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1.
Indian J Ophthalmol ; 2024 Mar 08.
Article in English | MEDLINE | ID: mdl-38454850

ABSTRACT

PURPOSE: To investigate and compare the anatomic and functional outcomes of chandelier-assisted scleral buckling (CASB) surgery using contact versus non-contact lens-based wide-angle viewing systems (WAVSs) in rhegmatogenous retinal detachment (RRD) patients. METHODS: This was a retrospective, multicenter study evaluating the anatomic (reattachment rate) and visual acuity (VA) outcomes at 6 months post-CASB for primary RRD. RESULTS: Forty-seven RRD patients underwent CASB with a non-contact WAVS (Group C1) and 90 with a contact lens WAVS (Group C2). Preoperative parameters including myopia, macula-off RRD, posterior vitreous detachment, number of retinal breaks, and retinal dialysis as the etiology of RRD did not differ significantly between the two groups. The outcomes of retinal attachment (85.11% of C1 patients and 76.67% of C2 patients, P = 0.34) and final visual outcome (VA ≥6/12: C1 = 61.7%; C2 = 46.67%, P = 0.13) were also comparable. Furthermore, no significant difference in postoperative complications such as cataracts, glaucoma, infection, buckle exposure, and buckle failure was observed. Finally, both groups were comparable in terms of re-detachment rates (10.64% in C1 and 23.33% in C2, P = 0.11). CONCLUSION: The two WAVS approaches used in CASB surgery have comparable surgical and functional outcomes and postoperative complications. The operating surgeon can freely choose between these viewing platforms during the contemporary scleral bucking (SB) surgery without impacting the outcome.

3.
J Sci Food Agric ; 103(2): 877-890, 2023 Jan 30.
Article in English | MEDLINE | ID: mdl-36057923

ABSTRACT

BACKGROUND: Computational tools may have an edge over conventional methods for the preliminary evaluation of food allergenicity. In this study, the allergenic potential of Lentinula edodes was evaluated and validated using in silico tools. RESULTS: The potential cross-reactivity of mushroom proteins with fungal allergens was determined using sequence alignment - the Fast Alignment (FASTA) and Basic Local Alignment Search Tool (BLAST) algorithm. Eight L. edodes proteins were cross-reactive with allergens from fungal origin, showing 52%-89% sequence identity using FASTA algorithm-based alignment. The BLAST data were corroborated by percentage identity and query coverage. Physico-chemical property-based allergenicity was deciphered by AlgPred, Allermatch, and AllergenFP software, which predicted six out of eight proteins as potential allergens. Sequence alignment showed 66%-86% conservancy between mushroom protein and known fungal allergens. Secondary structure and amino acid composition supported structural affinity between query and fungal proteins. Three-dimensional structures of five mushroom proteins were generated, quality assessed, and superimposed with fungal allergens, suggesting possible allergenicity of mushroom proteins. An enzyme-linked immunosorbent assay (ELISA) demonstrated immunoglobulin E (IgE) binding in 13 out of 21 food-hypersensitive patients' sera. CONCLUSION: In silico tools provide preliminary indications about the potential allergenicity and cross-reactivity of mushroom proteins. This approach may be used for the prelusive allergenicity assessment of allergen sources. © 2022 Society of Chemical Industry.


Subject(s)
Food Hypersensitivity , Shiitake Mushrooms , Humans , Allergens/chemistry , Sequence Alignment , Cross Reactions
4.
Front Microbiol ; 13: 962619, 2022.
Article in English | MEDLINE | ID: mdl-36060785

