Functional redundancy in the toxic pathway of Bt protein Cry1Ab, but not Cry1Fa, against the Asian corn borer
Proceedings of the National Academy of Sciences,
Год журнала:
2025,
Номер
122(16)
Опубликована: Апрель 17, 2025
Crops
genetically
engineered
to
produce
insecticidal
proteins
from
the
bacterium
Bacillus
thuringiensis
(Bt)
have
been
used
extensively
control
some
major
crop
pests,
but
their
benefits
decrease
when
pests
evolve
resistance.
Better
understanding
of
genetic
basis
resistance
is
needed
effectively
monitor,
manage,
and
counter
pest
Bt
crops.
Resistance
in
at
least
11
species
Lepidoptera,
including
many
important
associated
with
naturally
occurring
mutations
that
disrupt
one
or
more
three
larval
midgut
proteins:
cadherin
ATP-binding
cassette
ABCC2
ABCC3.
Here,
we
determined
how
CRISPR/Cas9-mediated
disrupting
cadherin,
ABCC2,
ABCC3
singly
pairs
affect
Cry1Ab
Cry1Fa
Asian
corn
borer
(
Ostrinia
furnacalis
),
which
most
damaging
Asia
closely
related
European
nubilalis
a
Europe
North
America.
The
results
bioassays
six
knockout
strains
parent
susceptible
strain
support
model
can
kill
larvae
via
path
requiring
another
ABCC3,
whereas
uses
only
first
path.
model’s
predictions
are
generally
supported
by
linkage
analyses
responses
Sf9
cells
Xenopus
oocytes
modified
pairs.
functional
redundancy
identified
here
for
could
sustain
its
efficacy
against
O.
may
exemplify
widespread
natural
strategy
delaying
Язык: Английский
Structural and functional roles of domain III in Vip3Aa and Vip3Ca: implications for membrane perforation and insecticidal efficacy
Pest Management Science,
Год журнала:
2025,
Номер
unknown
Опубликована: Май 24, 2025
Abstract
BACKGROUND
The
widespread
use
of
Bacillus
thuringiensis
Cry
proteins
in
pest
control
has
led
to
resistance
some
lepidopteran
pests.
Vip3
proteins,
lacking
sequence
homology
with
toxins,
offer
a
promising
alternative
due
distinct
insecticidal
mechanisms.
This
study
investigates
how
modulating
interactions
between
domain
III
and
the
N‐terminal
region
(P14–G22)
influences
their
activation
efficiency
activity.
RESULTS
Nine
residues
Vip3Aa
protein
were
selected
for
alanine
mutation.
After
testing
membrane
perforation
activity
mutants,
results
showed
that
mutant
Vip3Aa‐V383A
exhibited
increased
compared
protein.
Structural
analysis
found
replacing
residue
V383
can
reduce
hydrogen
bonding
Y19.
disulfide
bond
Vip3Aa‐N21C‐T525C
was
seriously
affected.
Based
on
this,
two
Vip3Ca
formed
bonds
Y19
mutated
respectively.
Vip3Ca‐K383A
also
Furthermore,
enhanced
against
four
tested
In
addition,
K385,
K526,
V529
critical
receptor
binding,
mutation
diminishing
binding
affinity
toxicity.
CONCLUSIONS
Targeted
disruption
enhances
efficacy
Vip3Ca,
offering
novel
engineering
strategy
optimizing
biopesticides.
©
2025
Society
Chemical
Industry.
Язык: Английский