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J Biol Chem, Vol. 275, Issue 19, 14423-14431, May 12, 2000
From the Specificity for target insects of Bacillus
thuringiensis insecticidal Cry toxins is largely determined by
toxin affinity for insect midgut receptors. The mode of binding for one
such toxin-receptor complex was investigated by extensive toxin
mutagenesis, followed by real-time receptor binding analysis using an
optical biosensor (BIAcore). Wild-type Cry1Ac, a three-domain,
lepidopteran-specific toxin, bound purified gypsy moth (Lymantria
dispar) aminopeptidase N (APN) biphasically. Site 1 displayed
fast association and dissociation kinetics, while site 2 possessed
slower kinetics, yet tighter affinity. We empirically determined that
two Cry1Ac surface regions are involved in in vivo toxicity
and APN binding. Mutations within domain III affected binding rates to
APN site 1, whereas mutations in domain II affected binding rates to
APN site 2. Furthermore, domain III contact is completely inhibited in
the presence of N-acetylgalactosamine, indicating loss of
domain III binding eliminates all APN binding. Based upon these
observations, the following model is proposed. A cavity in lectin-like
domain III initiates docking through recognition of an
N-acetylgalactosamine moiety on L. dispar APN.
Following primary docking, a higher affinity domain II binding
mechanism occurs, which is critical for insecticidal activity.
Bivalent Sequential Binding Model of a Bacillus
thuringiensis Toxin to Gypsy Moth Aminopeptidase N
Receptor*
,§
Department of Molecular Genetics and
§ Department of Biochemistry, Ohio State University,
Columbus, Ohio 43210 and the ¶ United States Department of
Agriculture Forest Service, Northeastern Research Station,
Delaware, Ohio 43015
*
This work was supported by National Institutes of Health
Grant R01 AI29092.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed: Ohio State
University, Biological Sciences Bldg., 484 W. 12th Ave., Columbus, OH
43210. Tel.: 614-292-8829; Fax: 614-292-6773; E-mail:
dean.10@osu.edu.
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