To prevent invasion by pathogen plant metabolism must be flexible and active. The life time of reactive oxygen species (ROS) within cell is determined by the antioxidative system which provides protection against oxidative damage. Antioxidant defense system in plants detoxifies the ROS generated during plant infected with the pathogen. The antioxidative system is comprised of several enzymes and compounds of low molecular weight (Noctor and Foyer 1998). If an antioxidant is not present in sufficient quantity to neutralize ROS in plants which is very toxic and reactive,  oxidation of biomolecule such as lipid peroxidation, protein damage, oxidation of  DNA and RNA, enzyme inhibition and activation of apoptosis will occur (Gill and Tuteja 2010; Dumonovic et al., 2021). The induced defense is facilitated via defensive enzymes such as peroxidase (POD), catalase (CAT), superoxide dismutase (SOD) and ascorbate peroxidase (APX). SOD catalyses the dismutation of superoxide anion radical (O2) to hydrogen peroxide (H2O2), CAT dismutases H2O2 to oxygen and water and APX reduces H2O2 to water by utilizing ascorbate (ASC) as the specific electron donor. Antioxidant in plant are water soluble ascorbate, glutathione and phenol and liposoluble tocopherols, tocotrienols and carotenoids (Dumanovic et al., 2021).

The increased activities of  POD, APX, CAT and SOD enzymes was observed in bean leaves infected with bean yellow mosaic virus  indicating ROS scavenging systems can have an important role in managing ROS generated in response to pathogen (Radwan et al., 2010).  Suppression of POD, APX and CAT activities and induction of SOD reflect the role of salicylic acid (SA) in defense responses against the virus infection ((Radwan et al., 2010). The stimulated antioxidative processes contribute to the suppression of necrotic symptom development in leaves with systemic acquired resistance (Fodor et al., 1997). Both plant and fungi have ROS scavenging activities that detoxify ROS directly through the action of enzyme SOD, CAT, glutathione peroxidase (GPX) and peroxiredoxins (Prx) or indirectly via ascorbic acid (vitamin C), tocopherols (vitamin E) and vitamin B6 (Breitenbach et al., 2015;  Hasanuzzaman et al., 2020). Vitamin B6 is an enzymatic cofactor and potent antioxidant and is thus of importance for cellular well-being (Mooney et al., 2009). 

Plant cell consume large quantity of ascorbate. Ascorbate peroxidase eliminate H2O2. Ascorbate is a substrate for cell wall peroxidases and may play a role in the regulation of cell wall lignification during the hypersensitive response (HR), through its capacity to inhibit the oxidation of phenolic compounds by peroxidases (Mehlhorn et al., 1996; Vanacker et al., 1998). The increased apoplastic antioxidant defences indicate establishment of biotrophy in a susceptible host (Vanacker et al., 1998).

Erysiphae graminis f. sp. hordei infects barley plant causing powdery mildew disease. E. graminis f. sp. hordei infection leads to significant changes in the antioxidant metabolism of barley.  El-Zahaby et al.(1995) concluded that in compatible plant-pathogen interaction the lipid peroxidation is insignificant and antioxidant reactions are induced that inhibit tissue necrotization.

The necrotrophic fungus Botrytis cinerea infection resulted in H2O2 and SOD that occurred during plant-pathogen interaction which is crucial for resistance. Nowogorska and Patykowski (2015) suggested Phaseolus vulgaris cv Korona plant was resistant to Pseudomonas syringae pv. phaseolicola (Psp). After inoculation with this pathogen, H2O2 and SOD level changed.  Indicating induction of enzymatic response after Psp, delayed growth of this necrotrophic pathogen.  Increased peroxidase with ferulic acid (FPOD) and peroxidase with syringaldazine (SPOD) activities were observed both after Psp  and Botrytis cinerea infection, which exhibited their role in strengthening plant cell wall during different kind of infection (Nowogorska and Patykowski 2015). The aim was how plants cope with multiple infection with pathogens having different strategy.  

