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Plant cell wall dynamics and wall-related susceptibility in plant–pathogen interactions

Daniela Bellincampi, Felice Cervone, Vincenzo Lionetti

Frontiers in Plant Science · 2014 · Review

doi:10.3389/fpls.2014.00228

Abstract

The cell wall is a dynamic structure that often determines the outcome of the interactions between plants and pathogens. It is a barrier that pathogens need to breach to colonize the plant tissue. While fungal necrotrophs extensively destroy the integrity of the cell wall through the combined action of degrading enzymes, biotrophic fungi require a more localized and controlled degradation of the cell wall in order to keep the host cells alive and utilize their feeding structures. Also bacteria and nematodes need to degrade the plant cell wall at a certain stage of their infection process, to obtain nutrients for their growth. Plants have developed a system for sensing pathogens and monitoring the cell wall integrity, upon which they activate defense responses that lead to a dynamic cell wall remodeling required to prevent the disease. Pathogens, on the other hand, may exploit the host cell wall metabolism to support the infection. We review here the strategies utilized by both plants and pathogens to prevail in the cell wall battleground.

Full text

From PubMed Central, U.S. National Library of Medicine, as current on Oct 18, 2026. Paragraph numbers are ours, so an answer can point at one.

INTRODUCTION

Phytopathogenic fungi, bacteria, and nematodes infect, grow and reproduce themselves on the plant tissues and, at least at the early stages of infection, require breaking the integrity of the host cell wall. Beyond the cuticle layer, the interaction with the plant cell wall and the extent of the wall degradation are determined by the lifestyle of the pathogen. Plants perceive a diverse set of microbial molecules referred to as microbial/pathogen associated molecular patterns (MAMPs/PAMPs; ) through high-affinity cell surface pattern recognition receptors (PRRs) leading to intracellular signaling, transcriptional reprogramming, and biosynthesis of defense metabolites that limit the microbial infection. Emerging evidences indicate that plant cells also exploit sophisticated mechanisms of sensing the alteration of cell wall integrity (CWI) during biotic stress. For instance, they perceive endogenous molecules produced in damaged tissues (the so-called damage-associated molecular patterns, or DAMPs) through membrane receptors. The loss of CWI induced by pathogens activates a variety of defense responses including a cell wall remodeling required to prevent the disease. To escape recognition, pathogens produce effector proteins that counteract the plant defenses and, sometimes, exploit the host cell wall metabolism to favor the infection process.

CELL WALL DYNAMICS DURING INFECTION BY MICROBIAL PATHOGENS

Infection by fungal necrotrophs is a complex process that includes conidial attachment, germination, host penetration, lesion formation and expansion, and tissue maceration followed by sporulation. Penetration may be achieved by degrading the external cuticle through the action of cutinases and lipases. The role of the cuticle in plant defense is discussed elsewhere. Once penetrated the cuticle, necrotrophs have a spatial and temporal strategy of attacking the plant cell wall by producing several cell wall degrading enzymes (CWDEs) belonging to multiple families (Figure 1A). The diversity of these enzymes mirrors the structural complexity and the dynamics of the cell wall as well as the lifestyle and host adaptation of the pathogen. The extensive degradation of cell wall polysaccharides by necrotrophs is sensed by plants. The leucine-rich repeat receptor-like kinase (LRR-RLK) ERECTA (ER) and the heterotrimeric G-protein are involved in cell wall remodeling during Arabidopsis defense response against Plectosphaerella cucumerina and probably control CWI. The impairment of cellulose synthases involved in secondary cell wall deposition is also a mechanism of sensing CWI and enhances disease resistance of Arabidopsis to P. cucumerina and Ralstonia solanacearum.

