메뉴 건너뛰기




Volumn 6, Issue 3, 2014, Pages 1049-1061

Identification of a key residue for oligomerisation and pore-formation of Clostridium perfringens NetB

Author keywords

Clostridium perfringens; Necrotic enteritis; NetB; Pore forming toxin

Indexed keywords

AMINO ACID; CLOSTRIDIUM TOXIN; LIPOSOME; NECROTIC ENTERITIS TOXIN B; PORE FORMING CYTOTOXIC PROTEIN; PROTEIN VARIANT; UNCLASSIFIED DRUG;

EID: 84897866626     PISSN: 20726651     EISSN: None     Source Type: Journal    
DOI: 10.3390/toxins6031049     Document Type: Article
Times cited : (13)

References (24)
  • 3
    • 0002517821 scopus 로고    scopus 로고
    • Clostridial enteritis is an often underestimated problem
    • Sluis, V.D. Clostridial enteritis is an often underestimated problem. World Poult. 2000, 16, 42-43.
    • (2000) World Poult. , vol.16 , pp. 42-43
    • Sluis, V.D.1
  • 5
    • 0030447720 scopus 로고    scopus 로고
    • Structure of staphylococcal alpha-hemolysin, a heptameric transmembrane pore
    • Song, L.; Hobaugh, M.R.; Shustak, C.; Cheley, S.; Bayley, H.; Gouaux, J.E. Structure of staphylococcal alpha-hemolysin, a heptameric transmembrane pore. Science 1996, 274, 1859-1866.
    • (1996) Science , vol.274 , pp. 1859-1866
    • Song, L.1    Hobaugh, M.R.2    Shustak, C.3    Cheley, S.4    Bayley, H.5    Gouaux, J.E.6
  • 6
    • 80054794259 scopus 로고    scopus 로고
    • Crystal structure of the octameric pore of staphylococcal gamma-hemolysin reveals the beta-barrel pore formation mechanism by two components
    • Yamashita, K.; Kawai, Y.; Tanaka, Y.; Hirano, N.; Kaneko, J.; Tomita, N.; Ohta, M.; Kamio, Y.; Yao, M.; Tanaka, I. Crystal structure of the octameric pore of staphylococcal gamma-hemolysin reveals the beta-barrel pore formation mechanism by two components. Proc. Natl. Acad. Sci. USA 2011, 108, 17314-17319.
    • (2011) Proc. Natl. Acad. Sci. USA , vol.108 , pp. 17314-17319
    • Yamashita, K.1    Kawai, Y.2    Tanaka, Y.3    Hirano, N.4    Kaneko, J.5    Tomita, N.6    Ohta, M.7    Kamio, Y.8    Yao, M.9    Tanaka, I.10
  • 7
    • 21744447839 scopus 로고    scopus 로고
    • Crystal structure of the Vibrio cholerae cytolysin (VCC) pro-toxin and its assembly into a heptameric transmembrane pore
    • Olson, R.; Gouaux, E. Crystal structure of the Vibrio cholerae cytolysin (VCC) pro-toxin and its assembly into a heptameric transmembrane pore. J. Mol. Biol. 2005, 350, 997-1016.
    • (2005) J. Mol. Biol. , vol.350 , pp. 997-1016
    • Olson, R.1    Gouaux, E.2
  • 8
    • 0030735356 scopus 로고    scopus 로고
    • Staphylococcal alpha-toxin: Formation of the heptameric pore is partially cooperative and proceeds through multiple intermediate stages
    • Valeva, A.; Palmer, M.; Bhakdi, S. Staphylococcal alpha-toxin: Formation of the heptameric pore is partially cooperative and proceeds through multiple intermediate stages. Biochemistry 1997, 36, 13298-13304.
    • (1997) Biochemistry , vol.36 , pp. 13298-13304
    • Valeva, A.1    Palmer, M.2    Bhakdi, S.3
  • 9
    • 0031877366 scopus 로고    scopus 로고
    • Alpha-hemolysin from Staphylococcus aureus: An archetype of beta-barrel, channel-forming toxins
    • Gouaux, E. Alpha-hemolysin from Staphylococcus aureus: An archetype of beta-barrel, channel-forming toxins. J. Struct. Biol. 1998, 121, 110-122.