Rice infected with Rhizoctonia solani induces enzymatic scavenger activities of peroxidase, ascorbate peroxidase, catalase and superoxide dismutase (Paranidharan et al., 2003). R. solani is classified into fourteen anastomosis group (AGs) based on hyphal fusion (Garcia et al., 2006). Samsatly et al.(2018) identified vitamin B6 biosynthetic machinery in R. solani AG3 as an antioxidant exhibiting high ability to quench ROS similar to CAT and glutathione s-transferase.   Non-enzymatic antioxidant carbohydrate mannitol is secreted by few fungus that may function as carbohydrate storage compound and as a scavenger of ROS (Jennings et al., 2002; Voegele et al., 2005; Bleau and Spoel 2021). Since Vicia faba plant is unable to synthesize or utilize mannitol thus it becomes a strategy for the biotrophic fungal pathogen (Voegele et al., 2005).

ROS produced in plant as a defense response to pathogen infection, include modulation of cell death and defense –related gene expression. The cell death as HR enhances resistance against biotrophic pathogen but favours infection by necrotrophs. The chloroplastic ROS generated facilitate infection by the necrotrophic fungal pathogen Botrytis cinerea. The modulation of chloroplastic ROS level by the expression of cyanobacterial antioxidant flavodoxin can provide protection against necrotrophic fungal pathogen (Rossi et al., 2017).

Trichoderma reduced H2O2 which might protect membrane lipid from peroxidation. Trichoderma citrinoviride protect plant from disease by functioning as antagonist or by triggering the antioxidant defense system in plants (Sekmen Cetinel et al., 2021).


Bleau, J. R. and Spoel, S. H. 2021 Selective Redox Signaling Shapes Plant Pathogen Interactions. Plant Physiol. 186(1): 53 – 65

Breitenbach, M., Weber, M., Rinnerthaler, M., Karl, T. and Breitenbach-Koller, L. 2015 Oxidative Stress in Fungi: Its Function in Signal Transduction, Interaction with Plant Hosts and Lignocellulose Degradation. Biomolecules 5(2): 318 – 342

doi: 10.3390/biom5020318

Dumanovic, J., Nepovimova, E., Natic, M., Kuca, K. and Jacevic, V. 2021 The Significance of Reactive Oxygen Species and Antioxidant Defense System in Plants. A Concise Overview. Front. Plant Sci. 11: 552969

doi: 10.3389/fpls.2020.552969

El-Zahaby, H. M., Gullner, G. and Kiraly, Z. 1995 Effects of Powdery Mildew Infection of Barley on the Ascorbate-Glutathione Cycle and Other Antioxidants in Different Host-Pathogen Interactions. Phytopathol. 85(10): 1225 – 1230

doi: 10.1094/Phyto-85-1225

Fodor, J., Gullner, G., Adam, A. L., Barna, B., Komives, T. and Kiraly, Z. 1997 Local and Systemic Responses of Antioxidants to Tobacco Mosaic Virus Infection and to Salicylic Acid in Tobacco (Role in Systemic Acquired Resistance). Plant Physiol. 114(4): 1443 – 1451

doi: 10.1104/pp.114.4.1443 z

Garcia, V. G., Onco, M. A. P. and Susan, V. R. 2006 Review Biology and Systematics of the Form Genus Rhizoctonia. Spanish J. Agricultural Res. 4(1): 55 – 79

Gill, S. S. and Tuteja, N. 2010 Reactive Oxygen Species and Antioxidant Machinery in Abiotic Stress Tolerance in Crop Plants. Plant Physiol. Biochem. 48(12): 909 – 930

doi: 10.1016/j.plaphy.2010.08.016

Hasanuzzaman, M., Bhuyan, M. H. M. B., Zulfiqar, F., Raza, A., Mohsin, S. M., Al Mahmud, J., Fujita, M. and Fotopoulos, V. 2020 Reactive Oxygen Species and Antioxidant Defense in Plants Under Abiotic Stress: Revisiting the Crucial Role of a Universal Defense Regulator. Antioxidants 9(8): 681

