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Screening of peptides binding on total cell extracts of Phytophthora capsici by phage display
Author(s) -
Park Hyeyeon,
Kim SungKun,
Yoon MoonYoung
Publication year - 2009
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.23.1_supplement.676.5
Subject(s) - phytophthora capsici , pepper , oomycete , blight , phytophthora , phage display , biology , biopanning , pathogen , plant disease , peptide library , peptide , botany , horticulture , microbiology and biotechnology , biochemistry , peptide sequence , gene
Phytophthora blight, caused by the oomycete pathogen Phytophthora capsici Leonian, is a completely destructive disease running rampant on the pepper plant, Capsicum annum. This blight is pronounced in regions where the pepper is commonly consumed and grown such as Korea as well as other parts of the world. At large, the main nuisance that has been reported about the Phytophthora disease is its responsibility for the major cultivation losses of the peppers. However, an even graver concern is that the pathogen can survive in the soil devoid of any host plants for many years. Therefore, P. capsici has been an attractive target for the prevention and diagnostics of Phytophthora blight of peppers. Recently, it has been reported that the molecule consists of multiple copies of P. capsici‐binding peptide, which is broadly applicable to the rapid development of plant defense mechanisms against novel plant disease resistance strategy. We screened P. capsici‐binding peptides using a M13 phage display method. In the course of 5 round biopanning, we identified P. capsici protein surface‐binding peptides from an M13 random peptide library, which was originally screened for other novel peptides that bind to P. capsici with a high affinity (picomolar range). As the result of identifying these peptides, they can be used as a basis to develop new potent inhibitors or diagnostic probes with a diverse polyvalence.