Parasporin-2Ab, a newly isolated cytotoxic crystal protein from Bacillus thuringiensis

Tohru Hayakawa, Rie Kanagawa, Yosuke Kotani, Mayumi Kimura, Masashi Yamagiwa, Yoshiharu Yamane, So Takebe, Hiroshi Sakai

Research output: Contribution to journalArticle

19 Citations (Scopus)

Abstract

A novel crystal protein that exhibited potent cytotoxicity against human leukemic T-cells was cloned from the Bacillus thuringiensis TK-E6 strain. The protein, designated as parasporin-2Ab (PS2Ab), was a polypeptide of 304 amino acid residues with a predicted molecular weight of 33,017. The deduced amino acid sequence of PS2Ab showed significant homology (84% identitiy) to parasporin-2Aa (PS2Aa) from the B. thuringiensis A1547 strain. Upon processing of PS2Ab with proteinase K, the active form of 29 kDa was produced. The activated PS2Ab showed potent cytotoxicity against MOLT-4 and Jurkat cells and the EC50 values were estimated as 0.545 and 0.745 ng/mL, respectively. The cytotoxicity of PS2Ab was significantly higher than that of PS2Aa reported elsewhere. Although both cytotoxins were structurally related, it was thought that the minor differences found were responsible for the different cytotoxicities of PS2Ab and PS2Aa.

Original languageEnglish
Pages (from-to)278-283
Number of pages6
JournalCurrent Microbiology
Volume55
Issue number4
DOIs
Publication statusPublished - Oct 2007

Fingerprint

Bacillus thuringiensis
parasporin
Bacillus Thuringiensis insecticidal crystal protein
Endopeptidase K
Jurkat Cells
Cytotoxins
Amino Acid Sequence
Proteins
Molecular Weight
T-Lymphocytes
Amino Acids
Peptides

ASJC Scopus subject areas

  • Microbiology

Cite this

Hayakawa, T., Kanagawa, R., Kotani, Y., Kimura, M., Yamagiwa, M., Yamane, Y., ... Sakai, H. (2007). Parasporin-2Ab, a newly isolated cytotoxic crystal protein from Bacillus thuringiensis. Current Microbiology, 55(4), 278-283. https://doi.org/10.1007/s00284-006-0351-8

Parasporin-2Ab, a newly isolated cytotoxic crystal protein from Bacillus thuringiensis. / Hayakawa, Tohru; Kanagawa, Rie; Kotani, Yosuke; Kimura, Mayumi; Yamagiwa, Masashi; Yamane, Yoshiharu; Takebe, So; Sakai, Hiroshi.

In: Current Microbiology, Vol. 55, No. 4, 10.2007, p. 278-283.

Research output: Contribution to journalArticle

Hayakawa, T, Kanagawa, R, Kotani, Y, Kimura, M, Yamagiwa, M, Yamane, Y, Takebe, S & Sakai, H 2007, 'Parasporin-2Ab, a newly isolated cytotoxic crystal protein from Bacillus thuringiensis', Current Microbiology, vol. 55, no. 4, pp. 278-283. https://doi.org/10.1007/s00284-006-0351-8
Hayakawa, Tohru ; Kanagawa, Rie ; Kotani, Yosuke ; Kimura, Mayumi ; Yamagiwa, Masashi ; Yamane, Yoshiharu ; Takebe, So ; Sakai, Hiroshi. / Parasporin-2Ab, a newly isolated cytotoxic crystal protein from Bacillus thuringiensis. In: Current Microbiology. 2007 ; Vol. 55, No. 4. pp. 278-283.
@article{1726501127ec4db4b32bd66bdeecc9ba,
title = "Parasporin-2Ab, a newly isolated cytotoxic crystal protein from Bacillus thuringiensis",
abstract = "A novel crystal protein that exhibited potent cytotoxicity against human leukemic T-cells was cloned from the Bacillus thuringiensis TK-E6 strain. The protein, designated as parasporin-2Ab (PS2Ab), was a polypeptide of 304 amino acid residues with a predicted molecular weight of 33,017. The deduced amino acid sequence of PS2Ab showed significant homology (84{\%} identitiy) to parasporin-2Aa (PS2Aa) from the B. thuringiensis A1547 strain. Upon processing of PS2Ab with proteinase K, the active form of 29 kDa was produced. The activated PS2Ab showed potent cytotoxicity against MOLT-4 and Jurkat cells and the EC50 values were estimated as 0.545 and 0.745 ng/mL, respectively. The cytotoxicity of PS2Ab was significantly higher than that of PS2Aa reported elsewhere. Although both cytotoxins were structurally related, it was thought that the minor differences found were responsible for the different cytotoxicities of PS2Ab and PS2Aa.",
author = "Tohru Hayakawa and Rie Kanagawa and Yosuke Kotani and Mayumi Kimura and Masashi Yamagiwa and Yoshiharu Yamane and So Takebe and Hiroshi Sakai",
year = "2007",
month = "10",
doi = "10.1007/s00284-006-0351-8",
language = "English",
volume = "55",
pages = "278--283",
journal = "Current Microbiology",
issn = "0343-8651",
publisher = "Springer New York",
number = "4",

