165-170. http://dx.doi.org/10.1097/QCO.0b013e328335af91.
    • (2010) Curr Opin Infect Dis , vol.23 , pp. 165-170
    • Zoumot, Z.1    Wilson, R.2
  • 4
    • 78650018649 scopus 로고    scopus 로고
    • Differential adaptation of microbial pathogens to airways of patients with cystic fibrosis and chronic obstructive pulmonary disease
    • Döring G, Parameswaran IG, Murphy TF. 2011. Differential adaptation of microbial pathogens to airways of patients with cystic fibrosis and chronic obstructive pulmonary disease. FEMS Microbiol Rev 35:124-146. http://dx.doi.org/10.1111/j.1574-6976.2010.00237.x.
    • (2011) FEMS Microbiol Rev , vol.35 , pp. 124-146
    • Döring, G.1    Parameswaran, I.G.2    Murphy, T.F.3
  • 5
    • 84864092949 scopus 로고    scopus 로고
    • Pseudomonas aeruginosa outbreaks in the neonatal intensive care unit-a systematic review of risk factors and environmental sources
    • Jefferies JM, Cooper T, Yam T, Clarke SC. 2012. Pseudomonas aeruginosa outbreaks in the neonatal intensive care unit-a systematic review of risk factors and environmental sources. J Med Microbiol 61(Pt 8):1052-1061. http://dx.doi.org/10.1099/jmm.0.044818-0.
    • (2012) J Med Microbiol , vol.61 , pp. 1052-1061
    • Jefferies, J.M.1    Cooper, T.2    Yam, T.3    Clarke, S.C.4
  • 6
    • 84866416261 scopus 로고    scopus 로고
    • Current dilemmas in antimicrobial therapy in cystic fibrosis
    • Jain K, Smyth AR. 2012. Current dilemmas in antimicrobial therapy in cystic fibrosis. Expert Rev Respir Med 6:407-422. http://dx.doi.org/10.1586/ers.12.39.
    • (2012) Expert Rev Respir Med , vol.6 , pp. 407-422
    • Jain, K.1    Smyth, A.R.2
  • 7
    • 2442589577 scopus 로고    scopus 로고
    • Type IV pilus structure and bacterial pathogenicity
    • Craig L, Pique ME, Tainer JA. 2004. Type IV pilus structure and bacterial pathogenicity. Nat Rev Microbiol 2:363-378. http://dx.doi.org/10.1038/nrmicro885.
    • (2004) Nat Rev Microbiol , vol.2 , pp. 363-378
    • Craig, L.1    Pique, M.E.2    Tainer, J.A.3
  • 8
    • 0028920724 scopus 로고
    • Role of Pseudomonas aeruginosa pili in acute pulmonary infection
    • Tang H, Kays M, Prince A. 1995. Role of Pseudomonas aeruginosa pili in acute pulmonary infection. Infect Immun 63:1278-1285.
    • (1995) Infect Immun , vol.63 , pp. 1278-1285
    • Tang, H.1    Kays, M.2    Prince, A.3
  • 9
    • 0028121070 scopus 로고
    • Differentiation of Pseudomonas aeruginosa pili based on sequence and B-cell epitope analyses
    • Castric PA, Deal CD. 1994. Differentiation of Pseudomonas aeruginosa pili based on sequence and B-cell epitope analyses. Infect Immun 62:371-376.
    • (1994) Infect Immun , vol.62 , pp. 371-376
    • Castric, P.A.1    Deal, C.D.2
  • 10
    • 2942614967 scopus 로고    scopus 로고
    • Significant differences in type IV pilin allele distribution among Pseudomonas aeruginosa isolates from cystic fibrosis (CF) versus non-CF patients
    • Kus JV, Tullis E, Cvitkovitch DG, Burrows LL. 2004. Significant differences in type IV pilin allele distribution among Pseudomonas aeruginosa isolates from cystic fibrosis (CF) versus non-CF patients. Microbiology 150(Pt 5):1315-1326. http://dx.doi.org/10.1099/mic.0.26822-0.