One of the strategies used by plants to limit the degradation of the cell wall polysaccharides by microbial CWDEs is the production of proteinaceous inhibitors (Figures 1A, B). Polygalacturonases (PGs) are pathogenicity factors produced at the earlier stages of a microbial infection that depolymerize the homogalacturonan (HG), i.e., the main component of pectin in dicots but also present in monocots. Against microbial and insect PGs, plants produce cell wall-associated polygalacturonase-inhibiting proteins (PGIPs; ). The over expression of PGIPs improves the resistance to fungal and bacterial necrotrophs in different plants. The PG-PGIP interaction results in the accumulation of elicitor-active oligogalacturonides (OGs) that are perceived in Arabidopsis by the receptor Wall Associated Kinase 1 (WAK1; ) to activate the plant immune responses. Accumulation and sensing of OGs in response to pathogens is critical for monitoring the pectin integrity and, in general, a tissue injury. Alteration of pectin integrity caused by the expression of PGII from Aspergillus niger in tobacco and Arabidopsis causes a constitutive activation of defense genes and resistance against Botrytis cinerea. Recently, B. cinerea and A. niger PGs have been proposed to function themselves as PAMPs recognized by the Arabidopsis Receptor-Like Responsiveness to Botrytis PolyGalacturonase 1 (RBPG1) belonging to a super clade of LRR receptor-like proteins (RLPs; ).

Xylan is the major hemicellulose polymer in cereals. To counteract xylan degradation by microbial endoxylanases, graminaceous monocots produce the Triticum aestivum xylanase inhibitor (TAXI), the xylanase inhibitor protein (XIP) and the thaumatin-like xylanase inhibitor (TL-XI;; ). The constitutive expression of TAXI-III in wheat reduces susceptibility to Fusarium graminearum. On the other hand, fungal xylanases function as PAMPs by eliciting defense responses and promoting necrosis. Ethylene inducing xylanases (EIXs) produced by Trichoderma species are perceived in tomato, by two specific LRR-RLPs receptors, LeEix1 and LeEix2. Both receptors bind Eixs, while only LeEix2 mediates defense responses. LeEix1 heterodimerizes with LeEix2 upon application of the Eixs and attenuates Eix-induced internalization and signaling of the LeEix2 receptor. Xyloglucan, i.e., the main hemicellulosic polysaccharide in the primary walls of dicots and non-graminaceous monocots, is degraded by microbial xyloglucan-specific endoglucanases (XEGs). Fungal XEGs are inhibited by xyloglucan endoglucanase inhibiting proteins (XEGIPs), which so far have been characterized in tomato, carrot and tobacco.

Reinforcement of the cell wall is initiated at the pathogen penetration sites in response to cell wall damage (Figure 1B). Deposition of callose by the callose synthase PMR4 occurs upon infection of Arabidopsis with P. cucumerina and Alternaria brassicicola. Callose deposition is triggered by PAMPs and DAMPs, is affected by environmental conditions and requires the apoplastic accumulation of the hydrolysis products of glucosinolates or benzoxazinoid metabolites.

Deposition of lignin has been associated to resistance of cotton to Verticillium dahliae and of Camelina sativa to Sclerotinia sclerotiorum. Lignin makes the cell wall more resistant to CWDEs and also prevents the diffusion of pathogen-produced toxins. The cell wall may also be reinforced by cross-links and insolubilization of structural proteins like the hydroxyproline-rich glycoproteins (HRGPs) by peroxidase-mediated isodityrosine linkages formed in response to pathogen attach. Plant peroxidases catalyze cross-links between phenolic compounds in the secondary walls and between polysaccharides and ferulic acid (FA) upon attack by necrotrophs. Crosslinks between FA and polysaccharides enhance the recalcitrance of the cell wall to digestion by microbial CWDEs and the overall resistance to fungi. On the other hand, fungal FA esterases may shear FA from the cell wall polysaccharides.

