Abstract

Arabinogalactans (AGs) are structural polysaccharides of the plant cell wall. A small proportion of the AGs are associated with hemicellulose and pectin. Furthermore, AGs are associated with proteins forming the so-called arabinogalactan proteins (AGPs), which can be found in the plant cell wall or attached through a glycosylphosphatidylinositol (GPI) anchor to the plasma membrane. AGPs are a family of highly glycosylated proteins grouped with cell wall proteins rich in hydroxyproline. These glycoproteins have important and diverse functions in plants, such as growth, cellular differentiation, signaling, and microbe-plant interactions, and several reports suggest that carbohydrate components are crucial for AGP functions. In beneficial plant-microbe interactions, AGPs attract symbiotic species of fungi or bacteria, promote the development of infectious structures and the colonization of root tips, and furthermore, these interactions can activate plant defense mechanisms. On the other hand, plants secrete and accumulate AGPs at infection sites, creating cross-links with pectin. As part of the plant cell wall degradation machinery, beneficial and pathogenic fungi and bacteria can produce the enzymes necessary for the complete depolymerization of AGs including endo-β-(1,3), β-(1,4) and β-(1,6)-galactanases, β-(1,3/1,6) galactanases, α-L-arabinofuranosidases, β-L-arabinopyranosidases, and β-D-glucuronidases. These hydrolytic enzymes are secreted during plant-pathogen interactions and could have implications for the function of AGPs. It has been proposed that AGPs could prevent infection by pathogenic microorganisms because their degradation products generated by hydrolytic enzymes of pathogens function as damage-associated molecular patterns (DAMPs) eliciting the plant defense response. In this review, we describe the structure and function of AGs and AGPs as components of the plant cell wall. Additionally, we describe the set of enzymes secreted by microorganisms to degrade AGs from AGPs and its possible implication for plant-microbe interactions.

Highlights

  • Cell wall is an essential component of plant cells; they confer flexibility and mechanical support to the cell and perform important functions such as the maintenance of cell, preservation of osmotic pressure, movement of water and nutrients, management of intercellular communication between adjacent cells and prominent involvement in plant-microbe interactions, constituting the main barrier against potential pathogens (Burton et al, 2010; Keegstra, 2010).Chemically, a plant cell wall (PCW) is composed of cellulosic polysaccharides, non-cellulosic polysaccharides, lignin, and proteins

  • Several studies have shown that plant pathogenic bacteria and fungi secrete a set of enzymes that degrade arabinogalactans from arabinogalactan proteins (AGPs), little attention has been paid to their role in infection processes

  • It has been suggested that AGPs can prevent infection by pathogenic microorganisms or inhibit their development because the degradation products generated by hydrolytic enzymes of pathogens can act as damage-associated molecular patterns (DAMPs) and promote the plant defense response

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Summary

Introduction

Cell wall is an essential component of plant cells; they confer flexibility and mechanical support to the cell and perform important functions such as the maintenance of cell, preservation of osmotic pressure, movement of water and nutrients, management of intercellular communication between adjacent cells and prominent involvement in plant-microbe interactions, constituting the main barrier against potential pathogens (Burton et al, 2010; Keegstra, 2010).Chemically, a plant cell wall (PCW) is composed of cellulosic polysaccharides (cellulose microfibrils from 40.6– 51.2% of dry weight), non-cellulosic polysaccharides, lignin, and proteins. Several studies have shown that plant pathogenic bacteria and fungi secrete a set of enzymes that degrade arabinogalactans from AGPs, little attention has been paid to their role in infection processes.

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