    • (2004) Microbiology , vol.150 , pp. 1315-1326
    • Kus, J.V.1    Tullis, E.2    Cvitkovitch, D.G.3    Burrows, L.L.4
  • 11
    • 28444450504 scopus 로고    scopus 로고
    • Influence of pilin glycosylation on Pseudomonas aeruginosa 1244 pilus function
    • Smedley JG, III, Jewell E, Roguskie J, Horzempa J, Syboldt A, Stolz DB, Castric P. 2005. Influence of pilin glycosylation on Pseudomonas aeruginosa 1244 pilus function. Infect Immun 73:7922-7931. http://dx.doi.org/10.1128/IAI.73.12.7922-7931.2005.
    • (2005) Infect Immun , vol.73 , pp. 7922-7931
    • Smedley, J.G.1    Jewell, E.2    Roguskie, J.3    Horzempa, J.4    Syboldt, A.5    Stolz, D.B.6    Castric, P.7
  • 12
    • 33845940986 scopus 로고    scopus 로고
    • Glycosylation of Pseudomonas aeruginosa strain Pa5196 type IV pilins with Mycobacterium-like alpha-1,5-linked D-Araf oligosaccharides
    • Voisin S, Kus JV, Houliston S, St-Michael F, Watson D, Cvitkovitch DG, Kelly J, Brisson JR, Burrows LL. 2007. Glycosylation of Pseudomonas aeruginosa strain Pa5196 type IV pilins with Mycobacterium-like alpha-1,5-linked D-Araf oligosaccharides. J Bacteriol 189:151-159. http://dx.doi.org/10.1128/JB.01224-06.
    • (2007) J Bacteriol , vol.189 , pp. 151-159
    • Voisin, S.1    Kus, J.V.2    Houliston, S.3    St-Michael, F.4    Watson, D.5    Cvitkovitch, D.G.6    Kelly, J.7    Brisson, J.R.8    Burrows, L.L.9
  • 13
    • 80051485101 scopus 로고    scopus 로고
    • Pseudomonas aeruginosa D-arabinofuranose biosynthetic pathway and its role in type IV pilus assembly
    • Harvey H, Kus JV, Tessier L, Kelly J, Burrows LL. 2011. Pseudomonas aeruginosa D-arabinofuranose biosynthetic pathway and its role in type IV pilus assembly. J Biol Chem 286:28128-28137. http://dx.doi.org/10.1074/jbc.M111.255794.
    • (2011) J Biol Chem , vol.286 , pp. 28128-28137
    • Harvey, H.1    Kus, J.V.2    Tessier, L.3    Kelly, J.4    Burrows, L.L.5
  • 14
    • 55749098829 scopus 로고    scopus 로고
    • Novel proteins that modulate type IV pilus retraction dynamics in Pseudomonas aeruginosa
    • Asikyan ML, Kus JV, Burrows LL. 2008. Novel proteins that modulate type IV pilus retraction dynamics in Pseudomonas aeruginosa. J Bacteriol 190:7022-7034. http://dx.doi.org/10.1128/JB.00938-08.
    • (2008) J Bacteriol , vol.190 , pp. 7022-7034
    • Asikyan, M.L.1    Kus, J.V.2    Burrows, L.L.3
  • 15
    • 78650778360 scopus 로고    scopus 로고
    • Evolutionary and functional diversity of the Pseudomonas type IVa pilin island
    • Giltner CL, Rana N, Lunardo MN, Hussain AQ, Burrows LL. 2011. Evolutionary and functional diversity of the Pseudomonas type IVa pilin island. Environ Microbiol 13:250-264. http://dx.doi.org/10.1111/j.1462-2920.2010.02327.x.
    • (2011) Environ Microbiol , vol.13 , pp. 250-264
    • Giltner, C.L.1    Rana, N.2    Lunardo, M.N.3    Hussain, A.Q.4    Burrows, L.L.5
  • 16
    • 0035854812 scopus 로고    scopus 로고
    • Structural characterization of the Pseudomonas aeruginosa 1244 pilin glycan
    • Castric P, Cassels FJ, Carlson RW. 2001. Structural characterization of the Pseudomonas aeruginosa 1244 pilin glycan. J Biol Chem 276:26479-26485. http://dx.doi.org/10.1074/jbc.M102685200.
