Review
Plant pattern-recognition receptors
Cyril Zipfel
The Sainsbury Laboratory, Norwich Research Park, Norwich NR4 7UH, UK
Plants are constantly exposed to would-be pathogens in
their immediate environment. Yet, despite relying on
innate immunity only, plants are resistant to most
microbes. They employ pattern-recognition receptors
(PRRs) for sensitive and rapid detection of the potential
danger caused by microbes and pests. Plant PRRs are
either surface-localized receptor kinases (RKs) or recep-
tor-like proteins (RLPs) containing various ligand-bind-
ing ectodomains that perceive pathogen-associated
molecular patterns (PAMPs) or damage-associated mo-
lecular patterns (DAMPs). In this review, I summarize our
current knowledge of plant PRRs and their ligands,
illustrating the multiple molecular strategies employed
by plant PRRs to activate innate immune signaling to
survive.
A two-tiered pathogen-detection system
Plants are sessile organisms that rely entirely on innate
immune responses for defense against potential pathogen-
ic microbes or pests. They lack specialized immune cells or
organs and each cell has the potential capacity to trigger
immune responses autonomously. Innate immune percep-
tion triggers both local and systemic responses, allowing a
plant to fight off pathogens both in a rapid and localized
manner and on an extended scale of time and space. For
these purposes, plants employ a two-tier innate immune
system that involves plasma membrane-localized and in-
tracellular immune receptors [1,2].
Cell surface-localized immune receptors function as
PRRs that perceive PAMPs or DAMPs of non-self and
self origin, respectively. Currently known plant PRRs are
either RKs, which have a ligand-binding ectodomain, a
single-pass transmembrane domain, and an intracellular
kinase domain, or RLPs, which share the same overall
structure but lack an intracellular kinase domain. Because
RLPs do not possess any obvious signaling domains in their
short intracellular region, they most likely always function
in conjunction with one or several RKs to transduce ligand
binding into intracellular signaling. Importantly, PRR-
triggered immunity (PTI) has the potential to fend off
multiple microbes, pathogenic or not, due to the conserved
nature of PAMPs (e.g., bacterial flagellin, fungal chitin)
across species, genera, family, or class. Thus, PRRs can
provide resistance to most non-adapted pathogens, as well
as contribute to basal immunity during infection.
Corresponding author: Zipfel, C. (cyril.zipfel@tsl.ac.uk).
Keywords: innate immunity; plant; receptor kinases; receptor-like proteins; PAMPs;
DAMPs.
1471-4906/
2014 Elsevier Ltd. All rights reserved. http://dx.doi.org/10.1016/j.it.2014.05.004
In addition to PTI, plants rely on effector-triggered
immunity (ETI). ETI employs intracellular immune recep-
tors, which are most are nucleotide-binding site leucine-
rich repeat (NBS-LRR) proteins, to perceive secreted viru-
lence effectors directly or indirectly. These effectors (e.g.,
AvrPto, AvrPtoB) have been evolved initially by adapted
pathogens to reprogram the hosts physiology toward in-
fectious compatibility, but their perception by NBS-LRR
proteins betrays the pathogens in what is the result of a
constant arms race between plants and their pathogens.
Notably, NBS-LRRs are structurally related to mammali-
an NOD-like receptors (NLRs).
In mammals, both surface-localized [e.g., Toll-like
receptors (TLRs)] and intracellular (e.g., NLRs) immune
receptors have been shown to recognize PAMPs [3]. This is
in contrast to plants, which seems to rely on plasma
membrane-localized RKs or RLPs only to perceive PAMPs
or DAMPs (Box 1). It is interesting to note that, as studied
for many years in plants, it is now also apparent that
mammalian NLRs also engage ETI [4,5].
Here I summarize our current knowledge on plant
PRRs. I illustrate the multiple molecular strategies
employed by plants to detect rapidly the multitude of
potential invaders in their immediate surroundings
strategies essential for their survival. For details on the
molecular immune signaling mechanisms triggered after
PAMP perception in plants, readers are directed to recent
reviews on this topic [6,7].
Perception of bacteria
Multiple recognition of flagellin and elongation factor Tu
The perception of bacterial flagellin by the LRR-RK FLS2
was the first plant PAMP/PRR pair to be characterized [8
10]. FLS2 recognizes flagellin via the direct binding of an
immunogenic epitope defined by a conserved stretch of 22
amino acids, referred to as flg22 (Figure 1), located close to
the N terminus of flagellin [1113]. FLS2 was initially
identified in the model plant Arabidopsis thaliana [8].
Flg22 seems to be recognized by most higher plants [14]
and functional orthologs of FLS2 have already been iden-
tified in a wild relative of tobacco (Nicotiana benthamiana),
rice (Oryza sativa), tomato (Solanum lycopersicum), and
grapevine (Vitis vinifera) [1518]. FLS2 from different
species have revealed interesting differences in flg22 rec-
ognition specificities that may reflect the evolutionary
histories of these species and their adaptation to their
respective microbiota.
Flg22 binding to FLS2 leads to the instantaneous re-
cruitment of the LRR-RK BAK1 (Figure 1), which acts as a
coreceptor for flg22 and is required for the full activation of
FLS2 and flg22-triggered immune signaling [9,13,19,20].
Trends in Immunology, July 2014, Vol. 35, No. 7 345
 Review Trends in Immunology July 2014, Vol. 35, No. 7