ABSTRACT

Pesticides are either natural or chemically synthesized compounds that are used to control a variety of pests. These chemical compounds are used in a variety of sectors like food, forestry, agriculture and aquaculture. Pesticides shows their toxicity into the living systems. The World Health Organization (WHO) categorizes them based on their detrimental effects, emphasizing the relevance of public health. The usage can be minimized to a least level by using them sparingly with a complete grasp of their categorization, which is beneficial to both human health and the environment. In this review, we have discussed pesticides with respect to their global scenarios, such as worldwide distribution and environmental impacts. Major literature focused on potential uses of pesticides, classification according to their properties and toxicity and their adverse effect on natural system (soil and aquatic), water, plants (growth, metabolism, genotypic and phenotypic changes and impact on plants defense system), human health (genetic alteration, cancer, allergies, and asthma), and preserve food products. We have also described eco-friendly management strategies for pesticides as a green solution, including bacterial degradation, myco-remediation, phytoremediation, and microalgae-based bioremediation. The microbes, using catabolic enzymes for degradation of pesticides and clean-up from the environment. This review shows the importance of finding potent microbes, novel genes, and biotechnological applications for pesticide waste management to create a sustainable environment.

5.
Curr Protein Pept Sci ; 23(7): 475-494, 2022.
Article in English | MEDLINE | ID: mdl-35927799

ABSTRACT

BACKGROUND: In-silico mapping of epitopes by immune-informatics has simplified the efforts towards understanding antigen-antibody interactions. The knowledge of allergen epitopes may help in advancing the diagnosis and therapy of allergic diseases. OBJECTIVE: This study was intended to identify B and T cell epitopes of cysteine protease allergen of Phaseolus vulgaris. METHODS: Modeller 9v20 software was used for the generation of three-dimensional model of cysteine protease and quality assessment was performed using SAVES webserver and other in silico software. Linear and conformational B and T cell epitopes were predicted via immuno-informatics based computational servers. Epitopes were synthesized and their immunoreactivity was analyzed using specific IgE ELISA with food allergy positive patient's sera. Cellular immune response of peptides was determined through basophil activation assay. Consurf and SDAP (property distance) were used to examine the evolutionary conservancy and potential cross-reactivity of predicted epitopes. MSA based positional conservancy between HDM allergen epitopes and predicted peptides was also established using IEDB epitope database. Finally, population coverage for each promiscuous T cell epitope was predicted using IEDB population coverage analysis tool. RESULTS: Cysteine protease structure was derived by homology modeling and combination of bioinformatic tools predicted three B- and three T-cell peptides by consensus method and validated computationally. ELISA with kidney bean sensitive patient's sera showed higher IgE binding of B-cell peptides as compared to T-cell or control peptides. Epitope conservancy revealed B-cell epitopes being upto 95% conserved in comparison to variable T-cell epitopes (upto 69%). B-cell peptides were crossreactive with homologous allergens based on PD values. Structural comparison of cysteine protease with Der p 1 and Der f 1 showed similar epitopic regions, validating the prediction accuracy of epitopes. Promiscuous T-cell epitopes binding to broad-spectrum class-II MHC alleles demonstrated the distribution of T-cell peptides world-wide (30-98%) and in Asian population (99%). CONCLUSION: The current approach can be applied for identification of epitopes. Analysis of crossreactive and widely-distributed specific epitopes of allergen and knowledge about their interactive surfaces will help in understanding of food allergy and related immune responses.


Subject(s)
Cysteine Proteases , Food Hypersensitivity , Phaseolus , Humans , Allergens , Epitopes, T-Lymphocyte/chemistry , Immunoglobulin E , Peptides
6.
J Med Life ; 15(5): 705-716, 2022 May.
Article in English | MEDLINE | ID: mdl-35815079

ABSTRACT

Numerous surgical procedures are used to correct gingival recession, like free gingival graft, pedicle graft, and connective tissue graft. Our study aimed to compare and clinically evaluate root coverage using a coronally advanced flap (CAF) with and without Biomesh® membrane to treat recession type 1 (RT1) and type 2 (RT2) defects. A total of 20 systemically stable patients, both males and females between the ages of 20 and 40, with bilateral recession defects in maxillary canines and premolars, were included in the study. Patients were divided into two groups: the control group: coronally advanced flap only and the test group: coronally advanced flap with Biomesh® membrane. All clinical parameters showed significant reductions from baseline, 1 month, 3 months, and 6 months post-surgery. Gingival recession significantly reduced both in test and control groups with no intergroup difference. The exposed root was covered by 70% in the test group and 78% in the control group. Clinical attachment level, the width of keratinized tissue, recession height, and recession width was significantly increased in the case of coronally advanced flap alone with significant intragroup comparison. The results for both treatment techniques for recession coverage were compared. CAF displayed superior results than CAF along with Biomesh® membrane in terms of clinical attachment level, root coverage percentage, and attached gingiva width.


