Expression and characterization of two domains of Pinellia ternata agglutinin (PTA), a plant agglutinin from Pinellia ternata with antifungal activity

Pinellia ternata agglutinin (PTA) from P. ternata f. angustata is a two-domain GNA-related lectin. The current study indicates that the PTA gene encodes a precursor consisting of two tandemly arrayed domains, N-terminal domain (PTA-DOM1) and C-terminal domain (PTA-DOM2). Both domains and the precurs...

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Bibliographic Details
Published in:World journal of microbiology & biotechnology 2010-03, Vol.26 (3), p.545-554
Main Authors: Ling, Li-Jun, Yang, Yan-Zhuo, Bi, Yu-Rong
Format: Article
Language:English
Subjects:
Antimicrobial agents
Applied Microbiology
Bacterial proteins
Binding sites
Biochemistry
Biological and medical sciences
Biomedical and Life Sciences
Biotechnology
Carbohydrates
Cloning
Crops
E coli
Environmental Engineering/Biotechnology
Flowers & plants
Fundamental and applied biological sciences. Psychology
Fungi
Gene expression
Lectins
Life Sciences
Microbiology
Original Paper
Pathogens
Peptides
Plant protection
Proteins
Studies
Transgenic plants
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Summary:Pinellia ternata agglutinin (PTA) from P. ternata f. angustata is a two-domain GNA-related lectin. The current study indicates that the PTA gene encodes a precursor consisting of two tandemly arrayed domains, N-terminal domain (PTA-DOM1) and C-terminal domain (PTA-DOM2). Both domains and the precursor without signal peptide (PTA-P) present different number of activity mannose-binding sites which play key roles for the lectin function. Analyses of the three fusion proteins, PTA-DOM1, PTA-DOM2 and PTA-P, expressed in Escherichia coli revealed that one mannose-binding site the agglutination activity while the additional sites do not possess such activity. However, the number of carbohydrate-binding sites suggests some significant properties on the antifungal effectiveness. In addition, each of the PTA domains has the same function when compared with the natural PTA (N-PTA). The information on PTA gene obtained in this study will served as baseline information in developing this protein as a form of transgenic plant protection.
ISSN:0959-3993
1573-0972
DOI:10.1007/s11274-009-0204-2