    • (2001) J Biol Chem , vol.276 , pp. 26479-26485
    • Castric, P.1    Cassels, F.J.2    Carlson, R.W.3
  • 17
    • 0036265917 scopus 로고    scopus 로고
    • Identification of the Pseudomonas aeruginosa 1244 pilin glycosylation site
    • Comer JE, Marshall MA, Blanch VJ, Deal CD, Castric P. 2002. Identification of the Pseudomonas aeruginosa 1244 pilin glycosylation site. Infect Immun 70:2837-2845. http://dx.doi.org/10.1128/IAI.70.6.2837-2845.2002.
    • (2002) Infect Immun , vol.70 , pp. 2837-2845
    • Comer, J.E.1    Marshall, M.A.2    Blanch, V.J.3    Deal, C.D.4    Castric, P.5
  • 18
    • 0036431682 scopus 로고    scopus 로고
    • Glycosylation of Pseudomonas aeruginosa 1244 pilin: glycan substrate specificity
    • DiGiandomenico A, Matewish MJ, Bisaillon A, Stehle JR, Lam JS, Castric P. 2002. Glycosylation of Pseudomonas aeruginosa 1244 pilin: glycan substrate specificity. Mol Microbiol 46:519-530. http://dx.doi.org/10.1046/j.1365-2958.2002.03171.x.
    • (2002) Mol Microbiol , vol.46 , pp. 519-530
    • DiGiandomenico, A.1    Matewish, M.J.2    Bisaillon, A.3    Stehle, J.R.4    Lam, J.S.5    Castric, P.6
  • 19
    • 0036154486 scopus 로고    scopus 로고
    • Identification of virulence genes in a pathogenic strain of Pseudomonas aeruginosa by representational difference analysis
    • Choi JY, Sifri CD, Goumnerov BC, Rahme LG, Ausubel FM, Calderwood SB. 2002. Identification of virulence genes in a pathogenic strain of Pseudomonas aeruginosa by representational difference analysis. J Bacteriol 184:952-961. http://dx.doi.org/10.1128/jb.184.4.952-961.2002.
    • (2002) J Bacteriol , vol.184 , pp. 952-961
    • Choi, J.Y.1    Sifri, C.D.2    Goumnerov, B.C.3    Rahme, L.G.4    Ausubel, F.M.5    Calderwood, S.B.6
  • 20
    • 10744225048 scopus 로고    scopus 로고
    • The broad host range pathogen Pseudomonas aeruginosa strain PA14 carries two pathogenicity islands harboring plant and animal virulence genes
    • He J, Baldini RL, Déziel E, Saucier M, Zhang Q, Liberati NT, Lee D, Urbach J, Goodman HM, Rahme LG. 2004. The broad host range pathogen Pseudomonas aeruginosa strain PA14 carries two pathogenicity islands harboring plant and animal virulence genes. Proc Natl Acad Sci U S A 101:2530-2535. http://dx.doi.org/10.1073/pnas.0304622101.
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 2530-2535
    • He, J.1    Baldini, R.L.2    Déziel, E.3    Saucier, M.4    Zhang, Q.5    Liberati, N.T.6    Lee, D.7    Urbach, J.8    Goodman, H.M.9    Rahme, L.G.10
  • 21
    • 77950217695 scopus 로고    scopus 로고
    • Pathogenicity islands PAPI-1 and PAPI-2 contribute individually and synergistically to the virulence of Pseudomonas aeruginosa strain PA14
    • Harrison EM, Carter ME, Luck S, Ou HY, He X, Deng Z, O'Callaghan C, Kadioglu A, Rajakumar K. 2010. Pathogenicity islands PAPI-1 and PAPI-2 contribute individually and synergistically to the virulence of Pseudomonas aeruginosa strain PA14. Infect Immun 78:1437-1446. http://dx.doi.org/10.1128/IAI.00621-09.