Box 1. Similarities and differences between plant and
animal PRRs
 Plants seems to rely only on plasma membrane-localized PRRs to
perceive PAMPs or DAMPs, in contrast to mammals, which
employ both surface-localized and intracellular immune receptors
to recognize PAMPs.
 Whereas animals have only a limited set of PRRs, plant genomes
encode a large number of RKs and RLPs that are potential PRRs.
 Plants have uniquely combined ligand-recognition domains (e.g.,
LRR, LysM) directly with an intracellular kinase domain in the case
of RK-type PRRs.
 Both plant and animal PRRs have evolved to perceive similar
PAMP molecules (e.g., bacterial flagellin). However, both the
epitopes recognized and the modular PRRs involved are distinct,
indicative of convergent evolution.
Notably, it is becoming increasingly apparent that BAK1
and related SERK proteins associate with several addi-
tional LRR-RKs or LRR-RLPs and regulate their function
[21], suggesting that they also act as coreceptors for other
ligands.
Plants seem able to recognize multiple epitopes within
flagellin [18,22,23]. A comparative genomic study of field-
isolated Pseudomonas syringae strains revealed the 28-
amino acid epitope flgII-28 to be under strong selective
pressure, potentially to evade plant immune recognition
[23]. flgII-28 induces immune responses in tomato, as well
as in several Solanaceae species, but does not seem to be
perceived by FLS2 (Figure 1), despite potential genetic
interactions between flg22 and flgII-28 recognition in to-
mato [22]. Notably, mammals can also recognize different
flagellin-derived epitopes, employing both extracellular
and intracellular PRRs such as TLR5 and NAIP5/6 [24]
(Box 1). However, plants do not seem able to perceive
flagellin intracellularly [25], suggesting that the PRR for
flgII-28 is a RK or RLP.
The perception of bacterial elongation factor Tu (EF-Tu)
by the Arabidopsis LRR-RK EFR defines another well-
studied plant PAMP/PRR pair (Figure 1). EFR directly
recognizes the conserved N-acetylated epitope elf18 de-
fined by the first 18 amino acids of EF-Tu [26,27]. Inter-
estingly, the ability to perceive elf18 seems restricted to the
plant family Brassicaceae [14]. Transgenic expression of
EFR in another plant family (Solanaceae) confirmed that
EFR confers elf18 perception and revealed that interfamily
transfer of plant PRRs can be used to engineer disease
resistance in crops [28].
Similarly to what has been recently discovered for
flagellin, plants can perceive EF-Tu via an epitope other
than elf18 (Figure 1). Indeed, treatment with the 50-amino
acid epitope EFa50 derived from the central region of EF-
Tu induces immune responses in rice via an as-yet-un-
known PRR [29].
Complex recognition of peptidoglycans (PGNs)
PGNs are a major constituent of bacterial cell walls and
represent a classical PAMP recognized by insects such as
Drosophila melanogaster [30]. Plants can also perceive
PGNs [31,32] (Figure 1). In Arabidopsis, this perception
involves two RLPs with lysine motif (LysM)-containing
ectodomains, AtLYM1 and AtLYM3, which specifically
bind PGNs [33]. PGN perception in rice involves the ortho-
logous LysM-RLPs OsLYP4 and OsLYP6 [34]. PGN-in-
duced responses in Arabidopsis also require the LysM-
RK CERK1, which does not bind PGN itself [33]. Also,
the tomato CERK1 orthologs Bti9 and SlLyk13 are re-
quired for full antibacterial immunity [35]. Thus, it is likely

