The toxicity of Jack bean (Canavalia ensiformis) cotyledon and seed coat proteins to the cowpea weevil (Callosobruchus maculatus)

1999 ◽  
Vol 92 (3) ◽  
pp. 249-255 ◽  
Author(s):  
Antonia Elenir A. Oliveira ◽  
Mauricio P. Sales ◽  
Olga Lima T. Machado ◽  
Katia Valevski S. Fernandes ◽  
Jose Xavier-Filho
2016 ◽  
Vol 64 (18) ◽  
pp. 3514-3522 ◽  
Author(s):  
Nadia C. M. Silva ◽  
Leonardo F. R. De Sá ◽  
Eduardo A. G. Oliveira ◽  
Monique N. Costa ◽  
Andre T. S. Ferreira ◽  
...  

2014 ◽  
Vol 60 ◽  
pp. 50-57 ◽  
Author(s):  
Leonardo Figueira Reis de Sá ◽  
Tierry Torres Wermelinger ◽  
Elane da Silva Ribeiro ◽  
Geraldo de Amaral Gravina ◽  
Kátia Valevski Sales Fernandes ◽  
...  

2004 ◽  
Vol 76 (1) ◽  
pp. 57-65 ◽  
Author(s):  
Luciana B. Silva ◽  
Maurício P. Sales ◽  
Antônia E. A. Oliveira ◽  
Olga L. T. Machado ◽  
Kátia V. S. Fernandes ◽  
...  

We have confirmed here that the seeds of the common bean (Phaseolus vulgaris, L.) do not support development of the bruchid Callosobruchus maculatus (F.), a pest of cowpea [Vigna unguiculata (L.) Walp] seeds. Analysis of the testa (seed coat) of the bean suggested that neither thickness nor the levels of compounds such as tannic acid, tannins, or HCN are important for the resistance. On the other hand, we have found that phaseolin (vicilin-like 7S storage globulin), detected in the testa by Western blotting and N-terminal amino acid sequencing, is detrimental to the development of C. maculatus. As for the case of other previously studied legume seeds (Canavalia ensiformis and Phaseolus lunatus) we suggest that the presence of vicilin-like proteins in the testa of P. vulgaris may have had a significant role in the evolutionary adaptation of bruchids to the seeds of leguminous plants.


2017 ◽  
Vol 91 (1) ◽  
pp. 313-326 ◽  
Author(s):  
Leonardo Figueira Reis de Sá ◽  
Kayan Eudorico Ventury ◽  
Olga Lima Tavares Machado ◽  
Kátia Valevski Sales Fernandes ◽  
José Xavier-Filho ◽  
...  

2000 ◽  
Vol 33 (2) ◽  
pp. 191-198 ◽  
Author(s):  
R.A. Moraes ◽  
M.P. Sales ◽  
M.S.P. Pinto ◽  
L.B. Silva ◽  
A.E.A. Oliveira ◽  
...  

2018 ◽  
Vol 14 ◽  
pp. 2156-2162 ◽  
Author(s):  
Maroš Bella ◽  
Sergej Šesták ◽  
Ján Moncoľ ◽  
Miroslav Koóš ◽  
Monika Poláková

A synthetic approach to 1,4-imino-L-lyxitols with various modifications at the C-5 position is reported. These imino-L-lyxitol cores were used for the preparation of a series of N-(4-halobenzyl)polyhydroxypyrrolidines. An impact of the C-5 modification on the inhibition and selectivity against GH38 α-mannosidases from Drosophila melanogaster, the Golgi (GMIIb) and lysosomal (LManII) mannosidases and commercial jack bean α-mannosidase from Canavalia ensiformis was evaluated. The modification at C-5 affected their inhibitory activity against the target GMIIb enzyme. In contrast, no inhibition effect of the pyrrolidines against LManII was observed. The modification of the imino-L-lyxitol core is therefore a suitable motif for the design of inhibitors with desired selectivity against the target GMIIb enzyme.


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