Issue Date

10-2013

Abstract

Brush border membrane vesicles (BBMVs) were prepared from 4th instar larvae of Asian corn borer Ostrinia furnacalis Guenee. SDS-PAGE analysis showed major protein bands with molecular weight in the range of 80 kDa to 250 kDa. Ligand blot analysis showed that biotinylated Cry1Ab δ-endotoxin strongly binds to a ~250 kDa receptor protein from 0. furnacalis BBMV. Another receptor protein of ~110 kDa weakly binds to Cry1Ab δ-endotoxin. At least two isoforms of the ~250 kDa receptor protein have a pH range of 5.5 to 6.5 as determined by 2D-electrophoresis. Post-translational modification of 0. furnacalis BBMV proteins was also detected as revealed by the presence of two glycosylated proteins with molecular weights of >250 kDa and 70 kDa, respectively. Alanine scanning mutations were introduced in domain III ß-sheet 13 of Cry1Ab δ-endotoxin. Results of bioassays showed a 5 to 7 fold reduction in insecticidal activity in Serine556Alanine, Serine557Alanine and Serine556Alanine-Serine557Alanine mutants of Cry1Ab protein. The decrease in insecticidal activity suggests that Serine556 and Serine557 are both important residues in the toxicity of Cry1Ab δ-endotoxin to 0. furnacalis.

Source or Periodical Title

The Philippine Entomologist

ISSN

0048-3753

Volume

27

Issue

2

Page

120-133

Document Type

Article

Frequency

semi-annually

Physical Description

illustrations ; tables

Language

English

En – AGROVOC descriptors

OSTRINIA FURNACALIS; BACILLUS THURINGIENSIS; ALANINE; ENDOTOXINS; PESTS OF PLANTS; BACTERIAL PESTICIDES; RECEPTORS

Share

COinS
 
 

To view the content in your browser, please download Adobe Reader or, alternately,
you may Download the file to your hard drive.

NOTE: The latest versions of Adobe Reader do not support viewing PDF files within Firefox on Mac OS and if you are using a modern (Intel) Mac, there is no official plugin for viewing PDF files within the browser window.