The activities of pectin methyl esterases (PMEs) from both plants and pathogens and the degree and pattern of pectin methyl esterification are critical for the outcome of plant–pathogen infections. The cell walls containing highly methylesterified pectin are somewhat protected against the action of microbial PGs and pectate lyases (PLs; ). PMEs, which remove methyl esters from pectin, are controlled by PME inhibitor proteins (PMEIs) either during growth and development and during plant–pathogen interactions. The biochemical and structural bases of the enzyme/inhibitor interaction have been elucidated. Arabidopsis over expressing PMEIs have a lower level of PME activity, a higher degree of pectin esterification and a concomitant reduced susceptibility to B. cinerea and Pectobacterium carotovorum. The ectopic expression in wheat of a PME inhibitor from kiwi reduces the susceptibility to F. graminearum and Bipolaris sorokiniana. The transcription factor MYB46 which affect the secondary cell wall biosynthesis, regulates the expression of genes encoding several cell wall proteins including PMEI and mediates disease susceptibility of Arabidopsis to B. cinerea. Recently, jasmonic acid has been proposed to modulate the degree of methylesterification in potato to protect pectin degradation by PLs produced by Dickeya dadantii. Acetylation of the cell wall polysaccharides is also a determinant of plant–pathogen interaction. An Arabidopsis mutant with reduced acetylation displays increased tolerance to B. cinerea. Arabidopsis and Brachypodium distachyon plants expressing xylan or pectin acetylesterases from A. nidulans activate specific defense responses and are more resistant to B. cinerea and B. sorokiniana.

Biotrophic and hemi-biotrophic fungi acquire nutrients from the host cells without causing their death. They often attack the plant surface and penetrate the external barriers by developing appressoria and exploiting the mechanical pressure. In order to breach the host cuticle they also secrete oxidases, esterases, cutinases, and lipases. Small amounts of CWDEs associated with local softening and loosening of plant cell walls are produced by biotrophic microorganisms (Figure 2A). Plants contrast invasion of biotrophs by the apposition of “papillae,” cell wall thickening early produced at the site of pathogen penetration (Figure 2B). Papillae contain callose, as most abundant constituent, cellulose, hemicelluloses, pectins, lignin, and structural proteins such as arabinogalactan proteins and HRGPs. Transgenic Arabidopsis plants overexpressing the callose synthase PMR4 show an early and elevated deposition of callose at the sites of penetration which prevents the haustoria formation and further penetration by Golovinomyces cichoracearum and Blumeria graminis. Papillae are also the sites where antimicrobial peptides, toxic secondary metabolites and reactive oxygen species (ROS) accumulate and contribute to plant resistance. Lignification and cross-links of proteins in the papillar cell wall may entrap the penetration peg of biotrophic fungi and render the cell wall more resistant to the mechanical pressure exerted by fungal appressoria. Lignin downregulation may also activate defense responses and increases the resistance to the hemibiotroph Colletotrichum trifolii in alfalfa (Medicago sativa L.).

A reduced cellulose content by mutation of cellulose synthase CESA3, involved in primary cell wall formation, leads to production of lignin, and makes Arabidopsis more resistant to different powdery mildew pathogens. RLKs belonging to the Catharanthus roseus (CrRLK)-like protein family are implicated in CWI mechanisms. Among these, THESEUS1 (THE1) is required for lignification in response to inhibition of cellulose biosynthesis.

Alteration of pectin integrity can trigger plant immunity also against hemibiotrophs. Arabidopsis PMEs, triggered by a Jasmonic acid dependent pathway, contribute to plant immunity against Pseudomonas syringae.

MICROBIAL PATHOGENS EXPLOIT THE HOST CELL WALL METABOLISM TO FACILITATE PATHOGENESIS

Necrotrophs can force plants to cooperate in disease by altering the host cell wall and favoring the cell wall accessibility to CWDEs (; Figure 1C). The Arabidopsis AtPME3 is induced upon infection with B. cinerea and P. carotovorum and functions as susceptibility factor required for the initial colonization of the host tissue. A PG (LePG) and expansin (LeExp1) cooperatively contribute to cell wall loosening during tomato ripening; their expression is induced by necrotrophic pathogens to successfully infect fruits. Transgenic tomato fruits with suppressed expression of LePG and LeExp1 exhibit a reduced susceptibility to B. cinerea. Silencing of two putative endo β-1,4-endoglucanases, involved in the hydrolysis of cellulose or hemicellulose during ripening, cause a reduced susceptibility of tomato fruits to B. cinerea.