    • (1998) J. Struct. Biol. , vol.121 , pp. 110-122
    • Gouaux, E.1
  • 10
    • 0031454754 scopus 로고    scopus 로고
    • Alpha-hemolysin, gamma-hemolysin, and leukocidin from Staphylococcus aureus: Distant in sequence but similar in structure
    • Gouaux, E.; Hobaugh, M.; Song, L. Alpha-hemolysin, gamma-hemolysin, and leukocidin from Staphylococcus aureus: Distant in sequence but similar in structure. Protein Sci. 1997, 6, 2631-2635.
    • (1997) Protein Sci. , vol.6 , pp. 2631-2635
    • Gouaux, E.1    Hobaugh, M.2    Song, L.3
  • 11
    • 0037407011 scopus 로고    scopus 로고
    • Arresting and releasing staphylococcal alpha-hemolysin at intermediate stages of pore formation by engineered disulfide bonds
    • Kawate, T.; Gouaux, E. Arresting and releasing staphylococcal alpha-hemolysin at intermediate stages of pore formation by engineered disulfide bonds. Protein Sci. 2003, 12, 997-1006.
    • (2003) Protein Sci. , vol.12 , pp. 997-1006
    • Kawate, T.1    Gouaux, E.2
  • 12
    • 0029125825 scopus 로고
    • Key residues for membrane-binding, oligomerization, and pore-forming activity of staphylococcal alpha-hemolysin identified by cysteine scanning mutagenesis and targeted chemical modification
    • Walker, B.; Bayley, H. Key residues for membrane-binding, oligomerization, and pore-forming activity of staphylococcal alpha-hemolysin identified by cysteine scanning mutagenesis and targeted chemical modification. J. Biol. Chem. 1995, 270, 23065-23071.
    • (1995) J. Biol. Chem. , vol.270 , pp. 23065-23071
    • Walker, B.1    Bayley, H.2
  • 13
    • 0030741317 scopus 로고    scopus 로고
    • The heptameric prepore of a staphylococcal alpha-hemolysin mutant in lipid bilayers imaged by atomic force microscopy
    • Fang, Y.; Cheley, S.; Bayley, H.; Yang, J. The heptameric prepore of a staphylococcal alpha-hemolysin mutant in lipid bilayers imaged by atomic force microscopy. Biochemistry 1997, 36, 9518-9522.
    • (1997) Biochemistry , vol.36 , pp. 9518-9522
    • Fang, Y.1    Cheley, S.2    Bayley, H.3    Yang, J.4
  • 14
    • 0029240394 scopus 로고
    • An intermediate in the assembly of a pore-forming protein trapped with a genetically-engineered switch
    • Walker, B.; Braha, O.; Cheley, S.; Bayley, H. An intermediate in the assembly of a pore-forming protein trapped with a genetically-engineered switch. Chem. Biol. 1995, 2, 99-105.
    • (1995) Chem. Biol. , vol.2 , pp. 99-105
    • Walker, B.1    Braha, O.2    Cheley, S.3    Bayley, H.4
  • 15
    • 0031887515 scopus 로고    scopus 로고
    • Site-directed mutagenesis of Clostridium perfringens beta-toxin: Expression of wild-type and mutant toxins in Bacillus subtilis
    • Steinthorsdottir, V.; Fridriksdottir, V.; Gunnarsson, E.; Andresson, O.S. Site-directed mutagenesis of Clostridium perfringens beta-toxin: Expression of wild-type and mutant toxins in Bacillus subtilis. FEMS Microbiol. Lett. 1998, 158, 17-23.
    • (1998) FEMS Microbiol. Lett. , vol.158 , pp. 17-23
    • Steinthorsdottir, V.1    Fridriksdottir, V.2    Gunnarsson, E.3    Andresson, O.S.4
  • 17
    • 0028365388 scopus 로고
    • Histidine residues near the N terminus of staphylococcal alpha-toxin as reporters of regions that are critical for oligomerization and pore formation
