Variant vicilins from a resistant Vigna unguiculata lineage (IT81D-1053) accumulate inside Callosobruchus maculatus larval midgut epithelium

Oliveira, Gabriel B.; Kunz, Daniele; Peres, Tanara Vieira; Leal, Rodrigo Bainy; Uchôa, Adriana Ferreira; Samuels, Richard Ian; Macedo, Maria Lígia Rodrigues; Carlini, Célia R.; Ribeiro, Alberto F.; Grangeiro, Thalles Barbosa; Terra, Walter R.; Xavier‐Filho, J.; Silva, Carlos P.

doi:10.1016/j.cbpb.2013.11.001

Cited by 13 publications

(10 citation statements)

References 29 publications

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“…These results are in accordance with those obtained by some authors (Sales et al, 1992;Macedo et al 1993;Ignacimuthu et al, 2000;Mota et al, 2003;Sales et al, 2005;Oliveira et al, 2014) working on legume seeds and their varieties, who reported that antinutrients like the vicilins (55 KD polypeptides) played a role in imparting resistance to bruchids. Moreover, Sales et al (2005) added that C. maculatus emerged from resistant cowpea seeds variety (IT81 D-1045) excreted 7 times higher vicilins and 0.4 time less trypsin inhibitors than that emerged from susceptible seeds variety (Epac 10).…”

Section: Vicilinssupporting

confidence: 92%

CERTAIN STORAGE PROTEINS AND THEIR ROLE IN THE RESISTANCE OF SOME LEGUME SEED TYPES AND VARIETIES TO INFESTATION WITH THE COWPEA SEEDS BEETLE, Callosobruchus maculatus (F.)

El-Sitiny

Hassanein

Hammad

et al. 2016

Zagazig Journal of Agricultural Research

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Seventeen legume seed varieties belonging to ten types were analyzed for each of total proteins, trypsin inhibitors, vicilins and lectins to study the relationship between the presence of the storage seed proteins in legume seeds and resistance to infestation with the cowpea seeds beetle, Callosobruchus maculatus (F.) under no-choice bioassay at constant conditions of 29±1°C and 70 ± 5% RH. The tested types and varieties were cowpea (Fitriat, Forage and Kafr El-Sheikh), fababean (Aquadams, Giza 843 and Sakha 1), pea (Master B and Smooth) common bean (Bronco and Nepraska), lupin (Giza 1 and White lupin), chickpea (Giza 195), soyabean (Giza 111), lentil (Giza 9), guar (Guvar bean) and lablab (Egyptian kidney bean). To clarify the impact of the storage seed proteins in legume seed varieties and types on infestation with C. maculatus, larval period, pupal period, least and mean complete developmental periods, number of emerged adults per female, percentage of adults emergence and sex ratio (as percentage of males) were determined. Moreover, susceptibility index, infested seeds (%), mean number of holes per infested seed, seeds weight loss (%), weight of early emerged adult and number of dead individuals inside seeds per female were assessed as infestation parameters. The obtained results showed that, each of total proteins, trypsin inhibitors, vicilins and lectins of different tested legume seed varieties and types are negatively correlated with all aforesaid resistance parameters with the exception of those respecting larval and pupal durations, least and mean complete developmental periods and number of dead individuals inside seeds per female. As regards total proteins of varieties, larval period, least and mean complete developmental periods, susceptibility index and number of dead individuals inside seeds per female reached high significance degree at 0.01 level of probability, whereas pupal period obviously showed significant correlation coefficient at 0.05 level of probability. But, the other studied resistance parameters did not demonstrate significant correlations. Significancy test of correlation relationships respecting trypsin inhibitors clearly proved to be insignificant for all studied characters, except for those of larval stage period, least and mean developmental periods which cleared highly significant correlations and significant ones with susceptibility index, number of holes per infested seed and number of dead individuals inside seeds per female. All tested seed varieties of guar, lupin and common bean revealed completely linear inverse relationship between trypsin inhibitors and susceptibility to cowpea seeds beetle infestation indicating deterring effects for insect development. Also, vicilins content proved that simple correlation coefficient values regarding the abovementioned resistance parameters reached high significancy degree excepting those concerning larval stage period, percentage of infested seeds, seeds weight loss percentage and weight of emerged adult that showed significant corr...

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Section: Vicilinssupporting

confidence: 92%

CERTAIN STORAGE PROTEINS AND THEIR ROLE IN THE RESISTANCE OF SOME LEGUME SEED TYPES AND VARIETIES TO INFESTATION WITH THE COWPEA SEEDS BEETLE, Callosobruchus maculatus (F.)

