Antiviral Action of Native and Methylated Lactoferrin and β-Lactoglobulin against Potato Virus Y (PVY) Infected into Potato Plants Grown in an Open Field

Abstract

Potato plants are liable to PVY infection without efficient control. Therefore, they were cultivated under greenhouse and open field conditions, artificially infected with PVY and then treated after 15 days of infection with native lactoferrin (LF) and native β-lactoglobulin (BL) and their esterified forms, MLF (methylated lactoferrin) and BLM (methylated β-lactoglobulin) to test the efficiency of this approach. Viral replication was inhibited by the applied substances, particularly the methylated forms, in a concentration-dependent manner, where the concentration of 500 μg·mL−1 was sufficient for plant protection against the PVY infection. An open field experiment showed that one single application of the antiviral substance was enough for maximum inhibitory action against PVY. The modified milk proteins induced higher inhibitory action on PVY virus replication in the plants, compared to their native forms, which was reflected by potato growth and yield. Using the dot blot hybridization and RT-PCR techniques to detect PVY in the experimental plants showed the supremacy of native and esterified LF in inhibiting the targeted virus. The generally observed scanning electronic microscopy (SEM) structural deformations and irregular appearance in PVY particles when treated with MLF and BLM revealed their direct action. BLM, MLF and LF are efficient antiviral agents against PVY. They can not only abolish the observed PVY-induced reduction in potato growth and tuber yield, but also further increase them to higher levels than negative control.

Soybean β‐conglycinin and catfish cutaneous mucous p22 glycoproteins deteriorate sporangial cell walls of Pseudoperonospora cubensis and suppress cucumber downy mildew

“…18 Numerous types of glycoproteins were recognized for their antimicrobial activity against co-existing plant, human and animal pathogens. 2,3,11,18,[70][71][72][73][74][75] Such species of bio-derived antimicrobial proteins represent an effective alternative for chemical fungicides as they do not harm the environmental safety and can efficiently eradicate microbial pathogens. This study defined the antifungal activity of four naturally derived glycoproteins and examined the mechanism by which they suppress the plant pathogenic fungus, P. cubensis.…”

Milk Whey Hydrolysates as High Value-Added Natural Polymers: Functional Properties and Applications

“…Hydrolysates, with a molecular weight under 10 kDa composed of basic, aliphatic and polar amino acids with an isoelectric point greater than 10, present excellent antiviral effect due to their capacity to form amphipathic structures. Their good efficacy, safe, selectivity, and predictable metabolism are the main strengths of peptides in drug production [ 123 , 124 , 125 , 126 , 127 ].…”

Foliar Spray with Pepsin-and Papain-Whey Protein Hydrolysates Promotes the Productivity of Pea Plants Cultivated in Clay Loam Soil

“…Generally, natural proteins are extracted in pure forms and can be biologically active at its native form [ 22 ] or after chemical [ 23 , 24 , 25 , 26 , 27 ] or enzymatic [ 17 ] modifications to improve or enhance their potential recycling uses [ 28 ]. Whey proteins and their main components (α-lactalbumin, β-lactoglobulin and lactoferrin) have been the focus of several studies to explore their chemical nature, their potential feasibility for chemical or enzymatic modifications and their possible biological reuses.…”

“…Pepsin is an endopeptidase that is most active in acidic environments at 37-42 • C and preferentially cleaves at the C-terminal side of aromatic amino acids, such as phenylalanine, tryptophan, and tyrosine [21]. Papain, also known as papaya proteinase I, is a cysteine protease (EC 3.4.22.2) present in papaya (Carica papaya) that is relatively heat-resistant and cleaves peptide bonds after arginine or lysine preceded by a hydrophobic unit [21] Generally, natural proteins are extracted in pure forms and can be biologically active at its native form [22] or after chemical [23][24][25][26][27] or enzymatic [17] modifications to improve or enhance their potential recycling uses [28]. Whey proteins and their main components (α-lactalbumin, β-lactoglobulin and lactoferrin) have been the focus of several studies to explore their chemical nature, their potential feasibility for chemical or enzymatic modifications and their possible biological reuses.…”