TY - JOUR
T1 - GalNAc pretreatment inhibits trapping of Bacillus thuringiensis Cry1Ac on the peritrophic membrane of Bombyx mori
AU - Hayakawa, Tohru
AU - Shitomi, Yasuyuki
AU - Miyamoto, Kazuhisa
AU - Hori, Hidetaka
N1 - Funding Information:
This work was supported, in part, by research grants from Ministry of Education, Culture, Sports, Science and Technology of Japan, 12558069 and 13306006 (HH) and 16780035 (TH). Grant for Promotion of Niigata University Research Projects (TH) also partially contributed to this research.
PY - 2004/10/22
Y1 - 2004/10/22
N2 - Bombyx mori (Shunrei×Shogetsu) is sensitive to Cry1Aa and resistant to Cry1Ac, both insecticidal proteins of Bacillus thuringiensis. Cry1Aa passed through the peritrophic membrane (PM) much faster (0.37 μg/mm2 PM/h) than Cry1Ac (0.05 μg/mm2 PM/h) during the initial observation period. Both Cry1Aa and Cry1Ac bound to the PM but only the binding of Cry1Ac was specifically inhibited by N-acetylgalactosamine (GalNAc). When Cry1Ac was pretreated with GalNAc, Cry1Ac permeated the PM much faster. These results suggested that Cry1Ac bound a PM protein via GalNAc on a sugar side chain. The role of the PM on Cry1Ac resistance of B. mori was briefly discussed.
AB - Bombyx mori (Shunrei×Shogetsu) is sensitive to Cry1Aa and resistant to Cry1Ac, both insecticidal proteins of Bacillus thuringiensis. Cry1Aa passed through the peritrophic membrane (PM) much faster (0.37 μg/mm2 PM/h) than Cry1Ac (0.05 μg/mm2 PM/h) during the initial observation period. Both Cry1Aa and Cry1Ac bound to the PM but only the binding of Cry1Ac was specifically inhibited by N-acetylgalactosamine (GalNAc). When Cry1Ac was pretreated with GalNAc, Cry1Ac permeated the PM much faster. These results suggested that Cry1Ac bound a PM protein via GalNAc on a sugar side chain. The role of the PM on Cry1Ac resistance of B. mori was briefly discussed.
KW - Bacillus thuringiensis
KW - Bombyx mori
KW - N-acetylgalactosamine
KW - Peritrophic membrane protein
KW - Permeability of peritrophic membrane
KW - δ-Endotoxin
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U2 - 10.1016/j.febslet.2004.09.029
DO - 10.1016/j.febslet.2004.09.029
M3 - Article
C2 - 15498557
AN - SCOPUS:6344290041
SN - 0014-5793
VL - 576
SP - 331
EP - 335
JO - FEBS Letters
JF - FEBS Letters
IS - 3
ER -