A5084601890- SARS-CoV-2 and COVID-19 Research
- Mosquito-borne diseases and control
- HIV Research and Treatment
- Vibrio bacteria research studies
- RNA Research and Splicing
- vaccines and immunoinformatics approaches
- Long-Term Effects of COVID-19
- Protein Structure and Dynamics
- Viral Infections and Vectors
- COVID-19 Clinical Research Studies
- Virology and Viral Diseases
- DNA Repair Mechanisms
- Genetics and Neurodevelopmental Disorders
- Immunotherapy and Immune Responses
- Malaria Research and Control
- Endoplasmic Reticulum Stress and Disease
- Ubiquitin and proteasome pathways
- Lipid Membrane Structure and Behavior
- Alzheimer's disease research and treatments
- Viral gastroenteritis research and epidemiology
- Influenza Virus Research Studies
- Essential Oils and Antimicrobial Activity
- Herbal Medicine Research Studies
- Monoclonal and Polyclonal Antibodies Research
- Mitochondrial Function and Pathology
Indian Institute of Technology Mandi
2020-2023
Abstract The phenomenon of protein aggregation is associated with a wide range human diseases. Our knowledge the behaviour viral proteins, however, still rather limited. Here, we investigated this in SARS-CoV and SARS-CoV-2 proteomes. An initial analysis using panel sequence-based predictors suggested presence multiple aggregation-prone regions (APRs) these proteomes revealed strong propensity some proteins. We then studied vitro predicted proteins regions, including signal sequence peptide...
The 26S proteasome is a large (~2.5 MDa) protein complex consisting of at least 33 different subunits and many other components, which form the ubiquitin proteasomal system (UPS), an ATP-dependent degradation in cell. UPS serves as essential component cellular surveillance machinery, its dysfunction leads to cancer, neurodegenerative immunological disorders. Importantly, functions regulations proteins are governed by combination ordered regions, intrinsically disordered regions (IDPRs)...
The ongoing life-threatening pandemic of coronavirus disease 2019 (COVID-19) has extensively affected the world. During this global health crisis, it is fundamentally crucial to find strategies combat SARS-CoV-2. Despite several efforts in direction and continuing clinical trials, no vaccine been approved for yet.To a preventive measure, we have computationally designed multi-epitopic subunit using immuno-informatic approaches.The structural proteins SARS-CoV-2 involved its survival...
Given the COVID-19 pandemic, currently, there are many drugs in clinical trials against this virus. Among excellent drug targets of SARS-CoV-2 its proteases (Nsp3 and Nsp5) that plays vital role polyprotein processing giving rise to functional nonstructural proteins, essential for viral replication survival. Nsp5 (also known as Mpro) hydrolyzes replicase (1ab) at eleven different sites. For targeting Mpro, we have employed repurposing approach identify potential inhibitors a shorter time...
Within 4 months of the ongoing COVID-19 pandemic caused by SARS-CoV-2, more than 250 nucleotide mutations have been detected in ORF1ab virus isolated from infected persons different parts globe. These observations open up an obvious question about rate and direction mutational pressure for further vaccine therapeutics designing. In this study, we did a comparative analysis ORF1a ORF1b using first isolate (Wuhan strain) as parent sequence. We observed that most are C to U transitions. The...
Abstract The phenomenon of protein aggregation is associated with a wide range human diseases. Our knowledge on the behaviour viral proteins, however, still rather limited. Here, we investigated this in SARS-CoV and SARS-CoV-2 proteomes. An initial analysis using panel sequence-based predictors suggested presence multiple aggregation-prone regions these proteomes, revealed an enhanced propensity some proteins. We then studied vitro predicted including signal sequence peptide fusion 1 spike...
Abstract The SARS-CoV-2 envelope protein (E) is involved in a broad spectrum of functions the cycle virus, including assembly, budding, formation, and pathogenesis. To enable these activities, E likely to be capable changing its conformation depending on environmental cues. investigate this issue, here we characterised structural properties C-terminal domain (E-CTD), which has been reported interact with host cell membranes. We first studied E-CTD solution, finding characteristic features...
Viral pathogenesis typically involves numerous molecular mechanisms. Protein aggregation is a relatively unknown characteristic of viruses, despite the fact that viral proteins have been shown to form terminally misfolded forms. Zika virus (ZIKV) neurotropic one with potential cause neurodegeneration. Its protein amyloid may link neurodegenerative component pathogenicity associated infection. Therefore, we investigated in ZIKV proteome as putative pathogenic route and alternate pathways. We...
Introduction The life cycle of a virus involves interacting with the host cell, entry, hijacking machinery for viral replication, evading host's immune system, and releasing mature virions. However, viruses, being small in size, can only harbor genome large enough to code minimal number proteins required replication maturation As result, many are multifunctional machines that do not directly obey classic structure-function paradigm. Often, such multifunctionality is rooted intrinsic disorder...
Abstract The ability of human encoded soluble proteins to convert into amyloid fibrils is now recognized as a generic phenomenon in several illnesses. Typically, such disease causal proteins/peptides consist aggregation-prone regions (APR) that make them susceptible misfolding and assemble highly ordered β-sheet rich fibrils, distinct from their native state. Here, we show the zika virus (ZIKV) consists aggregation prone hotspots spread across its entire proteome. Using combination...
Abstract Flavivirus Non-structural 1 (NS1) protein performs multiple functions such as host immune evasion, interaction with complement system factors, membrane rearrangement, etc. Therefore, it is highly plausible that significant structural and folding dynamics of NS1 might play a role in its multifunctionality. The dimeric structures flaviviruses, including Zika virus (ZIKV), are available. However, domain-wise perspective has not been explored so far. utmost importance to understand the...
A strong association between protein aggregation and human diseases (such as Alzheimer's, Parkinson's, Huntington's disease) is well demonstrated. Misfolding of p53, a central transcriptional mediator, has been revealed by various experimental evidence in different types cancers. Aggregation studies focusing on p53 domains, mostly, the core domain its mutants under influence environmental conditions, transactivation (TAD) (1–63) have reported. However, specific subdomains responsible for are...
Abstract In many cases, when cellular machinery is unable to restore changed protein conformations, they start sticking through exposed hydrophobic patches and form aggregates. A strong association between aggregation Human diseases (such as Alzheimer’s, Parkinson’s, Huntington’s disease) well proven. p53 a transcription factor that also known the guardian of genome associated with processes such DNA repair, apoptosis, senescence, control cell cycle, stress signaling homeostasis. The loss...