Bacillus thuringiensis Cry1A Insecticidal Toxins and Their Digests Do Not Stimulate Histamine Release from Cultured Rat Mast Cells

Public acceptance of genetically modified crops engineered with (Bt) insecticidal protein genes (BT-GMCs), which confer resistance to various lepidopteran insect pests, is generally lacking. As a major concern over BT-GMCs is the allergenicity of insecticidal proteins, alleviating safety concerns sh...

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Published in:Biology (Basel, Switzerland) Switzerland), 2024-12, Vol.14 (1), p.15
Main Authors: Ohto, Hisashi, Ohno, Mayumi, Suganuma-Katagiri, Miho, Hara, Takashi, Egawa, Yoko, Tomimoto, Kazuya, Haginoya, Kosuke, Hori, Hidetaka, Iwamoto, Yuzuri, Hayakawa, Tohru
Format: Article
Language:English
Subjects:
Allergenicity
Allergens
Bacillus thuringiensis
Chromatography
Corn
Cry1Ac toxin
Crystal proteins
Crystals
Food allergies
Histamine
insecticidal Cry1A toxins
Mast cells
Polypeptides
Proteins
rat mast cells
RBL-2H3
safety of genetically modified crops
simulated digestive fluids
Soil microorganisms
Sporulation
Toxins
Transmembrane domains
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Summary:Public acceptance of genetically modified crops engineered with (Bt) insecticidal protein genes (BT-GMCs), which confer resistance to various lepidopteran insect pests, is generally lacking. As a major concern over BT-GMCs is the allergenicity of insecticidal proteins, alleviating safety concerns should help increase public acceptance. In this study, three lepidopteran-specific Bt toxins, Cry1Aa, Cy1Ab, and Cry1Ac, were treated with simulated digestive fluids under various conditions. Western blotting using antiserum raised against individual segments (α-helices of domain I and β-sheets of domains II and III) of Cry1Aa showed that digestion produces a variety of polypeptides. In particular, the transmembrane α4-α5 of domain I, which may retain the ability to form pores, was the most resistant to digestion. Intact Cry1A toxins and these digests were then applied to RBL-2H3 cultured rat mast cells to determine whether the toxins directly induce histamine release. However, fluorescence microscopy revealed no specific binding of Cry1A toxins to RBL-2H3 cultured rat mast cells. In addition, neither the OPA method nor HPLC analysis detected significant histamine release from mast cells treated with Cry1A toxins and these digests. Our results provide important data supporting the safety of Cry1A toxins and potentially BT-GMCs.
ISSN:2079-7737
2079-7737
DOI:10.3390/biology14010015