메뉴 건너뛰기




Volumn 13, Issue 1, 2007, Pages 6-13

Antimicrobial activity of different proteins and their fragments from Bacillus thuringiensis parasporal crystals against clostridia and archaea

Author keywords

Antimicrobial activity; Cell walls; Clostridium butyricum; Cry proteins; Methanosarcina barkeri

Indexed keywords

BACTERIAL PROTEIN; CRY PROTEIN; CRY11A PROTEIN; CRY1AB PROTEIN; CRY1D PROTEIN; N ACETYLGALACTOSAMINE; TEICHOIC ACID; UNCLASSIFIED DRUG;

EID: 33847081533     PISSN: 10759964     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.anaerobe.2006.09.006     Document Type: Article
Times cited : (24)

References (26)
  • 1
    • 33847080937 scopus 로고    scopus 로고
    • Crickmore N. Full list of delta-endotoxins. 2006. 〈http://www.lifesci.sussex.ac.uk/home/Neil_Crickmore/Bt/toxins2.html〉.
  • 3
    • 24944523268 scopus 로고    scopus 로고
    • Partial restoration of antibacterial activity of the protein encoded by a cryptic open reading frame (cytCa) from Bacillus thuringiensis subsp. israelensis by site-directed mutagenesis
    • Itsko M., Manasherob R., and Zaritsky A. Partial restoration of antibacterial activity of the protein encoded by a cryptic open reading frame (cytCa) from Bacillus thuringiensis subsp. israelensis by site-directed mutagenesis. J Bacteriol 187 (2005) 6379-6385
    • (2005) J Bacteriol , vol.187 , pp. 6379-6385
    • Itsko, M.1    Manasherob, R.2    Zaritsky, A.3
  • 5
    • 33847018192 scopus 로고    scopus 로고
    • Yudina TG, Zalunin IA, Revina LP, Kostina LI. The determination of antibacterial activity of delta-endotoxins of Bacillus thuringiensis and their fragments during investigation of structural and functional organization. Abstracts of IX International Congress on Bacteriology and Applied Microbiology, IUMS, Australia, Sydney, BPO11.06, 1999. p. 86.
  • 6
    • 33746783839 scopus 로고    scopus 로고
    • Activity of δ-endotoxins of four Bacillus thuringiensis subspecies against prokaryotes
    • Yudina T.G., and Burtseva L.I. Activity of δ-endotoxins of four Bacillus thuringiensis subspecies against prokaryotes. Microbiology (Moscow) 66 (1997) 25-31
    • (1997) Microbiology (Moscow) , vol.66 , pp. 25-31
    • Yudina, T.G.1    Burtseva, L.I.2
  • 7
    • 3442900602 scopus 로고    scopus 로고
    • Susceptibility of archaea to the antibiotic effect of the parasporal inclusion proteins from different Bacillus thuringiensis subspecies
    • Yudina T.G., Bryukhanov A.L., and Netrusov A.I. Susceptibility of archaea to the antibiotic effect of the parasporal inclusion proteins from different Bacillus thuringiensis subspecies. Microbiology (Moscow) 73 (2004) 19-23
    • (2004) Microbiology (Moscow) , vol.73 , pp. 19-23
    • Yudina, T.G.1    Bryukhanov, A.L.2    Netrusov, A.I.3
  • 8
    • 0034551727 scopus 로고    scopus 로고
    • Impact of oxygen on metabolic fluxes and in situ rates of reductive acetogenesis in the hindgut of the wood-feeding termite Reticulitermes flavipes
    • Tholen A., and Brune A. Impact of oxygen on metabolic fluxes and in situ rates of reductive acetogenesis in the hindgut of the wood-feeding termite Reticulitermes flavipes. Environ Microbiol 2 (2000) 436-449
