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Clinical and Diagnostic Laboratory Immunology, July 2000, p. 625-634, Vol. 7, No. 4
Biotechnology & Food Research Institute,
Fukuoka Industrial Technology Center,1 and
Graduate School of Bioresource and Bioenvironmental Sciences,
Kyushu University,2 Fukuoka, Japan
Received 29 November 1999/Returned for modification 25 January
2000/Accepted 22 March 2000
An unusual property, human leukemic cell-recognizing activity,
associated with parasporal inclusions of a noninsecticidal Bacillus thuringiensis soil isolate was investigated, and a
protein (named parasporin in this study) responsible for the activity was cloned. The parasporin, encoded by a gene 2,169 bp long, was a
polypeptide of 723 amino acid residues with a predicted molecular weight of 81,045. The sequence of parasporin contained the five conserved blocks commonly found in B. thuringiensis Cry
proteins; however, only very low homologies (<25%) between parasporin
and the existing classes of Cry and Cyt proteins were detected.
Parasporin exhibited cytocidal activity only when degraded by proteases
into smaller molecules of 40 to 60 kDa. Trypsin and proteinase K
activated parasporin, while chymotrypsin did not. The activated
parasporin showed strong cytocidal activity against human leukemic T
cells (MOLT-4) and human uterus cervix cancer cells (HeLa) but not
against normal T cells.
1071-412X/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.
Parasporin, a Human Leukemic Cell-Recognizing
Parasporal Protein of Bacillus thuringiensis

*
Corresponding author. Mailing address: Biotechnology & Food Research Institute, Fukuoka Industrial Technology Center,
Aikawa-machi 1465-5, Kurume, Fukuoka 839-0861, Japan. Phone:
81(942)30-6644. Fax: 81(942)30-7244. E-mail:
emizuki{at}fitc.pref.fukuoka.jp.
Present address: Department of Life Science, Pohang University of
Science and Technology, Pohang, Kyungbuk 790-784, Republic of Korea.
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