    • (2010) Infect Immun , vol.78 , pp. 1437-1446
    • Harrison, E.M.1    Carter, M.E.2    Luck, S.3    Ou, H.Y.4    He, X.5    Deng, Z.6    O'Callaghan, C.7    Kadioglu, A.8    Rajakumar, K.9
  • 22
    • 84896375051 scopus 로고    scopus 로고
    • Type IV pilus of Pseudomonas aeruginosa confers resistance to antimicrobial activities of the pulmonary surfactant protein-A
    • Tan RM, Kuang Z, Hao Y, Lau GW. 2014. Type IV pilus of Pseudomonas aeruginosa confers resistance to antimicrobial activities of the pulmonary surfactant protein-A. J Innate Immun 6:227-239. http://dx.doi.org/10.1159/000354304.
    • (2014) J Innate Immun , vol.6 , pp. 227-239
    • Tan, R.M.1    Kuang, Z.2    Hao, Y.3    Lau, G.W.4
  • 23
    • 0035979193 scopus 로고    scopus 로고
    • A genomic island in Pseudomonas aeruginosa carries the determinants of flagellin glycosylation
    • Arora S, Bangera M, Lory S, Ramphal R. 2001. A genomic island in Pseudomonas aeruginosa carries the determinants of flagellin glycosylation. Proc Natl Acad Sci U S A 98:9342-9347. http://dx.doi.org/10.1073/pnas.161249198.
    • (2001) Proc Natl Acad Sci U S A , vol.98 , pp. 9342-9347
    • Arora, S.1    Bangera, M.2    Lory, S.3    Ramphal, R.4
  • 24
    • 33748655463 scopus 로고    scopus 로고
    • Comparative signature-tagged mutagenesis identifies Pseudomonas factors conferring resistance to the pulmonary collectin SP-A
    • Zhang S, Chen Y, Potvin E, Sanschagrin F, Levesque RC, McCormack FX, Lau GW. 2005. Comparative signature-tagged mutagenesis identifies Pseudomonas factors conferring resistance to the pulmonary collectin SP-A. PLoS Pathog 1:259-268.
    • (2005) PLoS Pathog , vol.1 , pp. 259-268
    • Zhang, S.1    Chen, Y.2    Potvin, E.3    Sanschagrin, F.4    Levesque, R.C.5    McCormack, F.X.6    Lau, G.W.7
  • 25
    • 4544364520 scopus 로고    scopus 로고
    • Effect of subinhibitory concentration of piperacillin-tazobactam on Pseudomonas aeruginosa
    • Fonseca AP, Extremina C, Fonseca AF, Sousa JC. 2004. Effect of subinhibitory concentration of piperacillin-tazobactam on Pseudomonas aeruginosa. J Med Microbiol 53(Pt 9):903-910. http://dx.doi.org/10.1099/jmm.0.45637-0.
    • (2004) J Med Microbiol , vol.53 , pp. 903-910
    • Fonseca, A.P.1    Extremina, C.2    Fonseca, A.F.3    Sousa, J.C.4
  • 27
    • 0029967458 scopus 로고    scopus 로고
    • Calcium-dependent association of surfactant protein A with pulmonary surfactant: application to simple surfactant protein A purification
    • Suwabe A, Mason RJ, Voelker DR. 1996. Calcium-dependent association of surfactant protein A with pulmonary surfactant: application to simple surfactant protein A purification. Arch Biochem Biophys 327:285-291. http://dx.doi.org/10.1006/abbi.1996.0123.
    • (1996) Arch Biochem Biophys , vol.327 , pp. 285-291
    • Suwabe, A.1    Mason, R.J.2    Voelker, D.R.3
  • 28
    • 80055117047 scopus 로고    scopus 로고
    • Pseudomonas aeruginosa elastase provides an escape from phagocytosis by degrading the pulmonary surfactant protein-A
    • Kuang Z, Hao Y, Walling BE, Jeffries JL, Ohman DE, Lau GW. 2011. Pseudomonas aeruginosa elastase provides an escape from phagocytosis by degrading the pulmonary surfactant protein-A. PLoS One 6:e27091. http://dx.doi.org/10.1371/journal.pone.0027091.