Flagellin EF-Tu PGN PGN ? ? ?

g22 gII-28 elf18 EFa50

FLS2 ? EFR ? LYM1/3 LYP4/6 XA21 XA3/26 ReMAX

BAK1 BAK1 CERK1 SERK2 SERK2

ts

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Ric

Ric

Ric

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ras idop
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Key: LRR domain

LysM domain
Kinase domain

TRENDS in Immunology

Figure 1. Recognition of bacteria by plant pattern-recognition receptors (PRRs). The conserved leucine-rich repeat receptor kinase (LRR-RK) FLS2 recognizes flagellin via the
flg22 epitope. The flagellin-derived epitope flgII-28 is recognized in tomato and other Solanaceae via an as-yet-unknown PRR. The LRR-RK EFR perceives elongation factor
Tu (EF-Tu) in Brassicaceae, whereas the EF-Tu-derived epitope EFa50 is recognized in rice by an as-yet-unknown PRR. Both FLS2 and EFR interact with the coreceptor LRR-
RK BAK1 immediately upon flg22 or elf18 binding, respectively. Peptidoglycans (PGNs) bind to the Arabidopsis lysine motif receptor-like proteins (LysM-RLPs) LYM1 and
LYM3, which may form a complex with the LysM-RK CERK1 on PGN recognition. In rice, PGNs bind to the LysM-RLPs LYP4 and LYP6. The rice LRR-RKs XA21 and XA3/26
interact with the LRR-RK OsCERK2 and confer resistance to Xanthomonas oryzae pv. oryzae via the recognition of as-yet-unknown pathogen-associated molecular patterns
(PAMPs). The Arabidopsis LRR-RLP ReMAX perceives an enigmatic PAMP from xanthomonads that also induces immune responses in other Brassicaceae. Block arrows
indicate direct binding; dashed arrows indicate lack of direct binding evidence, candidate PRR, or ligand.

346
Review Trends in Immunology July 2014, Vol. 35, No. 7

that PGN perception in plants employs a multimeric re-
ceptor system comprising PGN-binding LysM-RLPs and
signaling-transducing LysM-RKs, such as CERK1, in a
manner similar to chitin perception in rice (see below).
Orphan PRRs and bacterial PAMPs
Several potential plant PRRs recognizing bacteria have
been identified, but their specific agonists remain un-
known (Figure 1). These include the rice LRR-RKs XA21
and XA3/XA26, which mediate resistance to the bacterium
Xanthomonas oryzae pv. oryzae [3638], and the Arabidop-
sis LRR-RLP ReMAX/RLP1, which confers recognition of
the enigmatic bacterial PAMP eMax partially purified
from Xanthomonas axonopodis pv. citri [39]. From the
microbes perspective, several bacterial PAMPs, such as
lipopolysaccharides (LPSs) (reviewed in [32]), cold-shock
protein (CSP22) [40], and DNA [41], induce immune
responses in plants, but their corresponding PRRs are
unknown.
Perception of fungi and oomycetes
Chitin perception by LysM-RKs and LysM-RLPs:
variations on a common theme
Chitin is a major constituent of fungal cell walls. Chitin is a
potential agonist for TLR2 in mammals [42,43] and has
been studied for decades in plants as a classical PAMP [44].
Interestingly, different plants have evolved distinct mech-
anisms that employ common components for chitin percep-
tion (Figure 2). The first chitin-binding PRR was identified
in rice as the LysM-RLP CEBiP [45]. Notably, CEBiP
homodimerizes upon chitin binding and forms a hetero-
oligomeric complex with OsCERK1, the rice ortholog of
AtCERK1, forming a sandwich-type receptor system for
chitin [46,47]. The CEBiP-related LysM-RLPs OsLYP4
and OsLYP6 also bind chitin and participate in chitin
responsiveness [34].
The chitin perception mechanism of rice is distinct to
that in Arabidopsis, where AtCERK1 binds directly to
octamers of chitin, which in turn induces AtCERK1 homo-
dimerization and consequent immune signaling [4851].
The related Arabididopsis LysM-RK LYK4 can also bind
chitin and is involved in chitin responsiveness [52]. So, in
contrast to rice, Arabidopsis does not seem to employ
CEBiP-like LysM-RLPs to induce typical immune
responses (e.g., production of reactive oxygen species, im-
mune gene expression) upon chitin perception [52,53].
Making matters more complex, chitin induces the closure
of symplastic connections between neighboring cells
(known as plasmodesmata) and resistance to fungal patho-
gens in a manner that is CERK1 independent. This re-
sponse relies on the closest ortholog of CEBiP in
Arabidopsis, AtLYM2, which is also able to bind chitin
[51,5355]. Thus, Arabidopsis may also employ hetero-
oligomeric complexes between a chitin-binding LysM-
RLP (AtLYM2) and an as-yet-unknown LysM-RK poten-
tially related to CERK1 for a subset of chitin-triggered
responses [56].
Other PAMP/PRR pairs recognizing fungi
Several LRR-RLPs have been implicated in the recognition
of fungal PAMPs (Figure 2). Tomato Cf-9 was the first
LRR-RLP identified as being involved in plant immunity
and confers resistance to the filamentous fungus Clados-
porium fulvum [57]. The Cladosporium-secreted small
peptide AVR9 acts as an agonist for Cf-9, but the latter
is not likely to be the ligand-binding receptor because

