Isolation of pisumin, a novel antifungal protein from legumes of the sugar snap pea Pisum sativum var. macrocarpon

A novel antifungal protein from seeds of Sesbania virgata (Cav.) Pers. (Leguminosae-Faboideae)

“…A similar range of antifungal activity compared to various fungi was ascribed to other antifungal proteins at concentrations from 0.5 to 25 mg.mL -1 Almeida et al, 2000). Differences in the growth-inhibitory activity of F1 and F2 on the assayed fungal species were probably due to differences in fungal sensitivity, which has been reported for other proteins (Ye et al, 2000). However, after purification on the C-8 reversed phase column, no activity was found among fractions.…”

“…Antifungal proteins and peptides with molecular masses ranging from 5 to 38 kDa were isolated from legume seeds (Ye et al, 2000;Ng, 2002, 2005;.…”

“…These seed proteins can be modified by endogenous proteinases causing the release of antifungal peptides that, together with constitutive proteins, can act as a precocious defensive system during both germination and early stages of plant development (Wang et al, 2002). Proteins having important biological activities have been detected in seeds of leguminous plants such as Pisum sativum (Almeida et al, 2000;Ye et al, 2000), Phaseolus vulgaris (Wong and Ng, 2005), Phaseolus mungo (Wang et al, 2004;Ye and Ng, 2005), Glycine max (Krishnaveni et al, 1999), Vigna unguiculata (Gomes et al, 1998;Carvalho et al, 2001), Cicer arietinum (Ye et al, 2002) and Delandia umbellata (Ye and Ng, 2002).…”

Isolation and characterization of a 29-kDa glycoprotein with antifungal activity from bulbs of Urginea indica

“…When antifungal activity of U. indica protein is compared with those of other antifungal proteins, it is observed that Urginea protein displays a much broader specificity than others. Antifungal 28 kDa protein isolated from cowpea [35], 38 kDa Sativin from Pisum sativum [36], exerts a similar effect on F. oxysporum but not against R. solani. Microscopic observations on morphology of the fungus have shown that growth inhibition by some antifungal proteins is due to swelling and lysis of hyphae [4,11].…”

A Bowman–Birk-Type Trypsin-Chymotrypsin Inhibitor from Broad Beans

“…To date a diversity of antifungal proteins with different amino acid sequences has been isolated. Based on their structures or activities antifungal proteins have been classified into chitinases (1)(2)(3)(4)(5)(6), glucanases (2), thaumatin-like proteins (7,8), miraculin-like proteins (9), cyclophilin-like proteins (10), allergen-like proteins (11), embryo-abundant protein-like proteins (12), ribosome inactivating proteins (13,14), and antifungal peptides (15).…”