메뉴 건너뛰기




Volumn 9, Issue 2, 2013, Pages 5208-5215

Effect of gastric environment on Helicobacter pylori adhesion to a mucoadhesive polymer

Author keywords

Bacterial adhesion; Biomaterials; Chitosan; Helicobacter pylori; Thin films

Indexed keywords

ABSORPTION SPECTROSCOPY; ADHESION; BACTERIA; BIOMATERIALS; CHITOSAN; DRUG DELIVERY; GOLD COATINGS; METABOLISM; ULTRATHIN FILMS;

EID: 84872069015     PISSN: 17427061     EISSN: 18787568     Source Type: Journal    
DOI: 10.1016/j.actbio.2012.09.011     Document Type: Article
Times cited : (40)

References (52)
  • 1
    • 0021259505 scopus 로고
    • Unidentified curved bacilli in the stomach of patients with gastritis and peptic ulceration
    • B.J. Marshall, and J.R. Warren Unidentified curved bacilli in the stomach of patients with gastritis and peptic ulceration Lancet 1 8390 1984 1311 1315
    • (1984) Lancet , vol.1 , Issue.8390 , pp. 1311-1315
    • Marshall, B.J.1    Warren, J.R.2
  • 2
    • 78049354889 scopus 로고    scopus 로고
    • Helicobacter pylori and gastric cancer: Factors that modulate disease risk
    • L.E. Wroblewski, R.M. Peek, and K.T. Wilson Helicobacter pylori and gastric cancer: factors that modulate disease risk Clin Microbiol Rev 23 4 2010 713 739
    • (2010) Clin Microbiol Rev , vol.23 , Issue.4 , pp. 713-739
    • Wroblewski, L.E.1    Peek, R.M.2    Wilson, K.T.3
  • 3
    • 34250703132 scopus 로고    scopus 로고
    • Helicobacter pylori infection and related gastrointestinal diseases
    • D. Makola, D.A. Peura, and S.E. Crowe Helicobacter pylori infection and related gastrointestinal diseases J Clin Gastroenterol 41 6 2007 548 558
    • (2007) J Clin Gastroenterol , vol.41 , Issue.6 , pp. 548-558
    • Makola, D.1    Peura, D.A.2    Crowe, S.E.3
  • 4
    • 0031349567 scopus 로고    scopus 로고
    • The epidemiology of Helicobacter pylori
    • H.M. Mitchell The epidemiology of Helicobacter pylori Baillieres Clin Infect Dis 4 3 1997 257 281
    • (1997) Baillieres Clin Infect Dis , vol.4 , Issue.3 , pp. 257-281
    • Mitchell, H.M.1
  • 5
    • 6744268050 scopus 로고    scopus 로고
    • Helicobacter pylori infection occurs via close contact with infected individuals in early childhood
    • H. Miyaji, T. Azuma, S. Ito, Y. Abe, F. Gejyo, and N. Hashimoto Helicobacter pylori infection occurs via close contact with infected individuals in early childhood J Gastroenterol Hepatol 15 3 2000 257 262
    • (2000) J Gastroenterol Hepatol , vol.15 , Issue.3 , pp. 257-262
    • Miyaji, H.1    Azuma, T.2    Ito, S.3    Abe, Y.4    Gejyo, F.5    Hashimoto, N.6
  • 6
    • 0026497172 scopus 로고
    • Isolation of Helicobacter pylori from human feces
    • J.E. Thomas, G.R. Gibson, M.K. Darboe, A. Dale, and L.T. Weaver Isolation of Helicobacter pylori from human feces Lancet 340 8829 1992 1194 1195
    • (1992) Lancet , vol.340 , Issue.8829 , pp. 1194-1195
    • Thomas, J.E.1    Gibson, G.R.2    Darboe, M.K.3    Dale, A.4    Weaver, L.T.5
  • 8
    • 0036370334 scopus 로고    scopus 로고
    • Helicobacter pylori and gastrointestinal tract adenocarcinomas
    • R.M. Peek Jr., and M.J. Blaser Helicobacter pylori and gastrointestinal tract adenocarcinomas Nat Rev Cancer 2 1 2002 28 37