Chin Chin Chin Xylanase Ave1 AVR9 PGs AVRLM1 ? ? ? ? ?

CERK1 LYM2 CEBiP EIX2 Ve1 Cf-9 RBGP1 LepR3 RLP30 RLP1.1 Pi-d2 LRK10 RLK-R1/2/3

CERK1
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Key: LRR domain

pe

LysM domain
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(pl

B-lecn domain
S-domain
Cys-rich domain
Kinase domain

TRENDS in Immunology

Figure 2. Recognition of fungi by plant pattern-recognition receptors (PRRs). Chitin binds to homodimers of the Arabidopsis lysine motif receptor kinase (LysM-RK) CERK1
to induce typical immune responses, whereas it binds to the LysM receptor-like protein (LysM-RLP) LYM2 to trigger plasmodesmata closure. In rice, chitin binds to
homodimers of the LysM-RLP CEBiP, which induces the recruitment of an oligoheteromeric complex with the leucine-rich repeat (LRR)-RK CERK1. The CEBiP-related LysM-
RLPs OsLYP4 and OsLYP6 also bind chitin and participate in chitin responsiveness. The tomato LRR-RLPs EIX2 and Ve1 recognize xylanase and Ave1, respectively, whereas
the LRR-RLP Cf-9 mediates responsiveness to AVR9, most likely indirectly. The Arabidopsis LRR-RLP RBGP1 recognizes endopolygalacturonases (PGs), whereas the
rapeseed/canola LRR-RLP LepR3 perceives AVRLM1. The Arabidopsis and wheat LRR-RLPs RLP30 and RLP1.1, the rice B-lectin-RK Pi-d2, the wheat S-domain-RK LRK10, and
the wheat cysteine (Cys)-rich RKs RLK-R1, -R2, and -R3 are involved in antifungal immunity, but their corresponding ligands remain unknown. Block arrows indicate direct
binding; dashed arrows indicate lack of direct binding evidence or candidate ligand.

