Allergenic Content of New Alimentary Pasta Made of Lentils Compared with Lentil Seeds and Analysis of the Impact of Boiling Processing.

There is growing interest in legumes such as lentil as healthy ingredients in gluten-free products. In that respect, foods based on lentils, like alimentary pasta, have been produced and successfully commercialized in recent years. Lentils are also known for inducing severe allergic reactions; however, it is currently unknown if novel alimentary pasta based on lentil retains the same allergenic potential as lentil seeds. In this study, the allergenic content of alimentary lentil pasta compared with lentil seeds was analyzed by immunoassays using sera from patients with allergic sensitization to lentil or with specific antibodies that recognize major lentil allergens. The effect of boiling processing was also analyzed. Results showed that alimentary lentil pasta has a significant allergenic content close to the general allergenic content observed for lentil seeds. Both alimentary lentil pasta and lentil seeds were similarly affected by boiling, with an important transfer of allergens from the food to the boiling water. This study shows that alimentary pasta made of lentils has a significant allergenic potential and highlights the necessity to analyze the allergenic content of new foods and novel ingredients introduced in traditional food products.

Herpes simplex virus 1 proteins can induce skin inflammation in an atopic dermatitis-like mouse model.

Herpes simplex virus type 1 (HSV-1) can induce in certain individuals with atopic dermatitis (AD) severe cutaneous infections that can spread throughout the entire body, a condition named as AD complicated by eczema herpeticum (ADEH). It has been recently found that ADEH patients can produce specific IgE against HSV-1 proteins, which may contribute to lower protection against HSV-1. However, little is known about the capacity of these HSV-1 proteins to produce an inflammatory response at the skin level. In this study, using a mouse model of AD-like dermatitis, three HSV-1 proteins (glycoprotein D -gD-, glycoprotein B -gB- and VP22) were applied on tape-stripped back skin mice in three exposures periods. Ovalbumin (OVA) and 0.9% NaCl were used as positive and negative controls, respectively. Skin samples were obtained for analysis of specific cell components of skin infiltration. The results showed that the viral protein gD induced a statistically significant increase in the number of dermal infiltrating CD3+, CD4+ cells and mast cells compared with the negative control group. gD was also able to induce epidermal thickening and epidermal infiltration of T cells closely related to the one produced in mice sensitized with OVA. However, VP22 and gB contributed to a lesser extent to skin inflammation. These results showed that proteins from HSV-1, especially gD, can have per se an important T cell and mast cell-driven inflammatory potential at the skin level.

Novel alimentary pasta made of chickpeas has an important allergenic content that is altered by boiling in a different manner than chickpea seeds.

Alimentary pasta made of chickpeas has been recently introduced in the market. The novelty and presentation of this food can have a confounding effect on chickpea allergic patients and can pose a risk to them. The allergenic content of novel alimentary chickpea pasta in comparison with regular chickpea seeds has not been analyzed so far. Protein extracts were obtained, and the allergenic content was analyzed with sera from chickpea allergic patients and antibodies against major allergens by western blot, ELISA, dot blot, and cellular assays. Alimentary chickpea pasta showed an important content in IgE-binding proteins and chickpea allergens: 7S globulin, 2S albumin, LTP, and PR-10, similar to hydrated and boiled chickpea seeds. During boiling, more allergens from alimentary chickpea pasta were transferred to the boiling water than chickpea seeds. Novel alimentary chickpea pasta retains an important allergenic content which is affected by boiling by transferring allergens to the cooking water.

Acidic pH Decreases the Endonuclease Activity of Initiator RepB and Increases the Stability of the Covalent RepB-DNA Intermediate while Has Only a Limited Effect on the Replication of Plasmid pMV158 in Lactococcus lactis.

Plasmid vectors constitute a valuable tool for homologous and heterologous gene expression, for characterization of promoter and regulatory regions, and for genetic manipulation and labeling of bacteria. During the last years, a series of vectors based on promiscuous replicons of the pMV158 family have been developed for their employment in a variety of Gram-positive bacteria and proved to be useful for all above applications in lactic acid bacteria. A proper use of the plasmid vectors requires detailed knowledge of their main replicative features under the changing growth conditions of the studied bacteria, such as the acidification of the culture medium by lactic acid production. Initiation of pMV158 rolling-circle replication is catalyzed by the plasmid-encoded RepB protein, which performs a sequence-specific cleavage on one of the parental DNA strands and, as demonstrated in this work, establishes a covalent bond with the 5'-P end generated in the DNA. This covalent adduct must last until the leading-strand termination stage, where a new cleavage on the regenerated nick site and a subsequent strand-transfer reaction result in rejoining of the ends of the cleaved parental strand, whereas hydrolysis of the newly-generated adduct would release the protein from a nicked double-stranded DNA plasmid form. We have analyzed here the effect of pH on the different in vitro reactions catalyzed by RepB and on the in vivo replication ability of plasmid pMV158. We show that acidic pH greatly impairs the catalytic activity of the protein and reduces hydrolysis of the covalent RepB-DNA adduct, as expected for the nucleophilic nature of these reactions. Conversely, the ability of pMV158 to replicate in vivo, as monitored by the copy number and segregational stability of the plasmid in Lactococcus lactis, remains almost intact at extracellular pHs ranging from 7.0 to 5.0, and a significant reduction (by ∼50%) in the plasmid copy number per chromosome equivalent is only observed at pH 4.5. Moreover, the RepB to pMV158 molar ratio is increased at pH 4.5, suggesting the existence of compensatory mechanisms that operate in vivo to allow pMV158 replication at pH values that severely disturb the catalytic activity of the initiator protein.