    • (2002) Nat Rev Cancer , vol.2 , Issue.1 , pp. 28-37
    • Peek Jr., R.M.1    Blaser, M.J.2
  • 10
    • 0030909891 scopus 로고    scopus 로고
    • Urease-independent chemotactic responses of Helicobacter pylori to urea, urease inhibitors, and sodium bicarbonate
    • T. Mizote, H. Yoshiyama, and T. Nakazawa Urease-independent chemotactic responses of Helicobacter pylori to urea, urease inhibitors, and sodium bicarbonate Infect Immun 65 4 1997 1519 1521
    • (1997) Infect Immun , vol.65 , Issue.4 , pp. 1519-1521
    • Mizote, T.1    Yoshiyama, H.2    Nakazawa, T.3
  • 11
    • 0347519219 scopus 로고    scopus 로고
    • Comparison of H2-receptor antagonist- and proton-pump inhibitor-based triple regimens for the eradication of Helicobacter pylori in Chinese patients with gastritis or peptic ulcer
    • F.L. Hu, J.C. Jia, Y.L. Li, and G.B. Yang Comparison of H2-receptor antagonist- and proton-pump inhibitor-based triple regimens for the eradication of Helicobacter pylori in Chinese patients with gastritis or peptic ulcer J Int Med Res 31 6 2003 469 474
    • (2003) J Int Med Res , vol.31 , Issue.6 , pp. 469-474
    • Hu, F.L.1    Jia, J.C.2    Li, Y.L.3    Yang, G.B.4
  • 12
    • 33644782035 scopus 로고    scopus 로고
    • Helicobacter pylori treatment: A practical approach
    • N. Vakil Helicobacter pylori treatment: a practical approach Am J Gastroenterol 101 3 2006 497 499
    • (2006) Am J Gastroenterol , vol.101 , Issue.3 , pp. 497-499
    • Vakil, N.1
  • 13
    • 34548630860 scopus 로고    scopus 로고
    • Chitosan nanoparticles for oral drug and gene delivery
    • K. Bowman, and K.W. Leong Chitosan nanoparticles for oral drug and gene delivery Int J Nanomed 1 2 2006 117 128
    • (2006) Int J Nanomed , vol.1 , Issue.2 , pp. 117-128
    • Bowman, K.1    Leong, K.W.2
  • 14
    • 80053313377 scopus 로고    scopus 로고
    • Recent advances of chitosan nanoparticles as drug carriers
    • J. Wang Recent advances of chitosan nanoparticles as drug carriers Int J Nanomed 6 2011 765 774
    • (2011) Int J Nanomed , vol.6 , pp. 765-774
    • Wang, J.1
  • 18
    • 45749108316 scopus 로고    scopus 로고
    • Insights into the mode of action of chitosan as an antibacterial compound
    • D. Raafat, K. von Bargen, A. Haas, and H.G. Sahl Insights into the mode of action of chitosan as an antibacterial compound Appl Environ Microbiol 74 12 2008 3764 3773
    • (2008) Appl Environ Microbiol , vol.74 , Issue.12 , pp. 3764-3773
    • Raafat, D.1    Von Bargen, K.2    Haas, A.3    Sahl, H.G.4
  • 19
    • 77953602560 scopus 로고    scopus 로고
    • Chitosan and its antimicrobial potential - A critical literature survey
    • D. Raafat, and H.G. Sahl Chitosan and its antimicrobial potential - a critical literature survey Microb Biotechnol 2 2 2009 186 201
    • (2009) Microb Biotechnol , vol.2 , Issue.2 , pp. 186-201
    • Raafat, D.1    Sahl, H.G.2
  • 20
    • 34249660577 scopus 로고    scopus 로고
    • Coccoid form of Helicobacter pylori as a morphological manifestation of cell adaptation to the environment
    • N.F. Azevedo Coccoid form of Helicobacter pylori as a morphological manifestation of cell adaptation to the environment Appl Environ Microbiol 73 10 2007 3423 3427