347
Review
Cf-9-deficient lines still display a high-affinity binding site
for Avr9 [58].
Several other PRR/PAMP pairs have been tentatively
identified in plantfungus interactions (Figure 2). The
tomato LRR-RLP Eix2 is the PRR for fungal xylanase
[59]. Tomato Ve1 recognizes Ave1, a protein with homology
to plant natriuretic peptides that appears to be conserved
in multiple plant-pathogenic fungi and bacteria [60,61]. In
Arabidopsis, RBGP1/RLP42 perceives fungal endopolyga-
lacturonases (PGs) [62]. The rapeseed/canola (Brassica
napus) LRR-RLP LepR3 confers resistance to Lepto-
sphaeria maculans expressing AVRLM1 [63]. Despite
identification, proof of direct binding for the proposed
Ve1/Ave1, RBGP1/PGs and LepR3/AVRLM1 pairs remains
lacking.
Orphan PRRs and fungal/oomycete PAMPs
As for bacteria, several potential plant PRRs that recognize
fungi have been identified genetically but their specific
agonists remain unknown (Figure 2). These include the
Arabidopsis LRR-RLP RLP30, which is required for per-
ception of the as-yet-unidentified fungal PAMP SCFE1
partially purified from Sclerotinia sclerotorium [64], the
rice B-lectin-type RK Pi-d2 involved in resistance to Mag-
naporthe grisae [65], the wheat (Triticum aestivum) S-
domain-type RK TaLRK10 involved in resistance to leaf
rust disease [66], and the wheat LRR-RLP TaRLP1.1 and
cysteine-rich domain-type RKs TaRLK-R13 involved in
resistance to stripe rust disease [67,68]. The soluble beta-
glucan-binding protein (GBP) from soybean (Glycine max)
perceives heptaglucoside from the oomycete Phytophthora
sojae [69]. Although the soluble GBP can be defined as a
PRR based on its ligand-binding capacity, it most likely
depends on an as-yet-unknown transmembrane RK or RLP
to mediate intracellular immune signaling.
Additionally, several orphan PAMPs from fungi or
oomycetes have been identified that can trigger immune
signaling. Plants can perceive fungal ergosterol (reviewed
in [70]) or numerous oomycete PAMPs including arachi-
donic acid [71], elicitins (e.g., INF1) (reviewed in [72]), the
transglutaminase-derived immunogenic epitope Pep13
[73], cryptogein (reviewed in [74]), and cellulose-binding
elicitor lectin (CBEL) [75,76]. In all of these cases, no clear
PRRs have yet been defined.
Perception of viruses and insects
RNA silencing clearly represents a major plant immune
strategy against viruses [77] and no viral PAMP detected
by a plant PRR has been described to date. However, it was
recently found that Arabidopsis mutants of the LRR-RK
BAK1 are more susceptible to viral infection [78], suggest-
ing that PRRs, and thus an unidentified PAMP or DAMP,
may be involved in antiviral defense. Furthermore, the
Arabidopsis LRR-RKs NIK1 and NIK2 contribute to anti-
viral immunity [79,80]. Thus, future research is required to
understand mechanistically how these RKs are involved in
virus perception.
Recent findings suggest that insects could also be per-
ceived by plant surface-localized PRRs. For example, ovi-
position by Pieris brassicae induces immune responses in
Arabidopsis that depend on the lectin-domain RK (LecRK)
348
Trends in Immunology July 2014, Vol. 35, No. 7
LecRK-I.8 [81] and the LRR-RK BAK1 participates in
antiaphid immunity in Arabidopsis [82].
Overall, these findings suggest that surface-localized
LRR-RKs and/or LRR-RLPs are involved in sensing virus-
and insect-derived PAMPs or DAMPs released during
infection. Identification of these elicitors and the accompa-
nying insight into their nature and origin will be essential
to define the origin of these elicitors and the plant ligand-
binding PRRs involved. In particular, it will be important
to understand whether these distinct elicitors are recog-
nized as PAMPs or whether their perception is associated
with cell or tissue damage.
Perception of the infectious self
In addition to perceiving PAMPs that are characteristic of
non-self, plants can also sense self molecules (DAMPs) that
are available for recognition only after cell/tissue damage
or pathogen recognition. The first plant DAMP/PRR pairs
have been recently identified (Figure 3).
The Arabidopsis LRR-RKs PEPR1 and PEPR2 perceive
AtPep peptides. These peptides are derived from the pro-
peptide PROPEPs, which are encoded by a seven-member
multigenic family whose expression is induced by wound-
ing or PAMP perception [8386]. AtPep perception is part
of a PTI amplification loop and is important for the induc-
tion of systemic immunity [8792], wherein mobile signals,
the nature of which is not fully clear, spread across the
whole plant through the vasculature via the phloem. PRO-
PEPs are phylogenetically conserved in plants [93,94] and
several other plant-derived peptides have been shown to
activate immune responses in plants, via as-yet-unknown
PRRs [95].
PROPEPs OGs eATP
Peps
DORN1/
PEPR1/2 WAK1 LecRK-I.9
Arabidopsis
Key:
LRR domain
