Biology subjects

Kumari, D.

Publications and source records attributed to Kumari, D..

3 recordsLinked to original sources

bioRxiv2022

Human-Sloth Bear (Melursus ursinus) Conflicts in Nawada Forest Division, Nawada, Bihar, India

Sloth bears (Melursus ursinus) are endemic to the Indian subcontinent and frequently come into conflict with human. Both in Rajauli Wildlife Sanctuary (RWLS) and Kauwkol Forest Range (KFR), sand mining operations create heavy noise during the summer for stone crushing which could be the cause of disturbance in the sloth bear territory and sloth bear attacks during the summer and winter. During the study period of 2016 to 2018, a total of 16 sloth bear attacks were incidently reported in various ranges of NFD. There was a marked seasonal variation in human casualties by sloth bear in the study area. Out of 16 cases, highest number of casualties were observed in monsoon (n=8, 50%) as compared to casualties in Summer (n=5, 31.25%) and winter (n=3, 18.75%) season. Most of the attacks were reported during 4.01-8.00 hours (n=6, 37.5%), followed by incidences occurred during evening time, 16.01-20.00 hours (n=4, 25%), 8.01-12.00 hrs (n=3, 18.75%) and 12.01-16.00 (n=2, 12.5%). Moreover, males (n=10) were shown to have a 62 percent attack rate compared to females (n=6; 38 percent). The data also shows that the frequency of attacks on victims engaged in various activities were related to their intensity of usage of specific habitats. It is reported that highest incidences of HSBC occurred when the victims were engaged in NTFP collection (37.5%), followed by victims engaged in walking (25%), farming (18.75%), defection (12.5%) and cattle grazing (6.25%) activities. We recommend education programs among the people to reduce human injury through mitigation techniques.

ecology↗

bioRxiv2022

Restoration of beta-GC trafficking improves the lysosome function in Gaucher disease

Lysosomes function as a primary site for catabolism and cellular signaling. These organelles digest a variety of substrates received through endocytosis, secretion and autophagy with the help of resident acid hydrolases. Lysosomal enzymes are folded in the endoplasmic reticulum (ER) and trafficked to lysosomes via Golgi and endocytic route. The inability of hydrolase trafficking due to mutations or mutations in its receptor or cofactor leads to cargo accumulation (storage) in lysosomes, resulting in lysosome storage disorder (LSD). In Gauchers disease (GD), the lysosomes accumulate glucosylceramide due to a lack of {beta}-glucocerebrosidase ({beta}-GC) activity that causes lysosome enlargement/dysfunction. We hypothesize that improving the trafficking of mutant {beta}-GC to lysosomes may delay the progression of GD. RNAi screen using high throughput based lysosomal enzyme activity assay followed by reporter trafficking assay utilizing {beta}-GC-mCherry lead to the identification of nine potential phosphatases. Depletion of these phosphatases in HeLa cells enhanced the {beta}-GC activity by increasing the folding and trafficking of Gauchers mutants to the lysosomes. Consistently, the lysosomes in primary fibroblasts from GD patients restored their function upon the knockdown of these phosphatases. Thus, these studies provide evidence that altering phosphatome activity possibly delays the GD and forms an alternative therapeutic strategy for this genetic disease. Key pointsO_LIPhosphatome RNAi screen identified both activators and inhibitors of cellular glucocerebrosidase activity C_LIO_LIDepletion of selective phosphatases in HeLa cells improved the folding and trafficking of mutant {beta}-glucocerebrosidase to lysosomes C_LIO_LIKnockdown of selective phosphatases restored the low basal {beta}-glucocerebrosidase activity to that of wild-type in primary cells derived from Gauchers disease patients C_LIO_LIDepletion of selective phosphatases displayed variable {beta}-GC activity in neuropathic and non-neuropathic Gauchers disease patient cells C_LI

cell biology↗

bioRxiv2021

Identification and Characterization of novel mutants of Nsp13 Protein among Indian SARS-CoV-2 isolates.

SARS-CoV-2, the causative agent of COVID-19 has mutated rapidly which enabled them to adapt and evade the immune system of the host. Emerging SARS-CoV-2 variants with crucial mutations pose a global challenge in context of therapeutic drugs and vaccines being developed globally. There are currently no specific therapeutics or vaccines available to combat SARS-CoV-2 devastation. In view of this, the current study aimed to identify and characterize the mutations found in the Nsp13 of SARS-CoV-2 in Indian isolates. Non-structural protein, Nsp13 protein sequences from Indian isolates were analyzed by comparing with the first reported Severe acute respiratory syndrome Corona Virus-2 (SARS-CoV-2) protein sequence from Wuhan, China. Out of 825 Nsp13 protein sequences, a total of 38 mutations were observed among Indian isolates. Our data show that mutations in Nsp13 at various positions (H164Y, A237T, T214I, C309Y, S236I, P419S, V305E, G54S, H290Y, P53S, A308Y, and A308Y) have a significant impact on the proteins stability and flexibility. Also, the impact of Nsp13 mutations on the protein function were predicted based on PROVEAN score that includes 15 mutants as neutral and 23 mutants as deleterious effect. Furthermore, B-cell epitopes contributed by Nsp13 were identified using various predictive immunoinformatic tools. Immunological Parameters of Nsp13 such as antigenicity, allergenicity and toxicity were evaluated to predict the potential B-cell epitopes. The predicted peptide sequences were correlated with the observed mutants. Our predicted data showed that there are seven high rank linear epitopes as well as 18 discontinuous B-cell epitopes based on immunoinformatic tools. Moreover, it was observed that out of total 38 identified mutations among Indian SARS-CoV-2 Nsp13 protein, four mutant residues at position 142 (E142), 245 (H245), 247 (V247) and 419 (P419) are localised in the predicted B cell epitopic region. Altogether, the results of the present in-silico study might help to understand the impact of the identified mutations in Nsp13 protein on its stability, flexibility and function.

bioinformatics↗