tailieunhanh - Báo cáo khóa học: Purification and functional characterization of insecticidal sphingomyelinase C produced by Bacillus cereus

Bacillus cereusisolated from the larvae of Myrmeleon bore was found to secrete proteins that paralyze and kill German cockroaches, Blattela germanica, when injected. One of these active proteins was purified from the culture broth anion-exchange and gel-filtration chro-matography. The purified toxin, with a molecular mass of 34 kDa, was identified as sphingomyelinase C () on the basis of its N-terminal and internal amino-acid sequences. A recombinant sphingomyelinase C expressed in Escherichia coliwas as potent as the native protein in killing the cockroaches | Eur. J. Biochem. 271 601-606 2004 FEBS 2004 doi Purification and functional characterization of insecticidal sphingomyelinase C produced by Bacillus cereus Hisashi Nishiwaki Katsuhiko Ito Katsuhiko Otsuki Hiroyuki Yamamoto Koichiro Komai and Kazuhiko Matsuda Department of Agricultural Chemistry Faculty of Agriculture Kinki University Nara Japan Bacillus cereus isolated from the larvae of Myrmeleon bore was found to secrete proteins that paralyze and kill German cockroaches Blattela germanica when injected. One of these active proteins was purified from the culture broth of B. cereus using anion-exchange and gel-filtration chromatography. The purified toxin with a molecular mass of 34 kDa was identified as sphingomyelinase C EC on the basis of its N-terminal and internal amino-acid sequences. A recombinant sphingomyelinase C expressed in Escherichia coli was as potent as the native protein in killing the cockroaches. Site-directed mutagenesis His151Ala that inactivated the sphingomyelinase activity also abolished the insecticidal activity suggesting that the rapid insect toxicity of sphingomyelinase C results from its phospholipiddegrading activity. Keywords antlion Bacillus cereus insecticidal activity Myrmeleon bore sphingomyelinase C. A group of antlions the larvae of lacewing Myrmeleonti-dae make pits to capture prey. Before sucking the body fluid antlions inject their regurgitant into the prey from a pair of mandibles for extra digestion. As the prey of antlions appear to be paralyzed it has been postulated that toxic factors are contained in the regurgitant. In preliminary experiments the insecticidal factors were found to be sensitive to heat and proteinase treatments indicating that they are polypeptides. Antlion Myrmeleon bore toxin has been purified from the regurgitant of larvae of M. loiee and shown to be a single polypeptide with a molecular mass of 170 kDa 1 . In addition to this toxin a GroEL homolog has .

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