    • (2007) Appl Environ Microbiol , vol.73 , Issue.10 , pp. 3423-3427
    • Azevedo, N.F.1
  • 21
    • 0344306504 scopus 로고    scopus 로고
    • Protein adsorption on mixtures of hydroxyl- and methyl-terminated alkanethiols self-Assembled monolayers
    • M.C. Martins, B.D. Ratner, and M.A. Barbosa Protein adsorption on mixtures of hydroxyl- and methyl-terminated alkanethiols self-Assembled monolayers J Biomed Mater Res A 67 2003 158 171
    • (2003) J Biomed Mater Res A , vol.67 , pp. 158-171
    • Martins, M.C.1    Ratner, B.D.2    Barbosa, M.A.3
  • 22
    • 80054771159 scopus 로고    scopus 로고
    • Synthesis of an O-Alkynyl-chitosan and its chemoselective conjugation with a PEG-like amino-Azide through click chemistry
    • J.R.R. Oliveira, L. Mafra, M.C. Martins, and P. Gomes Synthesis of an O-Alkynyl-chitosan and its chemoselective conjugation with a PEG-like amino-Azide through click chemistry Carbohydr Polym 87 2012 240 249
    • (2012) Carbohydr Polym , vol.87 , pp. 240-249
    • Oliveira, J.R.R.1    Mafra, L.2    Martins, M.C.3    Gomes, P.4
  • 23
    • 42449149169 scopus 로고    scopus 로고
    • Interactions between chitosan and SDS at a low-charged silica substrate compared to interactions in the bulk - The effect of ionic strength
    • L. Macakova Interactions between chitosan and SDS at a low-charged silica substrate compared to interactions in the bulk - the effect of ionic strength Langmuir 24 8 2008 3814 3827
    • (2008) Langmuir , vol.24 , Issue.8 , pp. 3814-3827
    • MacAkova, L.1
  • 24
    • 0037178771 scopus 로고    scopus 로고
    • Helicobacter pylori SabA adhesin in persistent infection and chronic inflammation
    • J. Mahdavi, B. Sonden, M. Hurtig, F.O. Olfat, L. Forsberg, and N. Roche Helicobacter pylori SabA adhesin in persistent infection and chronic inflammation Science 297 5581 2002 573 578
    • (2002) Science , vol.297 , Issue.5581 , pp. 573-578
    • Mahdavi, J.1    Sonden, B.2    Hurtig, M.3    Olfat, F.O.4    Forsberg, L.5    Roche, N.6
  • 26
    • 33644875542 scopus 로고    scopus 로고
    • Chemical modification of chitosan by phosphorylation: An XPS, FT-IR and SEM study
    • I.F. Amaral, P.L. Granja, and M.A. Barbosa Chemical modification of chitosan by phosphorylation: an XPS, FT-IR and SEM study J Biomater Sci Polym Ed 16 12 2005 1575 1593
    • (2005) J Biomater Sci Polym Ed , vol.16 , Issue.12 , pp. 1575-1593
    • Amaral, I.F.1    Granja, P.L.2    Barbosa, M.A.3
  • 29
    • 34548094323 scopus 로고    scopus 로고
    • Fourier transform spectroscopic analysis of protein secondary structures
    • J. Kong Fourier transform spectroscopic analysis of protein secondary structures Acta Biochim Biophys Sin 39 8 2007 549 559
    • (2007) Acta Biochim Biophys Sin , vol.39 , Issue.8 , pp. 549-559
    • Kong, J.1
  • 30
    • 0026081335 scopus 로고
    • Effect of increasing Helicobacter pyloriammonia production by urea infusion on plasma gastrin-concentrations
    • R.S. Chittajallu Effect of increasing Helicobacter pyloriammonia production by urea infusion on plasma gastrin-concentrations Gut 32 1 1991 21 24
    • (1991) Gut , vol.32 , Issue.1 , pp. 21-24