    • (2011) PLoS One , vol.6
    • Kuang, Z.1    Hao, Y.2    Walling, B.E.3    Jeffries, J.L.4    Ohman, D.E.5    Lau, G.W.6
  • 29
    • 85047690807 scopus 로고    scopus 로고
    • Surfactant proteins A and D inhibit the growth of Gram-negative bacteria by increasing membrane permeability
    • Wu H, Kuzmenko A, Wan S, Schaffer L, Weiss A, Fisher JH, Kim KS, McCormack FX. 2003. Surfactant proteins A and D inhibit the growth of Gram-negative bacteria by increasing membrane permeability. J Clin Invest 111:1589-1602. http://dx.doi.org/10.1172/JCI16889.
    • (2003) J Clin Invest , vol.111 , pp. 1589-1602
    • Wu, H.1    Kuzmenko, A.2    Wan, S.3    Schaffer, L.4    Weiss, A.5    Fisher, J.H.6    Kim, K.S.7    McCormack, F.X.8
  • 30
    • 0035048532 scopus 로고    scopus 로고
    • Surfactant proteins a and d and pulmonary host defense
    • Crouch E, Wright JR. 2001. Surfactant proteins a and d and pulmonary host defense. Annu Rev Physiol 63:521-554. http://dx.doi.org/10.1146/annurev.physiol.63.1.521.
    • (2001) Annu Rev Physiol , vol.63 , pp. 521-554
    • Crouch, E.1    Wright, J.R.2
  • 31
    • 11244287371 scopus 로고    scopus 로고
    • Immunoregulatory functions of surfactant proteins
    • Wright JR. 2005. Immunoregulatory functions of surfactant proteins. Nat Rev Immunol 5:58-68. http://dx.doi.org/10.1038/nri1528.
    • (2005) Nat Rev Immunol , vol.5 , pp. 58-68
    • Wright, J.R.1
  • 32
    • 79951782204 scopus 로고    scopus 로고
    • The Pseudomonas aeruginosa flagellum confers resistance to pulmonary surfactant protein A by impacting the production of exoproteases through quorum-sensing
    • Kuang Z, Hao Y, Hwang S, Zhang S, Kim E, Akinbi HT, Schurr MJ, Irvin RT, Hassett DJ, Lau GW. 2011. The Pseudomonas aeruginosa flagellum confers resistance to pulmonary surfactant protein A by impacting the production of exoproteases through quorum-sensing. Mol Microbiol 79:1220-1235. http://dx.doi.org/10.1111/j.1365-2958.2010.07516.x.
    • (2011) Mol Microbiol , vol.79 , pp. 1220-1235
    • Kuang, Z.1    Hao, Y.2    Hwang, S.3    Zhang, S.4    Kim, E.5    Akinbi, H.T.6    Schurr, M.J.7    Irvin, R.T.8    Hassett, D.J.9    Lau, G.W.10
  • 33
    • 26044483536 scopus 로고    scopus 로고
    • C-reactive protein: ligands, receptors and role in inflammation
    • Marnell L, Mold C, Du Clos TW. 2005. C-reactive protein: ligands, receptors and role in inflammation. Clin Immunol 117:104-111. http://dx.doi.org/10.1016/j.clim.2005.08.004.
    • (2005) Clin Immunol , vol.117 , pp. 104-111
    • Marnell, L.1    Mold, C.2    Du Clos, T.W.3
  • 34
    • 34447631692 scopus 로고    scopus 로고
    • Pulmonary collectins in innate immunity of the lung
    • Kuroki Y, Takahashi M, Nishitani C. 2007. Pulmonary collectins in innate immunity of the lung. Cell Microbiol 9:1871-1879. http://dx.doi.org/10.1111/j.1462-5822.2007.00953.x.
    • (2007) Cell Microbiol , vol.9 , pp. 1871-1879
    • Kuroki, Y.1    Takahashi, M.2    Nishitani, C.3
  • 35
    • 34547877584 scopus 로고    scopus 로고
    • Macrophage complement receptors and pathogen clearance
    • van Lookeren Campagne M, Wiesmann C, Brown EJ. 2007. Macrophage complement receptors and pathogen clearance. Cell Microbiol 9:2095-2102. http://dx.doi.org/10.1111/j.1462-5822.2007.00981.x.