    • (2000) Environ Microbiol , vol.2 , pp. 436-449
    • Tholen, A.1    Brune, A.2
  • 9
    • 0034020328 scopus 로고    scopus 로고
    • Localization of symbiotic clostridia in the mixed segment of the termite Nasutitermes takasagoensis (Shiraki)
    • Tokuda G., Yamaoka I., and Noda H. Localization of symbiotic clostridia in the mixed segment of the termite Nasutitermes takasagoensis (Shiraki). Appl Environ Microbiol 66 (2000) 2199-2207
    • (2000) Appl Environ Microbiol , vol.66 , pp. 2199-2207
    • Tokuda, G.1    Yamaoka, I.2    Noda, H.3
  • 11
    • 0023411977 scopus 로고
    • Early changes in bacterial envelopes after inhibition of peptidoglycan synthesis, as shown by the use of a fluorescent probe
    • Rogers H.J., and Wright G. Early changes in bacterial envelopes after inhibition of peptidoglycan synthesis, as shown by the use of a fluorescent probe. J Gen Microbiol 133 (1987) 2567-2572
    • (1987) J Gen Microbiol , vol.133 , pp. 2567-2572
    • Rogers, H.J.1    Wright, G.2
  • 12
    • 0034082178 scopus 로고    scopus 로고
    • Surface of lactic acid bacteria: relationships between chemical composition and physicochemical properties
    • Boonaert C., and Rouxhet P. Surface of lactic acid bacteria: relationships between chemical composition and physicochemical properties. Appl Environ Microbiol 66 (2000) 2548-2554
    • (2000) Appl Environ Microbiol , vol.66 , pp. 2548-2554
    • Boonaert, C.1    Rouxhet, P.2
  • 13
    • 0019013770 scopus 로고
    • Crystal-forming proteins of Bacillus thuringiensis. The limited hydrolysis by endogenous proteases as a cause of their apparent multiplicity
    • Chestukhina G.G., Zalunin I.A., Kotova T.S., Kostina L.I., Katrukha S.P., and Stepanov V.M. Crystal-forming proteins of Bacillus thuringiensis. The limited hydrolysis by endogenous proteases as a cause of their apparent multiplicity. Biochem J 187 (1980) 457-465
    • (1980) Biochem J , vol.187 , pp. 457-465
    • Chestukhina, G.G.1    Zalunin, I.A.2    Kotova, T.S.3    Kostina, L.I.4    Katrukha, S.P.5    Stepanov, V.M.6
  • 14
    • 0000549132 scopus 로고
    • Carbonic anhydrase activity in acetate-grown Methanosarcina barkeri
    • Karrasch M., Bott M., and Thauer R.K. Carbonic anhydrase activity in acetate-grown Methanosarcina barkeri. Arch Microbiol 151 (1989) 137-142
    • (1989) Arch Microbiol , vol.151 , pp. 137-142
    • Karrasch, M.1    Bott, M.2    Thauer, R.K.3
  • 16
  • 17
    • 0028670834 scopus 로고
    • Production of multiple δ-endotoxins by Bacillus thuringiensis: δ-endotoxins produced by strains of the subspecies galleriae and wuhanensis
    • Chestukhina G.G., Kostina L.I., Zalunin I.A., Revina L.P., Mikhailova A.L., and Stepanov V.M. Production of multiple δ-endotoxins by Bacillus thuringiensis: δ-endotoxins produced by strains of the subspecies galleriae and wuhanensis. Can J Microbiol 40 (1994) 1026-1034
    • (1994) Can J Microbiol , vol.40 , pp. 1026-1034
    • Chestukhina, G.G.1    Kostina, L.I.2    Zalunin, I.A.3    Revina, L.P.4    Mikhailova, A.L.5    Stepanov, V.M.6
  • 18
    • 0031182629 scopus 로고    scopus 로고
