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Legume seed vicilins (7S storage proteins) interfere with the development of the cowpea weevil ( Callosobruchus maculatus (F))
Author(s) -
Yunes Andréa Neila A,
de Andrade Maria Tereza,
Sales Maurício P,
Morais Rosana A,
Fernandes Kátia Valevski S,
Gomes Valdirene M,
XavierFilho José
Publication year - 1998
Publication title -
journal of the science of food and agriculture
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.782
H-Index - 142
eISSN - 1097-0010
pISSN - 0022-5142
DOI - 10.1002/(sici)1097-0010(199801)76:1<111::aid-jsfa932>3.0.co;2-4
Subject(s) - callosobruchus maculatus , vigna , canavalia ensiformis , phaseolus , biology , legume , weevil , lima beans , vicilin , storage protein , botany , horticulture , pest analysis , biochemistry , gene
Vicilins (7S storage proteins) isolated from the seeds of the legumes Vigna unguiculata (cowpea), Vigna angularis (adzuki bean), Canavalia ensiformis (jack bean), Glycine max (soybean), Phaseolus vulgaris (common bean) and Phaseolus lunatus (lima bean) were shown to be immunologically related and to bind to a chitin matrix. The effect of the isolated vicilins on the development of the cowpea weevil Callosobruchus maculatus was examined. Vicilins from all non‐host seeds, including those of the C maculatus ‐resistant cowpea line IT81D‐1045, strongly inhibited larval development (ED 50 of 1·07±0·32% to 2·22±0·64%). Vicilins from the C maculatus ‐susceptible cowpea CE‐31 and adzuki bean seeds were the exception with ED 50 of 6·25±0·75% and 5·40±1·54%, respectively. These results correlate well with the host range of C maculatus and are possibly a reflection of the low digestibility of vicilins by insect midgut proteinases in addition to the ability they show in binding to chitin‐containing structures like the ones found in the bruchid midguts. © 1998 SCI.