Inhibition of Growth of Aspergillus flavus and Fungal α-Amylases by a Lectin-Like Protein from Lablab purpureus
Autor: | C. P. Woloshuk, A. M. Fakhoury |
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Rok vydání: | 2001 |
Předmět: |
Hyphal growth
Aflatoxin Antifungal Agents Lablab purpureus Physiology Molecular Sequence Data Aspergillus flavus Biology Plant disease resistance Microbiology Endosperm chemistry.chemical_compound food Aflatoxins Lectins Amino Acid Sequence Enzyme Inhibitors Mycotoxin Plant Diseases Plant Proteins Sequence Homology Amino Acid fungi food and beverages Fabaceae General Medicine Fungi imperfecti biology.organism_classification food.food Biochemistry chemistry Plant Lectins alpha-Amylases Agronomy and Crop Science |
Zdroj: | Molecular Plant-Microbe Interactions®. 14:955-961 |
ISSN: | 1943-7706 0894-0282 |
DOI: | 10.1094/mpmi.2001.14.8.955 |
Popis: | Aspergillus flavus is a fungal pathogen of maize causing an important ear rot disease when plants are exposed to drought and heat stress. Associated with the disease is the production of aflatoxins, which are a series of structurally related mycotoxins known to be carcinogenic. Previous research has suggested that the alpha-amylase of A. flavus promotes aflatoxin production in the endosperm of infected maize kernels. We report here the isolation and characterization of a 36-kDa alpha-amylase inhibitor from Lablab purpureus (AILP). AILP inhibited the alpha-amylases from several fungi but had little effect on those from animal and plant sources. The protein inhibited conidial germination and hyphal growth of A. flavus. The amino acid sequence indicated that AILP is similar to lectin members of a lectin-arcelin-alpha-amylase inhibitor family described in common bean and shown to be a component of plant resistance to insect pests. AILP also agglutinated papain-treated red blood cells from human and rabbit. These data indicate that AILP represents a novel variant in the lectin-arcelin-alpha-amylase inhibitor family of proteins having lectin-like and alpha-amylase inhibitory activity. |
Databáze: | OpenAIRE |
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