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Fasting
Published in Mehwish Iqbal, Complementary and Alternative Medicinal Approaches for Enhancing Immunity, 2023
The possible immune-dodging process of severe acute respiratory syndrome coronavirus 2, which includes viral protein ORF3a-arbitrated continuous stimulation of NLRP3 (NLR family pyrin domain containing 3), can also be regulated by intermittent fasting. Throughout intermittent fasting, conventional metabolism of energy shifts ideally towards the catabolism of fat and the synthesis of ketone bodies as immediate energy sources. The BHB (β-hydroxybutyrate), a significant ketone body that nourishes many vital organs throughout starvation and/or fasting, may also aid in alleviating inflammation by obstructing the over-stimulation of NLRP3. As obvious in investigational models, β-hydroxybutyrate decreased the synthesis of interleukin-1 beta and interleukin-18 arbitrated by inflammasome NLRP3 in monocytes of humans and repressed stimulation of interleukin-1β and caspase-1 synthesis in rodents (Hannan et al., 2020).
Coronavirus Epidemics and the Current COVID-19 Pandemic
Published in Debmalya Barh, Kenneth Lundstrom, COVID-19, 2022
Aparna Bhardwaj, Prateek Kumar, Shivani Krishna Kapuganti, Vladimir N. Uversky, Rajanish Giri
The structural and accessory proteins are translation products of ~10 kb from the 3′ end one-third of the genome. The genes of these proteins are interspersed along the genome. As mentioned earlier, the structural proteins of SARS-CoV-2 are the S, E, M, and N proteins, and the ORFs code for accessory proteins ORF3a, ORF6, ORF7a, ORF8, ORF9, and ORF10, which are involved in the pathogenesis of the virus [40]. The structural proteins play crucial roles in pathogenesis, replication, viral packaging, and assembly [26]. Docking studies have shown that all four structural proteins interact with each other during their arrangement in the lipid bilayer [41]. The crystal structures of proteins from SARS-CoV and SARS-CoV-2 are presented in Figure 1.3.
Modes of Transmission of Coronavirus
Published in Ram Shringar Raw, Vishal Jain, Sanjoy Das, Meenakshi Sharma, Pandemic Detection and Analysis Through Smart Computing Technologies, 2022
Mohd. Faiz Saifi, Colin E. Evans, Neha Gupta
Severe acute respiratory syndrome (SARS) is a dreadful disease caused by the CoVs, namely SARS-CoV and is characterized by some specific symptoms such as headache, extreme fever, and many severe symptoms of the respiratory tract such as short breath, pneumonia, and dry cough [61]. The pathogenic CoVs can infect humans and livestock such as mice, bats, and birds at various sites such as the gastrointestinal, respiratory, hepatic, and central nervous systems. Previously SARS-CoV belongs to the group of 2b (gene) CoV and now it is a member of lineage B of genus ß coronavirus belonging to the family of Coronaviridae and subfamily Coronavirinae [61]. The genome of SARS-CoV shares similarity to other coronaviruses, but have some specific unique genes including 3b, ORF3a, ORF7a, ORFa, 7b, ORF 8a, 8b, and 9b. Importantly, SARS-CoV interacts with the ACE-2 receptor of the host cell to infect bronchial epithelial cells and type II pneumocytes in the host. A recent spillover or outbreak of CoV strain (COVID-19) in China, in 2019, has gained attention all over the world, as continuous evolution and transformation led to the emergence of pandemic all over the world [62].
