Cell,
Journal Year:
2024,
Volume and Issue:
187(9), P. 2095 - 2116
Published: April 1, 2024
Plant
diseases
cause
famines,
drive
human
migration,
and
present
challenges
to
agricultural
sustainability
as
pathogen
ranges
shift
under
climate
change.
breeders
discovered
Mendelian
genetic
loci
conferring
disease
resistance
specific
isolates
over
100
years
ago.
Subsequent
breeding
for
underpins
modern
agriculture
and,
along
with
the
emergence
focus
on
model
plants
genetics
genomics
research,
has
provided
rich
resources
molecular
biological
exploration
last
50
years.
These
studies
led
identification
of
extracellular
intracellular
receptors
that
convert
recognition
microbe-encoded
patterns
or
pathogen-delivered
virulence
effectors
into
defense
activation.
receptor
systems,
downstream
responses,
define
plant
immune
systems
have
evolved
since
migration
land
∼500
million
Our
current
understanding
provides
platform
development
rational
enhancement
control
many
continue
plague
crop
production.
The Plant Cell,
Journal Year:
2022,
Volume and Issue:
34(5), P. 1447 - 1478
Published: Feb. 10, 2022
Understanding
the
plant
immune
system
is
crucial
for
using
genetics
to
protect
crops
from
diseases.
Plants
resist
pathogens
via
a
two-tiered
innate
detection-and-response
system.
The
first
Resistance
(R)
gene
was
cloned
in
1992
.
Since
then,
many
cell-surface
pattern
recognition
receptors
(PRRs)
have
been
identified,
and
R
genes
that
encode
intracellular
nucleotide-binding
leucine-rich
repeat
(NLRs)
cloned.
Here,
we
provide
list
of
characterized
PRRs
NLRs.
In
addition
receptors,
components
signaling
networks
were
discovered
over
last
30
years.
We
review
pathways,
physiological
responses,
molecular
regulation
both
PRR-
NLR-mediated
immunity.
Recent
studies
reinforced
importance
interactions
between
two
systems.
an
overview
immunity,
highlighting
challenges
perspectives
future
research.
Science,
Journal Year:
2020,
Volume and Issue:
370(6521)
Published: Dec. 4, 2020
Tetrameric
immune
receptors
Nucleotide-binding/leucine-rich
repeat
(NLR)
detect
pathogen
effectors
and
trigger
a
plant's
response.
Two
groups
have
now
defined
the
structures
of
two
NLRs
that
carry
Toll-like
interleukin-1
receptor
(TIR)
domains
(TIR-NLRs)
(see
Perspective
by
Tian
Li).
Ma
et
al.
studied
Arabidopsis
thaliana
TIR-NLR
RPP1
(recognition
Peronospora
parasitica
1)
its
response
to
from
an
oomycete
pathogen.
Martin
Nicotiana
benthamiana
ROQ1
XopQ
Xanthomonas
effector.
Both
found
these
TIR-NLRs
formed
tetramers
that,
when
activated
binding
effector,
exposed
active
site
nicotinamide
adenine
dinucleoside
(NAD)
hydrolase.
Thus,
recognition
effector
initiates
NAD
hydrolysis
begins
Science
,
this
issue
p.
eabe3069
eabd9993
;
see
also
1163
Nature,
Journal Year:
2022,
Volume and Issue:
610(7932), P. 532 - 539
Published: Sept. 26, 2022
Abstract
Plant
intracellular
nucleotide-binding
leucine-rich
repeat
receptors
(NLRs)
detect
pathogen
effectors
to
trigger
immune
responses
1
.
Indirect
recognition
of
a
effector
by
the
dicotyledonous
Arabidopsis
thaliana
coiled-coil
domain
containing
NLR
(CNL)
ZAR1
induces
formation
large
hetero-oligomeric
protein
complex,
termed
resistosome,
which
functions
as
calcium
channel
required
for
ZAR1-mediated
immunity
2–4
Whether
resistosome
and
activities
are
conserved
among
plant
CNLs
remains
unknown.
Here
we
report
cryo-electron
microscopy
structure
wheat
CNL
Sr35
5
in
complex
with
AvrSr35
6
stem
rust
pathogen.
Direct
binding
repeats
results
pentameric
Sr35–AvrSr35
term
resistosome.
Wheat
resistosomes
bear
striking
structural
similarities,
including
an
arginine
cluster
not
previously
recognized
conserved,
co-occurs
forms
intramolecular
interactions
'EDVID'
motif
domain.
Electrophysiological
measurements
show
that
exhibits
non-selective
cation
activity.
These
insights
allowed
us
generate
new
variants
closely
related
barley
orphan
NLRs
recognize
AvrSr35.
Our
data
support
evolutionary
conservation
plants
demonstrate
proof
principle
structure-based
engineering
crop
improvement.
Science,
Journal Year:
2022,
Volume and Issue:
377(6607)
Published: Aug. 11, 2022
Many
organisms
have
evolved
specialized
immune
pattern-recognition
receptors,
including
nucleotide-binding
oligomerization
domain-like
receptors
(NLRs)
of
the
STAND
superfamily
that
are
ubiquitous
in
plants,
animals,
and
fungi.
Although
roles
NLRs
eukaryotic
immunity
well
established,
it
is
unknown
whether
prokaryotes
use
similar
defense
mechanisms.
Here,
we
show
antiviral
(Avs)
homologs
bacteria
archaea
detect
hallmark
viral
proteins,
triggering
Avs
tetramerization
activation
diverse
N-terminal
effector
domains,
DNA
endonucleases,
to
abrogate
infection.
Cryo-electron
microscopy
reveals
sensor
domains
recognize
conserved
folds,
active-site
residues,
enzyme
ligands,
allowing
a
single
receptor
wide
variety
viruses.
These
findings
extend
paradigm
pattern
recognition
pathogen-specific
proteins
across
all
three
life.