Subject(s)
Gingival Recession , Female , Follow-Up Studies , Gingival Recession/surgery , Humans , Male , Periodontal Attachment Loss/surgery , Tooth Root/surgery , Treatment Outcome
8.
J Food Biochem ; 46(9): e14232, 2022 09.
Article in English | MEDLINE | ID: mdl-35592951

ABSTRACT

A commonly consumed legume in India, the kidney bean (Phaseolus vulgaris) is associated with allergy. We report molecular and immunological characterization of cysteine protease allergen and its cross-reactivity. In silico allergenicity assessment and phylogenetic analysis of kidney bean cysteine protease showed significant sequence homology (upto 67%) with allergens from kiwi, papaya, soybean, ragweed pollen and mites. Physicochemical properties and motif-analysis depicted cysteine protease as probable allergen. Multiple sequence alignment and phylogenetic analysis indicated structural conservation between kidney bean and homologous cysteine protease sequences. The gene was cloned, expressed and affinity purified. Cysteine protease was resolved at 42 kDa and exhibited high IgE binding (up to 89%) with hypersensitive sera. Cysteine protease showed functional property on cross-linking IgE receptors and upregulated expression of CD203c on activated basophils. In inhibition studies, 8.4 ng of cysteine protease was required for 50% self-inhibition, whereas significant inhibition was also observed with kidney bean (52 ng), black gram (155 ng), chick pea (437 ng), mesquite pollen (36 ng), house dust mite (64.85 ng), Alternaria alternata (78.8 ng) and Curvularia lunata (73.6 ng) extracts. ConSurf analysis indicated conserved active site and catalytic residues in mature domain among proteases from legumes, fruits, pollens, mites and fungus. In summary, P. vulgaris cysteine protease was molecularly characterized having functional activity. This study demonstrated, cross-reactivity between food and aeroallergens based on evolutionary conservancy that showed its clinical importance as cross-reactive allergen. PRACTICAL APPLICATIONS: Adaptation of sustainable lifestyle has led to a surge in consumption of plant-based foods especially legumes. Their high nutritional content lowers the risk of developing cardiovascular diseases, diabetes, obesity, and stroke. Kidney beans, a commonly consumed legume in Indian subcontinent, have a potential to be used as nutraceutical and functional food. Despite its alimentary nature, it elicits allergic reactions. Being a major sensitizer, trivial information regarding its allergic components has led to an urgent need for exploring its allergen repertoire. Our study reported biochemical and immunological characterization of its major cysteine protease allergen. Cysteine proteases are major cross-reactive allergens from insects, fruits and fungal sources. Identification and molecular characterization of such immunodominant allergens by RDT offers the prospect of using recombinant proteins for accurate diagnosis and therapeutic purposes. This study suggests that a potential major cross-reactive allergen may aid in developing allergy management interventions for a wide range of allergenic sources.


Subject(s)
Allergens , Cysteine Proteases , Phaseolus , Allergens/chemistry , Cysteine Proteases/genetics , Immunoglobulin E/genetics , Phaseolus/genetics , Phylogeny
9.
J Pharmacopuncture ; 22(2): 115-121, 2019 Jun.
Article in English | MEDLINE | ID: mdl-31338252