Recent trends in next generation immunoinformatics harnessed for universal coronavirus vaccine design
Published in Pathogens and Global Health, 2023
Chin Peng Lim, Boon Hui Kok, Hui Ting Lim, Candy Chuah, Badarulhisam Abdul Rahman, Abu Bakar Abdul Majeed, Michelle Wykes, Chiuan Herng Leow, Chiuan Yee Leow
Other proteins chosen for vaccine development includes 3CL hydrolase, nsp1, ORF3a protein and ORF7a protein. 3CL hydrolase is vital for proteolytic maturation of the virus. Short peptides were extracted from this protein as potential epitopes for both CTLs and HTLs in the design of a multiepitope vaccine [88]. The nsp1 may be a major virulence factor for coronaviruses as seen from its functions. It blocks host gene expression by preventing the translation involving 40S ribosomal subunit as well as degrades mRNA of the host cells. In infected cells, the expression of the IFN genes and the host antiviral signalling pathways were impeded [89]. E protein, ORF3a protein, N protein, ORF7a protein and M protein showed a remarkable linkage with the structural integrity and functionality of the virus [90]. ORF3a protein, N protein and M protein are important in the virus replication and function [91]. Figure 1 illustrates the open reading frames (ORFs) in coronavirus genome and a schematic coronavirus structure labelled with structural proteins.
Human bronchial-pulmonary proteomics in coronavirus disease 2019 (COVID-19) pandemic: applications and implications
Published in Expert Review of Proteomics, 2021
Heng Wee Tan, Yan-Ming Xu, Andy T. Y. Lau
Genes encoding for the coronavirus accessory proteins are dispersed in between (and sometimes overlapping) the structural genes [87]. These accessory proteins are poorly characterized structurally, and their exact functions remain largely mysterious – it is postulated that they may play a role in viral pathogenesis, evolution, and adaptation to the human host [87]. Some of these accessory proteins (e.g. ORF3a, ORF6, and ORF9b) are conserved in SARS-CoV-2 and SARS-CoV, while others appear to be species-specific. For example, ORF10 proteins are found in the proteome of SARS-CoV-2 and animal coronaviruses including pangolin and bat, but not in the SARS-CoV [88]. Interestingly, ORF10 of pangolin-coronaviruses showed 97.3–99.2% sequence similarity to SARS-CoV-2 ORF10, but their ORF10 proteins are expected to have very different physicochemical, structural, and immunological properties [88,89]. The pangolin is the suspected intermediate host of SARS-CoV-2. Therefore, based on the peptide signatures obtained from the main structural proteins of SARS-CoV-2 and other coronaviruses, researchers are able to detect and track the origin of SARS-CoV-2. For example, using a MS/MS proteomics approach, Gouveia et al. [90] identified a shortlist of 14 peptides that can be used for the detection of SARS-CoV-2 based on their species-specificity and other characteristics. In another study, a MS-based assay was established to detect the nucleoprotein peptides of SARS-CoV-2 directly from suspected COVID-19 patients [91].
The blood-gas barrier in COVID-19: an overview of the effects of SARS-CoV-2 infection on the alveolar epithelial and endothelial cells of the lung
Published in Tissue Barriers, 2021
Pyroptosis is an inflammatory type of caspase-mediated programmed cell death associated with the disruption of plasma membrane and release of cellular contents that can prompt an acute inflammatory response through the activation and recruitment of neutrophils45 that secrete the pro-inflammatory IL-1β and HMGB1. Increased levels of HMGB1 were indicated to trigger pyroptosis in bronchial epithelial cells42; hence, it can be argued that AECs could also be affected by HMGB1 and undergo pyroptosis46. Unlike the AECs, there is solid evidence regarding the caspase-1-mediated pyroptotic effect of HMGB1 on ECs in Kawasaki disease47. Importantly, Kawasaki-like disease was reported in a number of pediatric cases of COVID-1948. The pyroptosis associated with COVID-19 is mostly regulated by the expression of SARS-CoV-2 S-RBD, Env and ORF3a genes, which code for the receptor-binding domain of S protein, E protein and ORF3a protein, respectively. The latter is involved in the replication of SARS-CoV-2. Transfection of human bronchial cells with S-RBD and ORF3a primers was demonstrated to incite pyroptosis accompanied by elevated extracellular levels of HMGB1, hence, the positive feedback loop between SARS-CoV-2-induced pyroptosis and HMGB142 (Figure 1).