    • Jursch, R.; Hildebrand, A.; Hobom, G.; Tranum-Jensen, J.; Ward, R.; Kehoe, M.; Bhakdi, S. Histidine residues near the N terminus of staphylococcal alpha-toxin as reporters of regions that are critical for oligomerization and pore formation. Infect. Immun. 1994, 62, 2249-2256.
    • (1994) Infect. Immun. , vol.62 , pp. 2249-2256
    • Jursch, R.1    Hildebrand, A.2    Hobom, G.3    Tranum-Jensen, J.4    Ward, R.5    Kehoe, M.6    Bhakdi, S.7
  • 18
    • 0028216879 scopus 로고
    • Site-directed mutagenesis of the alpha-toxin gene of Staphylococcus-aureus-Role of histidines in toxin activity in-vitro and in a murine model
    • Menzies, B.E.; Kernodle, D.S. Site-directed mutagenesis of the alpha-toxin gene of Staphylococcus-aureus-Role of histidines in toxin activity in-vitro and in a murine model. Infect. Immun. 1994, 62, 1843-1847.
    • (1994) Infect. Immun. , vol.62 , pp. 1843-1847
    • Menzies, B.E.1    Kernodle, D.S.2
  • 19
    • 0029000140 scopus 로고
    • Correct oligomerization is a prerequisite for insertion of the central molecular domain of staphylococcal alpha-toxin into the lipid bilayer
    • Valeva, A.; Palmer, M.; Hilgert, K.; Kehoe, M.; Bhakdi, S. Correct oligomerization is a prerequisite for insertion of the central molecular domain of staphylococcal alpha-toxin into the lipid bilayer. Biochim. Biophys. Acta Biomembr. 1995, 1236, 213-218.
    • (1995) Biochim. Biophys. Acta Biomembr. , vol.1236 , pp. 213-218
    • Valeva, A.1    Palmer, M.2    Hilgert, K.3    Kehoe, M.4    Bhakdi, S.5
  • 21
    • 0029986936 scopus 로고    scopus 로고
    • Passive immunization with antiserum to a nontoxic alpha-toxin mutant from Staphylococcus aureus is protective in a murine model
    • Menzies, B.E.; Kernodle, D.S. Passive immunization with antiserum to a nontoxic alpha-toxin mutant from Staphylococcus aureus is protective in a murine model. Infect. Immun. 1996, 64, 1839-1841.
    • (1996) Infect. Immun. , vol.64 , pp. 1839-1841
    • Menzies, B.E.1    Kernodle, D.S.2
  • 22
    • 67650079244 scopus 로고    scopus 로고
    • Anti-alpha-hemolysin monoclonal antibodies mediate protection against Staphylococcus aureus pneumonia
    • Ragle, B.E.; Wardenburg, J.B. Anti-alpha-hemolysin monoclonal antibodies mediate protection against Staphylococcus aureus pneumonia. Infect. Immun. 2009, 77, 2712-2718.
    • (2009) Infect. Immun. , vol.77 , pp. 2712-2718
    • Ragle, B.E.1    Wardenburg, J.B.2
  • 23
    • 39549121471 scopus 로고    scopus 로고
    • Vaccine protection against Staphylococcus aureus pneumonia
    • Wardenburg, J.B.; Schneewind, O. Vaccine protection against Staphylococcus aureus pneumonia. J. Exp. Med. 2008, 205, 287-294.
    • (2008) J. Exp. Med. , vol.205 , pp. 287-294
    • Wardenburg, J.B.1    Schneewind, O.2
  • 24
    • 0042553279 scopus 로고
    • Smoothing and differentiation of data by simplified least squares procedures
    • Savitzky, A.; Golay, M.J.E. Smoothing and differentiation of data by simplified least squares procedures. Anal. Chem. 1964, 36, 1627-1639.
    • (1964) Anal. Chem. , vol.36 , pp. 1627-1639
    • Savitzky, A.1    Golay, M.J.E.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.