    • (2007) Cell Microbiol , vol.9 , pp. 2095-2102
    • van Lookeren Campagne, M.1    Wiesmann, C.2    Brown, E.J.3
  • 36
    • 79551698400 scopus 로고    scopus 로고
    • Impact of mannose-binding lectin insufficiency on the course of cystic fibrosis: a review and meta-analysis
    • Chalmers JD, Fleming GB, Hill AT, Kilpatrick DC. 2011. Impact of mannose-binding lectin insufficiency on the course of cystic fibrosis: a review and meta-analysis. Glycobiology 21:271-282. http://dx.doi.org/10.1093/glycob/cwq161.
    • (2011) Glycobiology , vol.21 , pp. 271-282
    • Chalmers, J.D.1    Fleming, G.B.2    Hill, A.T.3    Kilpatrick, D.C.4
  • 37
    • 35348924188 scopus 로고    scopus 로고
    • The flagellum of Pseudomonas aeruginosa is required for resistance to clearance by surfactant protein A
    • PMID: 17593964
    • Zhang S, McCormack FX, Levesque RC, O'Toole GA, Lau GW. 2007. The flagellum of Pseudomonas aeruginosa is required for resistance to clearance by surfactant protein A. PLoS One 2:e564. PMID: 17593964. http://dx.doi.org/10.1371/journal.pone.0000564.
    • (2007) PLoS One , vol.2
    • Zhang, S.1    McCormack, F.X.2    Levesque, R.C.3    O'Toole, G.A.4    Lau, G.W.5
  • 38
    • 0014730397 scopus 로고
    • Serological properties of Pseudomonas aeruginosa. II. Typespecific thermolabile (flagellar) antigens
    • Lanyi B. 1970. Serological properties of Pseudomonas aeruginosa. II. Typespecific thermolabile (flagellar) antigens. Acta Microbiol Acad Sci Hung 17:35-48.
    • (1970) Acta Microbiol Acad Sci Hung , vol.17 , pp. 35-48
    • Lanyi, B.1
  • 39
    • 0030569411 scopus 로고    scopus 로고
    • Genetic diversity of flagellins of Pseudomonas aeruginosa
    • Spangenberg C, Heuer T, Burger C, Tummler B. 1996. Genetic diversity of flagellins of Pseudomonas aeruginosa. FEBS Lett 396:213-217. http://dx.doi.org/10.1016/0014-5793(96)01099-X.
    • (1996) FEBS Lett , vol.396 , pp. 213-217
    • Spangenberg, C.1    Heuer, T.2    Burger, C.3    Tummler, B.4
  • 40
    • 0031750753 scopus 로고    scopus 로고
    • Cloning and comparison of fliC genes and identification of glycosylation in the flagellin of Pseudomonas aeruginosa a-type strains
    • Brimer CD, Montie TC. 1998. Cloning and comparison of fliC genes and identification of glycosylation in the flagellin of Pseudomonas aeruginosa a-type strains. J Bacteriol 178:3209-3217.
    • (1998) J Bacteriol , vol.178 , pp. 3209-3217
    • Brimer, C.D.1    Montie, T.C.2
  • 41
    • 0033952601 scopus 로고    scopus 로고
    • Identification of two distinct types of flagellar cap proteins, FliD, in Pseudomonas aeruginosa
    • Arora SK, Dasgupta N, Lory S, Ramphal R. 2000. Identification of two distinct types of flagellar cap proteins, FliD, in Pseudomonas aeruginosa. Infect Immun 68:1474-1479. http://dx.doi.org/10.1128/IAI.68.3.1474-1479.2000.
    • (2000) Infect Immun , vol.68 , pp. 1474-1479
    • Arora, S.K.1    Dasgupta, N.2    Lory, S.3    Ramphal, R.4
  • 42
    • 21544481151 scopus 로고    scopus 로고
    • Role of motility and flagellin glycosylation in the pathogenesis of Pseudomonas aeruginosa burn wound infections
    • Arora SK, Neely AN, Blair B, Lory S, Ramphal R. 2005. Role of motility and flagellin glycosylation in the pathogenesis of Pseudomonas aeruginosa burn wound infections. Infect Immun 73:4395-4398. http://dx.doi.org/10.1128/IAI.73.7.4395-4398.2005.