Biotrophic fungi, at a later stage of infection, produce a limited and localized degradation of the cell wall in the epidermal or mesophyll cells. On the other hand, they form intracellular structures, like the “haustoria,” i.e., feeding organs invaginated into the host membranes to acquire nutrients. Biotrophs need to avoid the host defense responses and carefully regulate the cell-wall degradation at the border of their feeding structures to allow fungal accommodation and haustorium function (Figure 2C). A screening for Arabidopsis powdery mildew-resistant mutants allowed isolating two pectin-related genes, PMR5 and PMR6 which are pathogen-induced and required for susceptibility to G. cichoracearum and G. orontii. PMR5 encodes a protein with unknown function that shares sequence similarity with genes encoding polysaccharide O-acetyltransferase. Therefore, acetylation may be a host susceptibility mechanism that is reprogrammed by biotrophs during infection. PMR6 encodes a putative PL that is, possibly, recruited by the fungi as a susceptible factor to reduce Ca++-pectate domains at the level of haustoria-plasma membrane and facilitate cell wall porosity and accessibility of host nutrients. Callose deposition may also work in favor of the pathogen by contributing to the stability and function of the haustoria and acting as a barrier that renders haustoria less susceptible to toxic metabolites that are produced by the host and accumulate in the site of infection. On the other hand, callose may limit the diffusion of pathogen-derived elicitors, thus reducing the activation of defense responses.

Many bacterial pathogens utilize a type III secretion system to inject effector proteins directly into the host cytoplasm and manipulate the host cellular activities to their own advantage. The effector AvrPto of P. syringae suppresses a set of Arabidopsis genes that encode cell wall-related defense proteins such as HRGPs.

CELL WALL DYNAMICS IN PLANT INTERACTIONS WITH NEMATODES AND VIRUSES

Changes in the cell wall metabolism occur during plant infection by nematodes. Like biotrophic pathogens, root-knot and cyst nematodes need to establish feeding structures inside the plant tissue to allow the uptake of nutrients. This process is assisted by the secretion of CWDEs such as pectinases and cellulases produced by the nematodes, and by the local expression of host proteins like expansins and cellulases. The sugar beet cyst nematode Heterodera schactii infects Arabidopsis roots and exploits the host-encoded AtPME3. Transgenic plants overexpressing AtPME3 exhibit an increased susceptibility to the nematode. It has been proposed that AtPME3 locally reduces the pectin esterification and improves the cell wall loosening of pre-syncytial cells during the early stages of syncytium formation.

Callose deposition at the level of plasmodesmata (PD) limits the cell-to-cell spreading of plant viruses. Due to the small diameter of the PD pore, some viruses utilize the viral movement proteins (MPs) to modify the PD size exclusion limit. Specific interactions of viral MPs with PME are often required. In addition to MP-PME interaction, the PME-dependent formation of methanol has also been reported to be important for viral cell-to-cell movement. The overexpression of PME inhibitor proteins in tobacco and Arabidopsis contrasts the cell-to-cell and systemic movement of tobamoviruses.

CONCLUSION

The cell wall is the battleground where plants and pathogens attempt to prevail by implementing contrasting wall-reinforcing and wall-weakening strategies. When pathogens start degrading the plant cell wall components, plants are capable of perceiving the loss of wall integrity and subsequently activate the defense signaling pathways. Pathogens try to escape the plant defenses and sometimes take advantage of the host cell wall metabolism to facilitate their entry into the tissue. These dynamic processes vary according to the lifestyle of the pathogen and the type of plant pathogen interaction. While necrotrophy involves a strong and diffused molecular warfare that may provoke extended lesions of the tissue, during biotrophy the battle involves a weaker cell wall degradation mainly localized at the point of penetration and at the level of the feeding apparatus. Perception of cell wall damage as well as the pathogen- and host-induced cell wall remodeling occurs in both cases. The damage of specific cell wall polysaccharides during infection may be perceived by receptors as THE1, ER and WAK1. Plants may also rely on the recognition of CWDEs by LRR-RLPs receptors, as RBPG1 and LeEIX1-2. Cell wall fragments may be released during infection and sensed as damage signals. Analysis of cell wall mutants has shed light on the relationship between cell wall remodeling and plant response to pathogens. The expression of endogenous and microbial CWDEs and their inhibitors is also a valuable approach for studying the dynamics of the cell wall during plant–pathogen interactions as well as a strategy to improve plant protection.