El-Sitiny

Hassanein

Hammad

et al. 2016

Zagazig Journal of Agricultural Research

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“…Vicilins isolated from a variety of legume seeds have been reported to bind strongly to chitin, chitosan and fully acetylated chitin [ 17 – 19 ]. These interactions were proposed to explain their detrimental effects on the development of the cowpea weevil ( Callosobruchus maculatus ), a bruchid insect that is a pest of cowpea seeds [ 19 , 20 ] as well as their interference with the germination of spores or conidia of phytopathogenic fungi [ 21 ].…”

Section: Introductionmentioning

confidence: 99%

A Nontoxic Polypeptide Oligomer with a Fungicide Potency under Agricultural Conditions Which Is Equal or Greater than That of Their Chemical Counterparts

et al. 2015

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There are literally hundreds of polypeptides described in the literature which exhibit fungicide activity. Tens of them have had attempted protection by patent applications but none, as far as we are aware, have found application under real agricultural conditions. The reasons behind may be multiple where the sensitivity to the Sun UV radiation can come in first place. Here we describe a multifunctional glyco-oligomer with 210 kDa which is mainly composed by a 20 kDa polypeptide termed Blad that has been previously shown to be a stable intermediary product of β-conglutin catabolism. This oligomer accumulates exclusively in the cotyledons of Lupinus species, between days 4 and 12 after the onset of germination. Blad-oligomer reveals a plethora of biochemical properties, like lectin and catalytic activities, which are not unusual per si, but are remarkable when found to coexist in the same protein molecule. With this vast range of chemical characteristics, antifungal activity arises almost as a natural consequence. The biological significance and potential technological applications of Blad-oligomer as a plant fungicide to agriculture, its uniqueness stems from being of polypeptidic in nature, and with efficacies which are either equal or greater than the top fungicides currently in the market are addressed.

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“…This interferes with digestive and absorptive processes resulting in substantial growth inhibition of larvae fed on resistant seeds. The toxicity of these vicilins seems to be related to their interaction with N ‐acetylglucosamine containing glycoproteins and other microvillar membrane constituents prior to their internalization by enterocytes which results in interference with the physiology of these cells . There is evidence that the internalization of vicilins into midgut epithelial cells of C. maculatus larvae is mediated by an enterocyte microvillar membrane‐bound receptor with homology to alpha‐tocopherol transfer proteins …”

Section: Functional Biology Of Proteins Present In Seeds and Peanutsmentioning

confidence: 99%

The functional biology of peanut allergens and possible links to their allergenicity

Ozias‐Akins

Breiteneder

2019

Allergy

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Peanut is one of the most common food triggers of fatal anaphylaxis worldwide although peanut allergy affects only 1%‐2% of the general population. Peanuts are the source of highly potent allergenic proteins. It is emerging that the allergenicity of certain proteins is linked to their biological function. Peanut is an unusual crop in that it flowers aboveground but produces its seed‐containing pods underground. This so‐called geocarpic fruiting habit exposes pods and seeds during their development to soilborne pathogens and pests. Pest damage can also open routes of entry for opportunistic fungi such as Aspergillus . Although seed proteins have primary functions in nutrient reservoirs, lipid storage bodies, or the cytoskeleton, they have also evolved to act as part of the plant's defense system to enhance fitness and survival of the species. When interacting with pathogens or pests, these proteins modify and damage cells' membranes, interact with immune receptors, and modulate signaling pathways. Moreover, following exposure, the immune system of predisposed individuals reacts to these proteins with the production of specific IgE. This review explores the evolutionary biology of peanut and its seed proteins and highlights possible links between the proteins' biological function and their allergenicity.

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Variant vicilins from a resistant Vigna unguiculata lineage (IT81D-1053) accumulate inside Callosobruchus maculatus larval midgut epithelium

Cited by 13 publications

References 29 publications

CERTAIN STORAGE PROTEINS AND THEIR ROLE IN THE RESISTANCE OF SOME LEGUME SEED TYPES AND VARIETIES TO INFESTATION WITH THE COWPEA SEEDS BEETLE, Callosobruchus maculatus (F.)

CERTAIN STORAGE PROTEINS AND THEIR ROLE IN THE RESISTANCE OF SOME LEGUME SEED TYPES AND VARIETIES TO INFESTATION WITH THE COWPEA SEEDS BEETLE, Callosobruchus maculatus (F.)

A Nontoxic Polypeptide Oligomer with a Fungicide Potency under Agricultural Conditions Which Is Equal or Greater than That of Their Chemical Counterparts

The functional biology of peanut allergens and possible links to their allergenicity

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