Purification and partial amino acid sequence of thuricin S, a new anti-Listeriabacteriocin from Bacillus thuringiensis

2007 ◽  
Vol 53 (2) ◽  
pp. 284-290 ◽  
Author(s):  
Sonia Chehimi ◽  
François Delalande ◽  
Sophie Sablé ◽  
Mohamed-Rabeh Hajlaoui ◽  
Alain Van Dorsselaer ◽  
...  

We report the isolation and characterization of a new bacteriocin, thuricin S, produced by the Bacillus thuringiensis subsp. entomocidus HD198 strain. This antibacterial activity is sensitive to proteinase K, is heat-stable, and is stable at a variety of pH values (3–10.5). The monoisotopic mass of thuricin S purified by high perfomance liquid chromatography, as determined with mass spectrometry ESI-TOF-MS, is 3137.61 Da. Edman sequencing and NanoESI-MS/MS experiments provided the sequence of the 18 N-terminal amino acids. Interestingly, thuricin S has the same N-terminal sequence (DWTXWSXL) as bacthuricin F4 and thuricin 17, produced by B. thuringiensis strains BUPM4 and NEB17, respectively, and could therefore be classified as a new subclass IId bacteriocin.

1984 ◽  
Vol 9 (4) ◽  
pp. 399-414 ◽  
Author(s):  
Charles Gerday ◽  
Marianne Herman ◽  
Jacques Olivy ◽  
Nicole Gerardin-Otthiers ◽  
Dominique Art ◽  
...  

2017 ◽  
Vol 39 (4) ◽  
pp. 417
Author(s):  
Janaina Zorzetti ◽  
Ana Paula Scaramal Ricietto ◽  
Fernanda Aparecida Pires Fazion ◽  
Ana Maria Meneguim ◽  
Pedro Manuel Oliveira Janeiro Neves ◽  
...  

2015 ◽  
Vol 10 (28) ◽  
pp. 2748-2755 ◽  
Author(s):  
Kassogue Adounigna ◽  
Maiga Kadia ◽  
Traore Diakaridia ◽  
Hamadoun Dicko Amadou ◽  
Fane Rokiatou ◽  
...  

2000 ◽  
Vol 46 (10) ◽  
pp. 913-919 ◽  
Author(s):  
Satoko Yamashita ◽  
Tetsuyuki Akao ◽  
Eiichi Mizuki ◽  
Hiroyuki Saitoh ◽  
Kazuhiko Higuchi ◽  
...  

An unusual activity, associated with non-insecticidal and non-haemolytic parasporal inclusion proteins of a Bacillus thuringiensis soil isolate, designated 89-T-26-17, was characterized. The parasporal inclusion of this isolate was bipyramidal, rounded at both ends, containing proteins of 180, 150, 120, 100, and 88 kDa. No homologies with the Cry and Cyt proteins of B. thuringiensis were detected based on N-terminal sequences. Proteolytic processing of the inclusion proteins by proteinase K, trypsin, and chymotrypsin produced a major protein of 64 kDa exhibiting cytocidal activity against human leukaemic T cells and uterus cervix cancer (HeLa) cells. The protease-activated proteins showed no cytotoxicity to normal T cells.Key words: Bacillus thuringiensis parasporal inclusion, non-insecticidal, non-haemolytic, cytocidal activity, human cancer cell.


2018 ◽  
Vol 64 (3) ◽  
pp. 183-190 ◽  
Author(s):  
Yingying Xiang ◽  
Shuang Wang ◽  
Jiankai Li ◽  
Yunlin Wei ◽  
Qi Zhang ◽  
...  

As the “kidneys of the Earth”, wetlands play important roles as biodiversity reservoirs, in water purification, and in flood control. In this study, 2 lytic cold-active bacteriophages, named VW-6S and VW-6B, infecting Pseudomonas fluorescens W-6 cells from the Napahai plateau wetland in China were isolated and characterized. Electron microscopy showed that both VW-6S and VW-6B had an icosahedral head (66.7 and 61.1 nm, respectively) and a long tail (8.3 nm width × 233.3 nm length and 11.1 nm width × 166.7 nm length, respectively). The bacteriophages VW-6S and VW-6B were classified as Siphoviridae and had an approximate genome size of 30–40 kb. The latent and burst periods of VW-6S were 60 and 30 min, whereas those of VW-6B were 30 and 30 min, respectively. The optimal pH values for the bacteriophages VW-6S and VW-6B were 8.0 and 10.0, respectively, and their activity decreased rapidly at temperatures higher than 60 °C. These cold-active bacteriophages provide good materials for further study of cold-adaptation mechanisms and interaction with the host P. fluorescens.


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