    • (2005) Infect Immun , vol.73 , pp. 4395-4398
    • Arora, S.K.1    Neely, A.N.2    Blair, B.3    Lory, S.4    Ramphal, R.5
  • 43
    • 28444479119 scopus 로고    scopus 로고
    • Roles of specific amino acids in the N terminus of Pseudomonas aeruginosa flagellin and of flagellin glycosylation in the innate immune response
    • Verma A, Arora SK, Kuravi SK, Ramphal R. 2005. Roles of specific amino acids in the N terminus of Pseudomonas aeruginosa flagellin and of flagellin glycosylation in the innate immune response. Infect Immun 73: 8237-8246. http://dx.doi.org/10.1128/IAI.73.12.8237-8246.2005.
    • (2005) Infect Immun , vol.73 , pp. 8237-8246
    • Verma, A.1    Arora, S.K.2    Kuravi, S.K.3    Ramphal, R.4
  • 44
    • 33744986533 scopus 로고    scopus 로고
    • Glycosylation of b-type flagellin of Pseudomonas aeruginosa: structural and genetic basis
    • Verma A, Schirm M, Arora SK, Thibault P, Logan SM, Ramphal R. 2006. Glycosylation of b-type flagellin of Pseudomonas aeruginosa: structural and genetic basis. J Bacteriol 188:4395-4403. http://dx.doi.org/10.1128/JB.01642-05.
    • (2006) J Bacteriol , vol.188 , pp. 4395-4403
    • Verma, A.1    Schirm, M.2    Arora, S.K.3    Thibault, P.4    Logan, S.M.5    Ramphal, R.6
  • 45
    • 0036127088 scopus 로고    scopus 로고
    • Campylobacter protein glycosylation affects host cell interactions
    • Szymanski CM, Burr DH, Guerry P. 2002. Campylobacter protein glycosylation affects host cell interactions. Infect Immun 70:2242-2244. http://dx.doi.org/10.1128/IAI.70.4.2242-2244.2002.
    • (2002) Infect Immun , vol.70 , pp. 2242-2244
    • Szymanski, C.M.1    Burr, D.H.2    Guerry, P.3
  • 46
    • 0242575011 scopus 로고    scopus 로고
    • Flagellin glycosylation island in Pseudomonas syringae pv. glycinea and its role in host specificity
    • Takeuchi K, Taguchi F, Inagaki Y, Toyoda K, Shiraishi T, Ichinose Y. 2003. Flagellin glycosylation island in Pseudomonas syringae pv. glycinea and its role in host specificity. J Bacteriol 185:6658-6665. http://dx.doi.org/10.1128/JB.185.22.6658-6665.2003.
    • (2003) J Bacteriol , vol.185 , pp. 6658-6665
    • Takeuchi, K.1    Taguchi, F.2    Inagaki, Y.3    Toyoda, K.4    Shiraishi, T.5    Ichinose, Y.6
  • 47
    • 84861473544 scopus 로고    scopus 로고
    • Lipopolysaccharide O-antigen prevents phagocytosis of Vibrio anguillarum by rainbow trout (Oncorhynchus mykiss) skin epithelial cells
    • Lindell K, Fahlgren A, Hjerde E, Willassen NP, Fallman M, Milton DL. 2012. Lipopolysaccharide O-antigen prevents phagocytosis of Vibrio anguillarum by rainbow trout (Oncorhynchus mykiss) skin epithelial cells. PLoS One 7:e37678. http://dx.doi.org/10.1371/journal.pone.0037678.
    • (2012) PLoS One , vol.7
    • Lindell, K.1    Fahlgren, A.2    Hjerde, E.3    Willassen, N.P.4    Fallman, M.5    Milton, D.L.6
  • 48
    • 73449121106 scopus 로고    scopus 로고
    • Burkholderia cenocepacia O antigen lipopolysaccharide prevents phagocytosis by macrophages and adhesion to epithelial cells
    • Saldias MS, Ortega X, Valvano MA. 2009. Burkholderia cenocepacia O antigen lipopolysaccharide prevents phagocytosis by macrophages and adhesion to epithelial cells. J Med Microbiol 58:1542-1548. http://dx.doi.org/10.1099/jmm.0.013235-0.