    • Chittajallu, R.S.1
  • 31
    • 0025812293 scopus 로고
    • Detection of Helicobacter pyloricarriers by discriminant-Analysis of urea and pH levels in gastric juices
    • F. Ameglio Detection of Helicobacter pyloricarriers by discriminant-Analysis of urea and pH levels in gastric juices Am J Clin Pathol 44 8 1991 697 698
    • (1991) Am J Clin Pathol , vol.44 , Issue.8 , pp. 697-698
    • Ameglio, F.1
  • 32
    • 0141830659 scopus 로고    scopus 로고
    • Polymeric nano- and microparticles for the oral delivery of peptides and peptidomimetics
    • E. Allemann, J. Leroux, and R. Gurny Polymeric nano- and microparticles for the oral delivery of peptides and peptidomimetics Adv Drug Deliv Rev 34 2-3 1998 171 189
    • (1998) Adv Drug Deliv Rev , vol.34 , Issue.23 , pp. 171-189
    • Allemann, E.1    Leroux, J.2    Gurny, R.3
  • 33
    • 0027442188 scopus 로고
    • Characterization of chitosan. Influence of ionic strength and degree of acetylation on chain expansion
    • M. Rinaudo, M. Milas, and P. Le Dung Characterization of chitosan. Influence of ionic strength and degree of acetylation on chain expansion Int. J. Biol. Macromol. 15 1993 281 285
    • (1993) Int. J. Biol. Macromol. , vol.15 , pp. 281-285
    • Rinaudo, M.1    Milas, M.2    Le Dung, P.3
  • 34
    • 0034249313 scopus 로고    scopus 로고
    • Synthesis and characterization of a novel chitosan-based network prepared using naturally occurring crosslinker
    • F. Mi Synthesis and characterization of a novel chitosan-based network prepared using naturally occurring crosslinker J Polym Sci, Part A: Polym Chem 38 15 2000 2804 2814
    • (2000) J Polym Sci, Part A: Polym Chem , vol.38 , Issue.15 , pp. 2804-2814
    • Mi, F.1
  • 35
    • 0035882708 scopus 로고    scopus 로고
    • Release of indomethacin from a novel chitosan microsphere prepared by a naturally occurring crosslinker: Examination of crosslinking and polycation-Anionic drug interaction
    • F. Mi Release of indomethacin from a novel chitosan microsphere prepared by a naturally occurring crosslinker: examination of crosslinking and polycation-Anionic drug interaction J Appl Polym Sci 81 7 2001 1700 1711
    • (2001) J Appl Polym Sci , vol.81 , Issue.7 , pp. 1700-1711
    • Mi, F.1
  • 37
    • 4444226939 scopus 로고    scopus 로고
    • Escherichia coli glutamate- and arginine-dependent acid resistance systems increase internal pH and reverse transmembrane potential
    • H. Richard, and J.W. Foster Escherichia coli glutamate- and arginine-dependent acid resistance systems increase internal pH and reverse transmembrane potential J Bacteriol 186 18 2004 6032 6041
    • (2004) J Bacteriol , vol.186 , Issue.18 , pp. 6032-6041
    • Richard, H.1    Foster, J.W.2
  • 38
    • 0031714167 scopus 로고    scopus 로고
    • Characterization of an acidic-pH-inducible stress protein (hsp70), a putative sulfatide binding adhesin, from Helicobacter pylori
    • M. Huesca, A. Goodwin, A. Bhagwansingh, P. Hoffman, and C.A. Lingwood Characterization of an acidic-pH-inducible stress protein (hsp70), a putative sulfatide binding adhesin, from Helicobacter pylori Infect Immun 66 9 1998 4061 4067