Jennings, D. B., Daub, M. E., Pharr, D. M. and Williamson, J. D. 2002 Constitutive Expression of a Celery Mannitol Dehydrogenase in Tobacco Enhances Resistance to the Mannitol-Secreting Fungal Pathogen  Alternaria alternata. Plant J. 41 – 49

doi: 10.1046/j.1365-313x.2001.01399.x

Mehlhorn, H., Lelandais, M., Korth, H. G. and Foyer, C. H. 1996 Ascorbate is the Natural Substrate for Plant. FEBS Lett. 378(3): 203 – 206

doi: 10.1016/0014-5793(95)01448-9

Mooney, S., Leuendorf, J-E., Hendrickson, C. and Hellmann, H. 2009 Vitamin B6: A Long known Compound of Surprising Complexity. Molecules 14(1): 329 – 351

doi: 10.3390/molecules14010329

Noctor, G. and Foyer, C. H. 1998 Ascorbate and Glutathione: Keeping Active Oxygen Under Control. Annu. Rev. Plant Physiol. Plant Mol. Biol. 49: 249 – 279

doi: 10.1146/annurev.arplant.49.1.249

Nowogorska, A. and Patykowski, J.  2015 Selected Reactive Oxygen Species and Antioxidant Enzymes in Common Bean after Pseudomons syringae pv. phaseolicola and Botrytis cinerea Infection. Acta Physiologiae Plantarum 37: 1725

Paranidharan, V., Palaniswami, A., Vidhyasekaran, P. and Velazhahan, R. 2003 Induction of Enzymatic Scavengers of Active Oxygen Species in Rice in Response to Infection by Rhizoctonia solani. Acta Physiologiae Plantarum 25: 91 – 96

Radwan, D. E. M., Fayez, K. A., Mahmoud, S. Y. and Lu, G. 2010 Modification of Antioxidant Activity and Protein Composition of Bean Leaf due to Bean Yellow Mosaic Virus  Infection and Salicylic Acid Treatments. Acta Physiol. Plant. 32(5): 891 – 904

doi: 10.1007/s11738-010-0477-y

Rossi, F. R., Krapp, A. R., Bisaro, F., Maiale, S. J., Pieckenstain, F. L. and Carrillo, N. 2017 Reactive Oxygen Species Generated in Chloroplasts Contribute to Tobacco Leaf Infection by the Necrotrophic Fungus Botrytis cinerea. 92(5): 761 – 773

doi: 10.1111/tpj.13718

Samsatly, J., Copley, T. R. and Jabaji, S. H. 2018 Antioxidant Genes of Plants and Fungal Pathogens are Distinctly Regulated during Disease Development in Different Rhizoctonia solani Pathosystems. PLoS ONE 13(2): e0192682

Sekmen Cetinel, A. H., Gokce, A., Erdik, E., Cetinel, B. and Cetinkaya, N. 2021 Trichoderma citrinoviride Treatment Under Salinity Combined to Rhizoctonia solani Infection in Strawberry. Agronomy 11: 1589

Vanacker, H., Carver, T. L. W. and Foyer, C. H. 1998 Pathogen-Induced Changes in the Antioxidant Status of the Apoplast in Barley Leaves. Plant Physiol. 117(3): 1103 – 1114

doi: 10.1104/pp.117.3.1103

Voegele, R. T., Hahn, M., Lohaus, G., Link, T., Heiser, I. and Mendgen, K. 2005 Possible Roles for Mannitol Dehydrogenase in the Biotrophic Plant Pathogen Uromyces fabae. Plant Physiol. 137(1): 190 – 198

doi: 10.1104/pp.104.051839

Leave a Reply

Fill in your details below or click an icon to log in: Logo

You are commenting using your account. Log Out /  Change )

Twitter picture

You are commenting using your Twitter account. Log Out /  Change )

Facebook photo

You are commenting using your Facebook account. Log Out /  Change )

Connecting to %s