Bombyx mori Midgut Membrane Protein P252, Which Binds to Bacillus thuringiensis Cry1A, Is a Chlorophyllide-Binding Protein, and the Resulting Complex Has Antimicrobial Activity

The epithelial cell membrane 252-kDa protein (P252) isolated in our laboratory from Bombyx mori midgut was shown to bind strongly with Cry1Aa, Cry1Ab, and Cry1Ac toxins of Bacillus thuringiensis (15). In the current paper, P252 was shown to bind with chlorophyllide (Chlide) to form red fluorescent p...

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Veröffentlicht in:	Applied and Environmental Microbiology 2008-03, Vol.74 (5), p.1324-1331
Hauptverfasser:	Pandian, Ganesh N, Ishikawa, Toshiki, Togashi, Makoto, Shitomi, Yasuyuki, Haginoya, Kohsuke, Yamamoto, Shuhei, Nishiumi, Tadayuki, Hori, Hidetaka
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Animals Anti-Infective Agents - metabolism Bacillus thuringiensis Bacillus thuringiensis - chemistry Bacillus thuringiensis Toxins Bacteria Bacterial proteins Bacterial Proteins - metabolism Bacterial Toxins - metabolism Binding sites Bombyx - chemistry Bombyx mori Cells Chemical synthesis Chlorophyllides - metabolism Chromatography, High Pressure Liquid Circular Dichroism Electrophoresis, Polyacrylamide Gel Endotoxins - metabolism Escherichia coli Gastric Mucosa - chemistry Hemolysin Proteins - metabolism Invertebrate Microbiology Luminescent Proteins - metabolism Membrane Proteins - genetics Membrane Proteins - metabolism Microbiology Molecular Sequence Data Multiprotein Complexes - metabolism Red Fluorescent Protein Saccharomyces cerevisiae Serratia marcescens Temperature
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