EGF domain
Lec domain
Kinase domain
TRENDS in Immunology
Figure 3. Recognition of the infectious-self by plant pattern-recognition receptors
(PRRs). The Arabidopsis leucine-rich repeat receptor kinases (LRR-RKs) PEPR1 and
PEPR2 recognize the endogenous peptides (Peps) potentially produced on
cleavage of propeptides (PROPEPs). The Arabidopsis epidermal growth factor
(EGF)-like RK WAK1 perceives cell wall-derived oligogalacturonides (OGs),
whereas the lectin-domain (Lec) RK DORN1/LecRK-I.9 binds extracellular ATP
(eATP). Block arrows indicate direct binding; dashed arrows indicate lack of direct
binding evidence or candidate ligand.
Review
Fungi produce cell wall-degrading enzymes during in-
fection and this process releases active molecules that are
normally embedded in the plant cell wall matrix. Such
molecules are oligogalacturonides (OGs), perceived by the
epidermal growth factor (EGF) motif-containing RK WAK1
in Arabidopsis [96]. Further, recently a plant receptor for
extracellular ATP (eATP) was identified as the Arabidopsis
DORN1/LecRK-I.9 [97]. eATP can be released on cell rup-
ture during pathogen attack or wounding and thus serves
as a DAMP. Although eATP perception in mammals
involves purinergic P2 receptors, plants do not possess
this family of receptors [97] and the identificiation of
DORN1/LecRK-I.9 thus defines a novel class of eukaryotic
eATP receptors.
Interfamily transfer of plant PRRs for disease-resistance
engineering
The availability of a few confirmed PAMP/PRR or DAMP/
PRR pairs has already clearly helped to demonstrate the
importance of these early sentinel mechanisms for plant
immunity. Some PAMPs and DAMPs are recognized in a
plant family-specific manner, which begs the question of
whether the corresponding PRRs could be transferred
across plant families to provide new recognition specifici-
ties that ultimately may increase disease resistance. In-
deed, expression of the Brassicaceae-specific EFR in N.
benthamiana and tomato (which are members of the Sola-
naceae) led to increased resistance to several pathogenic
bacteria belonging to different genera [28]. Similarly,
transfer of the rice XA21 into sweet orange (Citrus x
sinensis), tomato, and banana conferred enhanced resis-
tance to X. axonopodis pv. citri, Ralstonia solanacearum,
and Xanthomonas campestris pv. musacearum, respective-
ly [98100]. Additionally, expression of the Arabidopsis
eATP receptor DORN1/LecRK-I.9 in N. benthamiana and
potato (Solanum tuberosum) enhances resistance to the
oomycete Phytophthora infestans [101]. These results dem-
onstrate that immune signaling pathways downstream of
PRRs are conserved across plant families and that the
interfamily transfer of PRRs offers a novel potential bio-
technological approach to engineer disease-resistant crop
plants.
Concluding remarks
Plant genomes encode hundreds of RKs and RLPs that may
be potential PRRs. Future challenges include demonstrat-
ing direct binding of PAMPs or DAMPs to their proposed
PRRs, identifying PRRs for orphan PAMPs/DAMPs, and,
conversely, defining the molecules recognized by RKs and
RLPs genetically involved in immunity. Also, it will be
interesting to see whether NBS-LRRs can also be involved
in PAMP/DAMP perception, as observed in mammals. The
expansion of plant postgenomic tools is currently facilitat-
ing rapid identification of plant PRRs. However, the iden-
tification of purified PAMPs/DAMPs remains a major
obstacle; PAMP/DAMP identification is a task often re-
quiring labor-intensive and technically challenging bio-
chemical purifications. Comparative genomic approaches
have led to the successful identification of novel bacterial
PAMPs [23,102] that could be applied to identify further
proteinaceous PAMPs. The identification of PAMPs that
Trends in Immunology July 2014, Vol. 35, No. 7
may be recognized in a family-, genus-, or species-specific
manner also requires the development of bioassay tool-
boxes to measure immune induction in a range of plant
species beyond traditional model plants [17,103].
It is important to define further PAMP or DAMP recog-
nition systems to understand fully the molecular bases of
immune recognition, but also to deploy and engineer these
immune receptors to achieve durable broad-spectrum re-
sistance in crop plants, something that is crucial to guar-
antee the food security required to feed the worlds ever-
expanding population.
Acknowledgments
The author apologizes to colleagues whose work could not be cited here
due to length limitations. Work in the authors laboratory is funded by the
Gatsby Charitable Foundation, the 2Blades Foundation, the European
Research Council, and the UK Biotechnology and Biological Sciences
Research Council. The author thanks his laboratory members for
discussion and C. Faulkner for critical reading of the manuscript.
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