title: Aminopeptidase N isoforms from the midgut of Bombyx mori and Plutella xylostella -- their classification and the factors that determine their binding specificity to Bacillus thuringiensis Cry1A toxin.
abstract: Novel aminopeptidase N (APN) isoform cDNAs, BmAPN3 and PxAPN3, from the midguts of Bombyx mori and Plutella xylostella, respectively, were cloned, and a total of eight APN isoforms cloned from B. mori and P. xylostella were classified into four classes. Bacillus thuringiensis Cry1Aa and Cry1Ab toxins were found to bind to specific APN isoforms from the midguts of B. mori and P. xylostella, and binding occurred with fragments that corresponded to the BmAPN1 Cry1Aa toxin-binding region of each APN isoform. The results suggest that APN isoforms have a common toxin-binding region, and that the apparent specificity of Cry1Aa toxin binding to each intact APN isoform seen in SDS-PAGE is determined by factors such as expression level in conjunction with differences in binding affinity.
authors.affiliation: Graduate School of Bio-Applications and Systems Engineering, Tokyo University of Agriculture and Technology, Koganei, Tokyo, Japan.
authors.forename: Kazuko
authors.initials: K
authors.lastname: Nakanishi
authors.forename: Katsuro
authors.initials: K
authors.lastname: Yaoi
authors.forename: Yasushi
authors.initials: Y
authors.lastname: Nagino
authors.forename: Hirotaka
authors.initials: H
authors.lastname: Hara
authors.forename: Madoka
authors.initials: M
authors.lastname: Kitami
authors.forename: Shogo
authors.initials: S
authors.lastname: Atsumi
authors.forename: Nami
authors.initials: N
authors.lastname: Miura
authors.forename: Ryoichi
authors.initials: R
authors.lastname: Sato
mesh_terms: D000626:Aminopeptidases / Q000145:classification* / Q000235:genetics* / Q000378:metabolism; D000818:Animals; D000083722:Bacillus thuringiensis Toxins; D001426:Bacterial Proteins / Q000378:metabolism*; D001427:Bacterial Toxins / Q000378:metabolism; D001665:Binding Sites / Q000235:genetics; D012831:Bombyx / Q000201:enzymology; D003001:Cloning, Molecular; D018076:DNA, Complementary / Q000235:genetics; D004064:Digestive System / Q000201:enzymology; D004591:Electrophoresis, Polyacrylamide Gel; D004731:Endotoxins / Q000378:metabolism*; D006460:Hemolysin Proteins; D015151:Immunoblotting; D019476:Insect Proteins / Q000145:classification* / Q000235:genetics* / Q000378:metabolism; D007527:Isoenzymes / Q000145:classification / Q000235:genetics / Q000378:metabolism; D007915:Lepidoptera / Q000201:enzymology*; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D010802:Phylogeny; D011485:Protein Binding / Q000502:physiology; D011993:Recombinant Fusion Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D017386:Sequence Homology, Amino Acid; D013379:Substrate Specificity / Q000502:physiology
chemical_list: D000083722:Bacillus thuringiensis Toxins; D001426:Bacterial Proteins; D001427:Bacterial Toxins; D018076:DNA, Complementary; D004731:Endotoxins; D006460:Hemolysin Proteins; D019476:Insect Proteins; D007527:Isoenzymes; D010446:Peptide Fragments; D011993:Recombinant Fusion Proteins; C030956:insecticidal crystal protein, Bacillus Thuringiensis; D000626:Aminopeptidases