Proteomic analysis of novel Cry1Ac binding proteins in Helicoverpa armigera (Hübner).
Aminopeptidase N (APN) and cadherin-like proteins have been previously identified as Cry1Ac-binding proteins in Helicoverpa armigera (Hübner). In this study, a proteomic approach was used to identify novel Cry1Ac-binding proteins in H. armigera. Brush border membrane vesicles (BBMV) of H. armigera were extracted and separated by two-dimensional gel electrophoresis (2-DE). Cry1Ac-binding proteins were detected using antisera against Cry1Ac. Peptide mass fingerprinting (PMF) was used to identify Cry1Ac-binding proteins. In total, four proteins were identified as candidate Cry1Ac-binding proteins in H. armigera: vacuolar ATP synthase (V-ATPase) subunit B, actin, heat shock cognate protein (HSCP), and a novel protein.
Institute of Plant Protection, Chinese Academy of Agricultural Sciences, Beijing, P.R. China.
Li-Zhen
LZ
Chen
Ge-Mei
GM
Liang
Jie
J
Zhang
Kong-Ming
KM
Wu
Yu-Yuan
YY
Guo
Brian G
BG
Rector
D000818:Animals; D000083722:Bacillus thuringiensis Toxins; D001426:Bacterial Proteins / Q000378:metabolism*; D022162:Cytoplasmic Vesicles / Q000737:chemistry / Q000378:metabolism; D004731:Endotoxins / Q000378:metabolism*; D041981:Gastrointestinal Tract / Q000737:chemistry / Q000648:ultrastructure; D006460:Hemolysin Proteins / Q000378:metabolism*; D019476:Insect Proteins / Q000378:metabolism*; D008871:Microvilli / Q000737:chemistry / Q000378:metabolism; D009036:Moths; D011485:Protein Binding; D040901:Proteomics
D000083722:Bacillus thuringiensis Toxins; D001426:Bacterial Proteins; D004731:Endotoxins; D006460:Hemolysin Proteins; D019476:Insect Proteins; C030956:insecticidal crystal protein, Bacillus Thuringiensis