Conflict of Interest Statement

The Review Editor, Dr Ferrari, declares that, despite being affiliated to the same institution as authors Dr Daniela Bellincampi and Dr Felice Cervone, the review process was handled objectively. The authors declare that the research was conducted in the absence of any commercial or financial relationships that could be construed as a potential conflict of interest.

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    Hauck P. Thilmony R. He S. Y. (2003 ). A Pseudomonas syringae type III effector suppresses cell wall-based extracellular defense in susceptible Arabidopsis plants. Proc. Natl. Acad. Sci. U.S.A. 100 8577–8582

    Not in our library10.1073/pnas.1431173100

  50. 50.

    Hematy K. Sado P. E. Van Tuinen A. Rochange S. Desnos T. Balzergue S. (2007 ). A receptor-like kinase mediates the response of Arabidopsis cells to the inhibition of cellulose synthesis. Curr. Biol. 17 922–931

    Not in our library10.1016/j.cub.2007.05.018

  51. 51.

    Herbert C. O’Connell R. Gaulin E. Salesses V. Esquerre-Tugaye M. T. Dumas B. (2004 ). Production of a cell wall-associated endopolygalacturonase by Colletotrichum lindemuthianum and pectin degradation during bean infection. Fungal Genet. Biol. 41 140–147

    Not in our library10.1016/j.fgb.2003.09.008

  52. 52.

    Hernandez-Blanco C. Feng D. X. Hu J. Sanchez-Vallet A. Deslandes L. Llorente F. (2007 ). Impairment of cellulose synthases required for Arabidopsis secondary cell wall formation enhances disease resistance. Plant Cell 19 890–903

    Not in our library10.1105/tpc.106.048058

  53. 53.

    Hewezi T. Howe P. Maier T. R. Hussey R. S. Mitchum M. G. Davis E. L. (2008 ). Cellulose binding protein from the parasitic nematode Heterodera schachtii interacts with Arabidopsis pectin methylesterase: cooperative cell wall modification during parasitism. Plant Cell 20 3080–3093

    Not in our library10.1105/tpc.108.063065

  54. 54.

    Hok S. Attard A. Keller H. (2010 ). Getting the most from the host: how pathogens force plants to cooperate in disease. Mol. Plant Microbe Interact. 23 1253–1259

    Not in our library10.1094/mpmi-04-10-0103

  55. 55.

    Jacobs A. K. Lipka V. Burton R. A. Panstruga R. Strizhov N. Schulze-Lefert P. (2003 ). An Arabidopsis callose synthase, GSL5, is required for wound and papillary callose formation. Plant Cell 15 2503–2513

    Not in our library10.1105/tpc.016097

  56. 56.

    Juge N. (2006 ). Plant protein inhibitors of cell wall degrading enzymes. Trends Plant Sci. 11 359–367

    Not in our library10.1016/j.tplants.2006.05.006

  57. 57.
    Arsenal of plant cell wall degrading enzymes reflects host preference among plant pathogenic fungi · 2011
    No notice
  58. 58.

    Komarova T. V. Sheshukova E. V. Dorokhov Y. L. (2014 ). Cell wall methanol as a signal in plant immunity. Front. Plant Sci. 5:101

    Not in our library10.3389/fpls.2014.00101

  59. 59.

    Laluk K. Mengiste T. (2010 ). Necrotroph attacks on plants: wanton destruction or covert extortion? Arabidopsis Book 8:e0136

    Not in our library10.1199/tab.0136

  60. 60.

    Lionetti V. Cervone F. Bellincampi D. (2012 ). Methyl esterification of pectin plays a role during plant–pathogen interactions and affects plant resistance to diseases. J. Plant Physiol. 169 1623–1630

    Not in our library10.1016/j.jplph.2012.05.006

  61. 61.

    Lionetti V. Raiola A. Camardella L. Giovane A. Obel N. Pauly M. (2007 ). Overexpression of pectin methylesterase inhibitors in Arabidopsis restricts fungal infection by Botrytis cinerea. Plant Physiol. 143 1871–1880

    Not in our library10.1104/pp.106.090803

  62. 62.