    • (1998) Infect Immun , vol.66 , Issue.9 , pp. 4061-4067
    • Huesca, M.1    Goodwin, A.2    Bhagwansingh, A.3    Hoffman, P.4    Lingwood, C.A.5
  • 39
    • 0029929131 scopus 로고    scopus 로고
    • Acidic pH changes receptor binding specificity of Helicobacter pylori: A binary adhesion model in which surface heat shock (stress) proteins mediate sulfatide recognition in gastric colonization
    • M. Huesca, S. Borgia, P. Hoffman, and C.A. Lingwood Acidic pH changes receptor binding specificity of Helicobacter pylori: a binary adhesion model in which surface heat shock (stress) proteins mediate sulfatide recognition in gastric colonization Infect Immun 64 7 1996 2643 2648
    • (1996) Infect Immun , vol.64 , Issue.7 , pp. 2643-2648
    • Huesca, M.1    Borgia, S.2    Hoffman, P.3    Lingwood, C.A.4
  • 40
    • 46749099880 scopus 로고    scopus 로고
    • The changes of proteomes components of Helicobacter pylori in response to acid stress without urea
    • C.H. Shao, Q.Y. Zhang, W. Tang, Q. Wei, Y.B. Zhou, and Y.D. Sun The changes of proteomes components of Helicobacter pylori in response to acid stress without urea J Microbiol 46 3 2008 331 337
    • (2008) J Microbiol , vol.46 , Issue.3 , pp. 331-337
    • Shao, C.H.1    Zhang, Q.Y.2    Tang, W.3    Wei, Q.4    Zhou, Y.B.5    Sun, Y.D.6
  • 41
    • 0038781648 scopus 로고    scopus 로고
    • PH-regulated gene expression of the gastric pathogen Helicobacter pylori
    • D.S. Merrell, M.L. Goodrich, G. Otto, L.S. Tompkins, and S. Falkow PH-regulated gene expression of the gastric pathogen Helicobacter pylori Infect Immun 71 6 2003 3529 3539
    • (2003) Infect Immun , vol.71 , Issue.6 , pp. 3529-3539
    • Merrell, D.S.1    Goodrich, M.L.2    Otto, G.3    Tompkins, L.S.4    Falkow, S.5
  • 42
    • 79951997008 scopus 로고    scopus 로고
    • Functional and structural aspects of Helicobacter pyloriacidic stress response factors
    • G. Zanotti, and L. Cendron Functional and structural aspects of Helicobacter pyloriacidic stress response factors IUBMB Life 62 10 2010 715 723
    • (2010) IUBMB Life , vol.62 , Issue.10 , pp. 715-723
    • Zanotti, G.1    Cendron, L.2
  • 43
    • 51149097716 scopus 로고    scopus 로고
    • Expression of the Helicobacter pylori adhesin SabA is controlled via phase variation and the ArsRS signal transduction system
    • A.C. Goodwin, D.M. Weinberger, C.B. Ford, J.C. Nelson, J.D. Snider, and J.D. Hall Expression of the Helicobacter pylori adhesin SabA is controlled via phase variation and the ArsRS signal transduction system Microbiology-SGM 154 2008 2231 2240
    • (2008) Microbiology-SGM , vol.154 , pp. 2231-2240
    • Goodwin, A.C.1    Weinberger, D.M.2    Ford, C.B.3    Nelson, J.C.4    Snider, J.D.5    Hall, J.D.6
  • 44
    • 33646772149 scopus 로고    scopus 로고
    • Helicobacter pylori outer membrane proteins and gastroduodenal disease
    • Y. Yamaoka, O. Ojo, S. Fujimoto, S. Odenbreit, R. Haas, and O. Gutierrez Helicobacter pylori outer membrane proteins and gastroduodenal disease Gut 55 6 2006 775 781
    • (2006) Gut , vol.55 , Issue.6 , pp. 775-781
    • Yamaoka, Y.1    Ojo, O.2    Fujimoto, S.3    Odenbreit, S.4    Haas, R.5    Gutierrez, O.6
