The Site-Directed Mutagenesis of Gastrodia Anti-Fungal Protein Mannose-Binding Sites and Its Expression in Escherichia Coli
Gastrodia anti-fungal protein (GAFP) displays strong inhibitory activity against certain fungal pathogens. Five GAFP analogues with different mutations at mannose-binding sites and the wild-type one were expressed and purified in Escherichia coli. The inhibitory analysis of the purified various GAFPs against the growth of Trichoderma viride indicates that single amino acid mutated-type GAFPs have inhibitory activity, but its activity is much less than the wild-type one. The double and triplicate amino acids mutated GAFPs have very low inhibitory activity. For the first time it was proved that GAFP mannosebinding sites play key role in anti-fungi process.
Keywords: escherichia coli; expressed and purified; gafp mannose-binding sites; gastrodia anti-fungal protein; inhibitory activity; site-directed mutagenesis; trichoderma viride
Document Type: Review Article
Affiliations: Institute of Genetics and Developmental Biology, Chinese Academy of Sciences, Beijing, 100101, P.R. China.
Publication date: 01 December 2003
- Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.
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