    Lionetti V. Raiola A. Cervone F. Bellincampi D. (2013 ). Transgenic expression of pectin methylesterase inhibitors limits tobamovirus spread in tobacco and Arabidopsis. Mol. Plant Pathol. 15 265–274

    Not in our library10.1111/mpp.12090

  63. 63.

    Llorente F. Alonso-Blanco C. Sanchez-Rodriguez C. Jorda L. Molina A. (2005 ). ERECTA receptor-like kinase and heterotrimeric G protein from Arabidopsis are required for resistance to the necrotrophic fungus Plectosphaerella cucumerina. Plant J. 43 165–180

    Not in our library10.1111/j.1365-313x.2005.02440.x

  64. 64.

    Luna E. Pastor V. Robert J. Flors V. Mauch-Mani B. Ton J. (2011 ). Callose deposition: a multifaceted plant defense response. Mol. Plant Microbe Interact. 24 183–193

    Not in our library10.1094/mpmi-07-10-0149

  65. 65.

    Manabe Y. Nafisi M. Verhertbruggen Y. Orfila C. Gille S. Rautengarten C. (2011 ). Loss-of-function mutation of reduced wall acetylation2 in Arabidopsis leads to reduced cell wall acetylation and increased resistance to Botrytis cinerea. Plant Physiol. 155 1068–1078

    Not in our library10.1104/pp.110.168989

  66. 66.

    Mattei B. Raiola A. Caprari C. Federici L. Bellincampi D. De Lorenzo G. (2002 ) “Studies on plant inhibitors of pectin modifying enzymes: polygalacturonase-inhibiting protein (PGIP) and pectin methylesterase inhibitor (PMEI),” in Carbohydrate Bioengineering Interdisciplinary approaches edsTeeri T. T. Svensson B. Gilbert H. J. Feizi T. (CambridgeRoyal Society of Chemistry) 160–167

    Not in our library

  67. 67.

    Moscetti I. Tundo S. Janni M. Sella L. Gazzetti K. Tauzin A. (2013 ). Constitutive expression of the xylanase inhibitor TAXI-III delays fusarium head blight symptoms in durum wheat transgenic plants. Mol. Plant Microbe Interact. 26 1464–1472

    Not in our library10.1094/mpmi-04-13-0121-r

  68. 68.
    The Botrytis cinerea xylanase Xyn11A contributes to virulence with its necrotizing activity, not with its catalytic activity · 2010
    No notice
  69. 69.

    O’Brien J. A. Daudi A. Butt V. S. Bolwell G. P. (2012 ). Reactive oxygen species and their role in plant defence and cell wall metabolism. Planta 236 765–779

    Not in our library10.1007/s00425-012-1696-9

  70. 70.

    Passardi F. Penel C. Dunand C. (2004 ). Performing the paradoxical: how plant peroxidases modify the cell wall. Trends Plant Sci. 9 534–540

    Not in our library10.1016/j.tplants.2004.09.002

  71. 71.

    Pogorelko G. Lionetti V. Bellincampi D. Zabotina O. (2013a ). Cell wall integrity: Targeted post–synthetic modifications to reveal its role in plant growth and defense against pathogens. Plant Signal. Behav. 8 1–8

    Not in our library10.4161/psb.25435

  72. 72.

    Pogorelko G. Lionetti V. Fursova O. Sundaram R. M. Qi M. S. Whitham S. A. (2013b ). Arabidopsis and Brachypodium distachyon transgenic plants expressing Aspergillus nidulans acetylesterases have decreased degree of polysaccharide acetylation and increased resistance to pathogens. Plant Physiol. 162 9–23

    Not in our library10.1104/pp.113.214460

  73. 73.

    Prins T. W. Tudzynski P. Von Tiedemann A. Tudzynski B. ten Have A. Hansen M. E. (2000 ). “Infection strategies of Botrytis cinerea and related necrotrophic pathogens,” in Fungal Pathology ed.Kronstad J. (Dordrecht: Kluwer Academic Publishers) 33–64

    Not in our library10.1007/978-94-015-9546-9_2

  74. 74.