ABSTRACT

OBJECTIVES: The objective of this study was to evaluate antidiabetic activity of Chaturmukha rasa based on streptozotocin induced diabetes model, alpha amylase inhibitory activity, alpha Glucosidase inhibitory activity and inhibition of sucrase. METHODS: Chaturmukha rasa was prepared as per Ayurvedic formulary. Antidiabetic activity was measured in experimentally streptozotocin induced rats. The dose was taken as 45 mg/kg, i.p. The antidiabetic activity of Chaturmukha rasa was compared Triphala Kwatha, a marketed formulation. Further In vitro ά-Amylase Inhibitory Assay, In vitro salivary amylase Inhibitory Assay, In vitro α-Glucosidase Inhibitory Assay and In vitro Sucrase Inhibitory Assay was performed with respect to Chaturmukha rasa. The IC50 value was calculated for all the above activity. RESULTS: Streptozotocin with Acarbose showed significant decrease in blood glucose level whereas streptozotocin with Triphala kwatha showed more decrease in blood glucose level than Streptozotocin with Acarbose. The combination of Streptozotocin + Triphala kwatha + Chaturmukha rasa showed a significant decrease in blood glucose level on 21st day. In vitro ά-Amylase Inhibitory Assay the Chaturmukha rasa showed IC50 value 495.94 µl when compared with Acarbose 427.33 µl, respectively. In the α-Glucosidase Inhibitory Assay Chaturmukha rasa showed IC50 value 70.93 µl when compared with Acarbose 102.28 µl, respectively. In vitro Sucrase Inhibitory Assay Chaturmukha rasa showed IC50 value 415.4 µl when compared with Acarbose 371.43 µl, respectively. CONCLUSION: This study supports that Chaturmukha rasa may inhibit diabetes by inhibition of salivary amylase or alpha Glucosidase or sucrase. This may be the mechanism by which Chaturmukha rasa inhibits diabetes. Further this study supports the usage of Chaturmukha rasa for the management of diabetes.

10.
J Biol Chem ; 293(39): 14962-14972, 2018 09 28.
Article in English | MEDLINE | ID: mdl-30104413

ABSTRACT

The genomes of the malaria-causing Plasmodium parasites encode a protein fused of 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase (HPPK) and dihydropteroate synthase (DHPS) domains that catalyze sequential reactions in the folate biosynthetic pathway. Whereas higher organisms derive folate from their diet and lack the enzymes for its synthesis, most eubacteria and a number of lower eukaryotes including malaria parasites synthesize tetrahydrofolate via DHPS. Plasmodium falciparum (Pf) and Plasmodium vivax (Pv) HPPK-DHPSs are currently targets of drugs like sulfadoxine (SDX). The SDX effectiveness as an antimalarial drug is increasingly diminished by the rise and spread of drug-resistant mutations. Here, we present the crystal structure of PvHPPK-DHPS in complex with four substrates/analogs, revealing the bifunctional PvHPPK-DHPS architecture in an unprecedented state of enzymatic activation. SDX's effect on HPPK-DHPS is due to 4-amino benzoic acid (pABA) mimicry, and the PvHPPK-DHPS structure sheds light on the SDX-binding cavity, as well as on mutations that effect SDX potency. We mapped five dominant drug resistance mutations in PvHPPK-DHPS: S382A, A383G, K512E/D, A553G, and V585A, most of which occur individually or in clusters proximal to the pABA-binding site. We found that these resistance mutations subtly alter the intricate enzyme/pABA/SDX interactions such that DHPS affinity for pABA is diminished only moderately, but its affinity for SDX is changed substantially. In conclusion, the PvHPPK-DHPS structure rationalizes and unravels the structural bases for SDX resistance mutations and highlights architectural features in HPPK-DHPSs from malaria parasites that can form the basis for developing next-generation anti-folate agents to combat malaria parasites.


Subject(s)
Dihydropteroate Synthase/chemistry , Diphosphotransferases/chemistry , Malaria, Vivax/drug therapy , Plasmodium vivax/chemistry , Sulfadoxine/chemistry , Amino Acids/chemistry , Amino Acids/genetics , Crystallography, X-Ray , Dihydropteroate Synthase/genetics , Diphosphotransferases/genetics , Drug Resistance/genetics , Humans , Malaria, Vivax/parasitology , Mutation , Plasmodium falciparum , Plasmodium vivax/genetics , Plasmodium vivax/pathogenicity , Sulfadoxine/therapeutic use , Tetrahydrofolates/chemistry
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