}

TY - JOUR

T1 - Parasporin-2Ab, a newly isolated cytotoxic crystal protein from Bacillus thuringiensis

AU - Hayakawa, Tohru

AU - Kanagawa, Rie

AU - Kotani, Yosuke

AU - Kimura, Mayumi

AU - Yamagiwa, Masashi

AU - Yamane, Yoshiharu

AU - Takebe, So

AU - Sakai, Hiroshi

PY - 2007/10

Y1 - 2007/10

N2 - A novel crystal protein that exhibited potent cytotoxicity against human leukemic T-cells was cloned from the Bacillus thuringiensis TK-E6 strain. The protein, designated as parasporin-2Ab (PS2Ab), was a polypeptide of 304 amino acid residues with a predicted molecular weight of 33,017. The deduced amino acid sequence of PS2Ab showed significant homology (84% identitiy) to parasporin-2Aa (PS2Aa) from the B. thuringiensis A1547 strain. Upon processing of PS2Ab with proteinase K, the active form of 29 kDa was produced. The activated PS2Ab showed potent cytotoxicity against MOLT-4 and Jurkat cells and the EC50 values were estimated as 0.545 and 0.745 ng/mL, respectively. The cytotoxicity of PS2Ab was significantly higher than that of PS2Aa reported elsewhere. Although both cytotoxins were structurally related, it was thought that the minor differences found were responsible for the different cytotoxicities of PS2Ab and PS2Aa.

AB - A novel crystal protein that exhibited potent cytotoxicity against human leukemic T-cells was cloned from the Bacillus thuringiensis TK-E6 strain. The protein, designated as parasporin-2Ab (PS2Ab), was a polypeptide of 304 amino acid residues with a predicted molecular weight of 33,017. The deduced amino acid sequence of PS2Ab showed significant homology (84% identitiy) to parasporin-2Aa (PS2Aa) from the B. thuringiensis A1547 strain. Upon processing of PS2Ab with proteinase K, the active form of 29 kDa was produced. The activated PS2Ab showed potent cytotoxicity against MOLT-4 and Jurkat cells and the EC50 values were estimated as 0.545 and 0.745 ng/mL, respectively. The cytotoxicity of PS2Ab was significantly higher than that of PS2Aa reported elsewhere. Although both cytotoxins were structurally related, it was thought that the minor differences found were responsible for the different cytotoxicities of PS2Ab and PS2Aa.

UR - http://www.scopus.com/inward/record.url?scp=34648817546&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=34648817546&partnerID=8YFLogxK

U2 - 10.1007/s00284-006-0351-8

DO - 10.1007/s00284-006-0351-8

M3 - Article

VL - 55

SP - 278

EP - 283

JO - Current Microbiology

JF - Current Microbiology

SN - 0343-8651

IS - 4

ER -