    Raiola A. Camardella L. Giovane A. Mattei B. De Lorenzo G. Cervone F. (2004 ). Two Arabidopsis thaliana genes encode functional pectin methylesterase inhibitors. FEBS Lett. 557 199–203

    Not in our library10.1016/s0014-5793(03)01491-1

  75. 75.

    Raiola A. Lionetti V. Elmaghraby I. Immerzeel P. Mellerowicz E. J. Salvi G. (2011 ). Pectin methylesterase is induced in Arabidopsis upon infection and is necessary for a successful colonization by necrotrophic pathogens. Mol. Plant Microbe Interact. 24 432–440

    Not in our library10.1094/mpmi-07-10-0157

  76. 76.

    Ramirez V. Agorio A. Coego A. Garcia-Andrade J. Hernandez M. J. Balaguer B. (2011 ). MYB46 modulates disease susceptibility to Botrytis cinerea in Arabidopsis. Plant Physiol. 155 1920–1935

    Not in our library10.1104/pp.110.171843

  77. 77.

    Reca I. B. Lionetti V. Camardella L. D’Avino R. Giardina T. Cervone F. (2012 ). A functional pectin methylesterase inhibitor protein (SolyPMEI) is expressed during tomato fruit ripening and interacts with PME-1. Plant Mol. Biol. 79 429–442

    Not in our library10.1007/s11103-012-9921-2

  78. 78.

    Rocchi V. Janni M. Bellincampi D. Giardina T D’Ovidio R. (2011 ). Intron retention regulates the expression of pectin methylesterase inhibitor (Pmei) genes during wheat growth and development. Plant Biol. 14 365–373

    Not in our library10.1111/j.1438-8677.2011.00508.x

  79. 79.

    Ron M. Avni A. (2004 ). The receptor for the fungal elicitor ethylene-inducing xylanase is a member of a resistance-like gene family in tomato. Plant Cell 16 1604–1615

    Not in our library10.1105/tpc.022475

  80. 80.

    Sanchez-Rodriguez C. Estevez J. M. Llorente F. Hernandez-Blanco C. Jorda L. Pagan I. (2009 ). The ERECTA receptor-like kinase regulates cell wall-mediated resistance to pathogens in Arabidopsis thaliana. Mol. Plant Microbe Interact. 22 953–963

    Not in our library10.1094/mpmi-22-8-0953

  81. 81.
    Modifying lignin to improve bioenergy feedstocks: strengthening the barrier against pathogens?† · 2013
    No notice
  82. 82.

    Sella L. Gazzetti K. Faoro F. Odorizzi S. D’Ovidio R. Schafer W. (2013 ). A Fusarium graminearum xylanase expressed during wheat infection is a necrotizing factor but is not essential for virulence. Plant Physiol. Biochem. 64 1–10

    Not in our library10.1016/j.plaphy.2012.12.008

  83. 83.

    Spadoni S. Zabotina O. Di Matteo A. Mikkelsen J. D. Cervone F. DL G. (2006 ). Polygalacturonase-inhibiting protein (PGIP) interacts with pectin through a binding site formed by four clustered residues of arginine and lysine. Plant Physiol. 141 557–564

    Not in our library10.1104/pp.106.076950

  84. 84.

    Taurino M. Abelenda J. A. Rio-Alvarez I. Navarro C. Vicedo B. Farmaki T. (2014 ). Jasmonate-dependent modifications of the pectin matrix during potato development function as a defense mechanism targeted by Dickeya dadantii virulence factors. Plant J. 77 418–429

    Not in our library10.1111/tpj.12393

  85. 85.

    Ton J. Mauch-Mani B. (2004 ). Beta-amino-butyric acid-induced resistance against necrotrophic pathogens is based on ABA-dependent priming for callose. Plant J. 38 119–130

    Not in our library10.1111/j.1365-313x.2004.02028.x

  86. 86.