    • Intramolecular proteolytic cleavage of Bacillus thuringiensis Cry3A δ-endotoxin may facilitate its coleopteran toxicity
    • Carroll J., Convents D., Van Damme J., Boets A., Van Rie J., and Ellar D.J. Intramolecular proteolytic cleavage of Bacillus thuringiensis Cry3A δ-endotoxin may facilitate its coleopteran toxicity. J Invertebrate Pathol 70 (1997) 41-49
    • (1997) J Invertebrate Pathol , vol.70 , pp. 41-49
    • Carroll, J.1    Convents, D.2    Van Damme, J.3    Boets, A.4    Van Rie, J.5    Ellar, D.J.6
  • 21
    • 0025822526 scopus 로고
    • Structural features of cell wall teichoic acid and peptidoglycan of Actinomadura cremea INA 292
    • Potekhina N.V., Naumova I.B., Shashkov A.S., and Terekhova L.P. Structural features of cell wall teichoic acid and peptidoglycan of Actinomadura cremea INA 292. Eur J Biochem 199 (1991) 313-316
    • (1991) Eur J Biochem , vol.199 , pp. 313-316
    • Potekhina, N.V.1    Naumova, I.B.2    Shashkov, A.S.3    Terekhova, L.P.4
  • 22
    • 33847008775 scopus 로고    scopus 로고
    • Sensitivity of Micrococcus luteus dissociation variants to δ-endotoxins of Bacillus thuringiensis
    • Yudina T.G., Mil'ko E.S., and Egorov N.S. Sensitivity of Micrococcus luteus dissociation variants to δ-endotoxins of Bacillus thuringiensis. Microbiology (Moscow) 61 (1996) 577-584
    • (1996) Microbiology (Moscow) , vol.61 , pp. 577-584
    • Yudina, T.G.1    Mil'ko, E.S.2    Egorov, N.S.3
  • 23
    • 3142610852 scopus 로고    scopus 로고
    • Cryptic endotoxic nature of Bacillus thuringiensis Cry1Ab insecticidal crystal protein
    • Vazgues-Padron R.I., de la Riva G., Aguero G., Silva Y., Pham S.M., Soberon M., et al. Cryptic endotoxic nature of Bacillus thuringiensis Cry1Ab insecticidal crystal protein. FEBS Lett 570 (2004) 30-36
    • (2004) FEBS Lett , vol.570 , pp. 30-36
    • Vazgues-Padron, R.I.1    de la Riva, G.2    Aguero, G.3    Silva, Y.4    Pham, S.M.5    Soberon, M.6
  • 24
    • 7744222624 scopus 로고    scopus 로고
    • Oligomerization triggers binding of a Bacillus thuringiensis Cry1Ab pore-forming toxin to aminopeptidase N receptor leading to insertion into membrane microdomains
    • Bravo A., Gomez I., Conde J., Munoz-Garay C., Sanchez J., Miranda R., et al. Oligomerization triggers binding of a Bacillus thuringiensis Cry1Ab pore-forming toxin to aminopeptidase N receptor leading to insertion into membrane microdomains. Biochim Biophys Acta 1667 (2004) 38-46
    • (2004) Biochim Biophys Acta , vol.1667 , pp. 38-46
    • Bravo, A.1    Gomez, I.2    Conde, J.3    Munoz-Garay, C.4    Sanchez, J.5    Miranda, R.6
  • 25
    • 33847078123 scopus 로고    scopus 로고
    • Yudina TG, Zalunin IA, Chestukhina GG. 2006, Unpublished data.
  • 26
    • 19444374889 scopus 로고    scopus 로고
    • Fusobacterium necrophorum infections in animals: pathogenesis and pathogenic mechanism
    • Nagaraja T.G., Narayanan G.C., Stewart M.M., and Chengappa M.M. Fusobacterium necrophorum infections in animals: pathogenesis and pathogenic mechanism. Anaerobe 11 (2005) 239-246
    • (2005) Anaerobe , vol.11 , pp. 239-246
    • Nagaraja, T.G.1    Narayanan, G.C.2    Stewart, M.M.3    Chengappa, M.M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.