V-type proton ATPase 116 kDa subunit a isoform 2 |
VVCACRRALCLPLERRAGFCRIRGRIHPLCCRR |
cytomegalovirus chemokine homolog-2 |
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[Vitis vinifera antimicrobial peptide 1] This peptide of 77 amino acids has been isolated from the berries of Vitis vinifera (de Beer and Vivier, 2008). Vv-AMP1 shows sequence homology to the family of plant defensins. Vv-AMP1 is expressed specifically in berry tissue at the onset of berry ripening and onwards. Recombinant Vv-AMP1 is extremely heat-stable and shows strong antifungal activity against a broad spectrum of plant pathogenic fungi, with very high levels of activity against the wilting disease causing pathogens Fusarium oxysporum and Verticillium dahliae. Vv-AMP1 peptide does not induce morphological changes on treated fungal hyphae, but strongly inhibits hyphal elongation.
For other proteins/peptides with functions in innate immunity and/or antimicrobial activities see also:
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