    Udatha D. B. R. K. Mapelli V. Panagiotou G. Olsson L. (2012 ). Common and distant structural characteristics of feruloyl esterase families from Aspergillus oryzae. PLoS ONE 7:e39473

    Not in our library10.1371/journal.pone.0039473

  87. 87.

    Underwood W. (2012 ). The plant cell wall: a dynamic barrier against pathogen invasion. Front. Plant Sci. 3:85

    Not in our library10.3389/fpls.2012.00085

  88. 88.

    Vanholme B. De Meutter J. Tytgat T. Van Montagu M. Coomans A. Gheysen G. (2004 ). Secretions of plant-parasitic nematodes: a molecular update. Gene 332 13–27

    Not in our library10.1016/j.gene.2004.02.024

  89. 89.

    Vogel J. P. Raab T. K. Schiff C. Somerville S. C. (2002 ). PMR6, a pectate lyase-like gene required for powdery mildew susceptibility in Arabidopsis. Plant Cell 14 2095–2106

    Not in our library10.1105/tpc.003509

  90. 90.

    Vogel J. P. Raab T. K. Somerville C. R. Somerville S. C. (2004 ). Mutations in PMR5 result in powdery mildew resistance and altered cell wall composition. Plant J. 40 968–978

    Not in our library10.1111/j.1365-313x.2004.02264.x

  91. 91.
    Callose-mediated resistance to pathogenic intruders in plant defense-related papillae · 2014
    No notice
  92. 92.

    Volpi C. Janni M. Lionetti V. Bellincampi D. Favaron F D’Ovidio R. (2011 ). The ectopic expression of a pectin methyl esterase inhibitor increases pectin methyl esterification and limits fungal diseases in wheat. Mol. Plant Microbe Interact. 24 1012–1019

    Not in our library10.1094/mpmi-01-11-0021

  93. 93.

    Wieczorek K. Golecki B. Gerdes L. Heinen P. Szakasits D. Durachko D. M. (2006 ). Expansins are involved in the formation of nematode-induced syncytia in roots of Arabidopsis thaliana. Plant J. 48 98–112

    Not in our library10.1111/j.1365-313x.2006.02856.x

  94. 94.

    Wieczorek K. Hofmann J. Blochl A. Szakasits D. Bohlmann H Grundler F. M. W. (2008 ). Arabidopsis endo-1,4-beta-glucanases are involved in the formation of root syncytia induced by Heterodera schachtii. Plant J. 53 336–351

    Not in our library10.1111/j.1365-313x.2007.03340.x

  95. 95.

    Williamson V. M. Kumar A. (2006 ). Nematode resistance in plants: the battle underground. Trends Genet. 22 396–403

    Not in our library10.1016/j.tig.2006.05.003

  96. 96.

    Wilson R. A. Talbot N. J. (2009 ). Under pressure: investigating the biology of plant infection by Magnaporthe oryzae. Nat. Rev. Microbiol. 7 185–195

    Not in our library10.1038/nrmicro2032

  97. 97.

    Xu L. Zhu L. F. Tu L. L. Liu L. L. Yuan D. J. Jin L. (2011 ). Lignin metabolism has a central role in the resistance of cotton to the wilt fungus Verticillium dahliae as revealed by RNA-Seq-dependent transcriptional analysis and histochemistry. J. Exp. Bot. 62 5607–5621

    Not in our library10.1093/jxb/err245

  98. 98.

    Zhang L. Kars I. Essenstam B. Liebrand T. W. Wagemakers L. Elberse J. (2014 ). Fungal endopolygalacturonases are recognized as microbe-associated molecular patterns by the Arabidopsis receptor-like protein responsiveness to Botrytis polygalacturonases1. Plant Physiol. 164 352–364

    Not in our library10.1104/pp.113.230698

  99. 99.
    Comparative analysis of fungal genomes reveals different plant cell wall degrading capacity in fungi · 2013
    Corrected
  100. 100.

    Zhong R. Richardson E. A. Ye Z. H. (2007 ). The MYB46 transcription factor is a direct target of SND1 and regulates secondary wall biosynthesis in Arabidopsis. Plant Cell 19 2776–2792

    Not in our library10.1105/tpc.107.053678

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