    • (2009) J Med Microbiol , vol.58 , pp. 1542-1548
    • Saldias, M.S.1    Ortega, X.2    Valvano, M.A.3
  • 49
    • 33645214751 scopus 로고    scopus 로고
    • Altering the length of the lipopolysaccharide O antigen has an impact on the interaction of Salmonella enterica serovar Typhimurium with macrophages and complement
    • Murray GL, Attridge SR, Morona R. 2006. Altering the length of the lipopolysaccharide O antigen has an impact on the interaction of Salmonella enterica serovar Typhimurium with macrophages and complement. J Bacteriol 188:2735-2739. http://dx.doi.org/10.1128/JB.188.7.2735-2739.2006.
    • (2006) J Bacteriol , vol.188 , pp. 2735-2739
    • Murray, G.L.1    Attridge, S.R.2    Morona, R.3
  • 50
    • 14244264773 scopus 로고    scopus 로고
    • The core lipopolysaccharide of Escherichia coli is a ligand for the dendritic-cell-specific intercellular adhesion molecule nonintegrin CD209 receptor
    • Klena J, Zhang P, Schwartz O, Hull S, Chen T. 2005. The core lipopolysaccharide of Escherichia coli is a ligand for the dendritic-cell-specific intercellular adhesion molecule nonintegrin CD209 receptor. J Bacteriol 187:1710-1715. http://dx.doi.org/10.1128/JB.187.5.1710-1715.2005.
    • (2005) J Bacteriol , vol.187 , pp. 1710-1715
    • Klena, J.1    Zhang, P.2    Schwartz, O.3    Hull, S.4    Chen, T.5
  • 52
    • 33748502748 scopus 로고    scopus 로고
    • Role of N-acetylglucosamine within core lipopolysaccharide of several species of gram-negative bacteria in targeting the DC-SIGN (CD209)
    • Zhang P, Snyder S, Feng P, Azadi P, Zhang S, Bulgheresi S, Sanderson KE, He J, Klena J, Chen T. 2006. Role of N-acetylglucosamine within core lipopolysaccharide of several species of gram-negative bacteria in targeting the DC-SIGN (CD209). J Immunol 177:4002-4011. http://dx.doi.org/10.4049/jimmunol.177.6.4002.
    • (2006) J Immunol , vol.177 , pp. 4002-4011
    • Zhang, P.1    Snyder, S.2    Feng, P.3    Azadi, P.4    Zhang, S.5    Bulgheresi, S.6    Sanderson, K.E.7    He, J.8    Klena, J.9    Chen, T.10
  • 53
    • 84920010336 scopus 로고    scopus 로고
    • Exploitation of the macrophage mannose receptor (CD206) in infectious disease diagnostics and therapeutics
    • Azad AK, Rajaram MV, Schlesinger LS. 2014. Exploitation of the macrophage mannose receptor (CD206) in infectious disease diagnostics and therapeutics. J Cytol Mol Biol 1:1000003. http://dx.doi.org/10.13188/2325-4653.1000003.
    • (2014) J Cytol Mol Biol , vol.1 , pp. 1000003
    • Azad, A.K.1    Rajaram, M.V.2    Schlesinger, L.S.3
  • 54
    • 0036784647 scopus 로고    scopus 로고
    • Pulmonary surfactant protein A up-regulates activity of the mannose receptor, a pattern recognition receptor expressed on human macrophages
    • Beharka AA, Gaynor CD, Kang BK, Voelker DR, McCormack FX, Schlesinger LS. 2002. Pulmonary surfactant protein A up-regulates activity of the mannose receptor, a pattern recognition receptor expressed on human macrophages. J Immunol 169:3565-3573. http://dx.doi.org/10.4049/jimmunol.169.7.3565.
    • (2002) J Immunol , vol.169 , pp. 3565-3573
    • Beharka, A.A.1    Gaynor, C.D.2    Kang, B.K.3    Voelker, D.R.4    McCormack, F.X.5    Schlesinger, L.S.6

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