HOST-MEDIATED INDUCTION OF alpha-AMYLASES BY LARVAE OF THE MEXICAN BEAN WEEVIL Zabrotes subfasciatus (COLEOPTERA: CHRYSOMELIDAE: BRUCHINAE) IS IRREVERSIBLE AND OBSERVED FROM THE INITIATION OF THE FEEDING PERIOD
Contribuinte(s) |
UNIVERSIDADE DE SÃO PAULO |
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Data(s) |
20/10/2012
20/10/2012
2010
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Resumo |
Larvae of Zabrotes subfasciatus secrete alpha-amylases that are insensitive to the alpha-amylase inhibitor found in seeds of Phaseolus vulgaris. By analyzing amylase activities during larval development on P. vulgaris, we detected activity of the constitutive amylase and the two inducible amylase isoforms at all stages. When larvae were transferred from the non alpha-amylase inhibitor containing seeds of Vigna unguiculata to P. vulgaris, the inducible alpha-amylases were expressed at the same level as in control larvae fed on P. vulgaris. Interestingly, when larvae were transferred from seeds of P. vulgaris to those of V. unguiculata, inducible alpha-amylases continued to be expressed at a level similar to that found in control larvae fed P. vulgaris continuously. When 10-day-old larvae were removed from seeds of V. unguiculata and transferred into capsules containing flour of P. vulgaris cotyledons, and thus maintained until completing 17 days ( age when the larvae stopped feeding), we could detect higher activity of the inducible alpha-amylases. However, when larvae of the same age were transferred from P. vulgaris into capsules containing flour of V. unguiculata, the inducible alpha-amylases remained up-regulated. These results suggest that the larvae of Z. subfasciatus have the ability to induce insensitive amylases early in their development. A short period of feeding on P. vulgaris cotyledon flour was sufficient to irreversibly induce the inducible alpha-amylase isoforms. Incubations of brush border membrane vesicles with the alpha-amylase inhibitor 1 from P. vulgaris suggest that the inhibitor is recognized by putative receptors found in the midgut microvillar membranes. (C) 2010 Wiley Periodicals, Inc. Fundação de Amparo à Pesquisa do Estado do Rio de Janeiro (FAPERJ) FAPERJ CNPq Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq) |
Identificador |
ARCHIVES OF INSECT BIOCHEMISTRY AND PHYSIOLOGY, v.74, n.4, p.247-260, 2010 0739-4462 http://producao.usp.br/handle/BDPI/28677 10.1002/arch.20375 |
Idioma(s) |
eng |
Publicador |
WILEY-BLACKWELL |
Relação |
Archives of Insect Biochemistry and Physiology |
Direitos |
restrictedAccess Copyright WILEY-BLACKWELL |
Palavras-Chave | #induction of alpha-amylase #alpha-amylase inhibitor #insect digestion #Vigna unguiculata #Phaseolus vulgaris #PHASEOLUS-VULGARIS L #PROTEINASE-INHIBITORS #BICINCHONINIC ACID #SERINE PROTEINASES #STARCH GRANULES #ADAPTATION #MIDGUT #RESISTANCE #PROTEASE #DEFENSE #Biochemistry & Molecular Biology #Entomology #Physiology |
Tipo |
article original article publishedVersion |