Will weather stem the spread of the COVID-19 in Pakistan?

The pandemic of COVID-19 started spreading more exponentially across Pakistan since the end of February 2020. