Research articles
ScienceAsia 49 (2023):ID 754-759 |doi:
10.2306/scienceasia1513-1874.2023.077
Characterization of a novel ETX/MTX2 domain-presenting
parasporal crystal protein from Bacillus toyonensis HSY140
strain
Yinghong Jina, Yiming Huanga, Jiali Hea, Yangyang Wanga, Yuquan Xub, Ruiping Wanga, Wenfei Zhanga,*
ABSTRACT: The soil-derived Bacillus toyonensis HSY140 strain was found to produce parasporal crystalline inclusions.
Genome sequencing and annotation did not find the three-domain Cry (3d-Cry) and Cyt toxins, but a novel mpp23-
like gene (918 bp) containing an ETX/MTX2 domain was detected. Alignment and phylogenetic analysis revealed
that the translated Mpp23-like protein had the highest homology to Cry23Aa1 (now named Mpp23Aa1, AAA22333.1).
Cloning and expression of the mpp23-like gene into the acrystalliferous Bacillus thuringiensis BMB171 (cry?
) generated
a recombinant strain able to produce elliptical parasporal crystals with the same shape as those of the HSY140 strain.
Finally, bioassay experiments indicated that the expressed Mpp23-like protein did not exhibit any activity to the
lepidopteran insects of Plutella xylostella, Helicoverpa armigera, and Spodoptera exigua and the dipteran insect of Aedes
aegypti. Altogether, we have characterized for the first time a new toxin, Mpp23-like protein, responsible for the
formation of crystalline inclusions in B. toyonensis HSY140 strain.
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| a |
Ministry of Education Key Laboratory for Ecology of Tropical Islands, Key Laboratory of Tropical Animal and Plant
Ecology of Hainan Province, College of Life Sciences, Hainan Normal University, Haikou 571158 China |
| b |
Biotechnology Research Institute, The Chinese Academy of Agricultural Sciences, Beijing 100081 China |
* Corresponding author, E-mail: wenfei2007@163.com, wfzhang@hainnu.edu.cn
Received 14 Sep 2022, Accepted 4 Jul 2023
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