  • 45
    • 0016690348 scopus 로고
    • Primary structure of porcine pepsin. III. Amino acid sequence of a cyanogen bromide fragment, CB2A, and the complete structure of porcine pepsin
    • P. Sepulveda Primary structure of porcine pepsin. III. Amino acid sequence of a cyanogen bromide fragment, CB2A, and the complete structure of porcine pepsin J Biol Chem 250 13 1975 5082 5088
    • (1975) J Biol Chem , vol.250 , Issue.13 , pp. 5082-5088
    • Sepulveda, P.1
  • 46
    • 13844297711 scopus 로고    scopus 로고
    • Bioadhesive oesophageal bandages: Protection against acid and pepsin injury
    • M. Tang, P. Dettmar, and H. Batchelor Bioadhesive oesophageal bandages: protection against acid and pepsin injury Int J Pharm 292 1-2 2005 169 177
    • (2005) Int J Pharm , vol.292 , Issue.12 , pp. 169-177
    • Tang, M.1    Dettmar, P.2    Batchelor, H.3
  • 47
    • 0015459595 scopus 로고
    • Isoelectric spectra of native and base denatured crystallized swine pepsin
    • M. Jonsson Isoelectric spectra of native and base denatured crystallized swine pepsin Acta Chem Scand 26 9 1972 3435 3440
    • (1972) Acta Chem Scand , vol.26 , Issue.9 , pp. 3435-3440
    • Jonsson, M.1
  • 48
    • 20144367704 scopus 로고    scopus 로고
    • Rapid loss of motility of Helicobacter pylori in the gastric lumen in vivo
    • S. Schreiber Rapid loss of motility of Helicobacter pylori in the gastric lumen in vivo Infect Immun 73 3 2005 1584 1589
    • (2005) Infect Immun , vol.73 , Issue.3 , pp. 1584-1589
    • Schreiber, S.1
  • 49
    • 0034636112 scopus 로고    scopus 로고
    • A partially unfolded structure of the alkaline-denatured state of pepsin and its implication for stability of the zymogen-derived protein
    • T. Konno, Y.O. Kamatari, N. Tanaka, H. Kamikubo, C.M. Dobson, and K. Nagayama A partially unfolded structure of the alkaline-denatured state of pepsin and its implication for stability of the zymogen-derived protein Biochemistry 39 14 2000 4182 4190
    • (2000) Biochemistry , vol.39 , Issue.14 , pp. 4182-4190
    • Konno, T.1    Kamatari, Y.O.2    Tanaka, N.3    Kamikubo, H.4    Dobson, C.M.5    Nagayama, K.6
  • 50
    • 0032407988 scopus 로고    scopus 로고
    • Crystallographic and mutational analyses of an extremely acidophilic and acid-stable xylanase: Biased distribution of acidic residues and importance of Asp37 for catalysis at low pH
    • S. Fushinobu, K. Ito, M. Konno, T. Wakagi, and H. Matsuzawa Crystallographic and mutational analyses of an extremely acidophilic and acid-stable xylanase: biased distribution of acidic residues and importance of Asp37 for catalysis at low pH Protein Eng 11 12 1998 1121 1128
    • (1998) Protein Eng , vol.11 , Issue.12 , pp. 1121-1128
    • Fushinobu, S.1    Ito, K.2    Konno, M.3    Wakagi, T.4    Matsuzawa, H.5
  • 51
    • 73949137561 scopus 로고    scopus 로고
    • A review of the antimicrobial activity of chitosan
    • Rejane.C. Goy A review of the antimicrobial activity of chitosan Polímeros: Ciência e Tecnologia 19 3 2009 241 247
    • (2009) Polímeros: Ciência e Tecnologia , vol.19 , Issue.3 , pp. 241-247
    • Goy, Rejane.C.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.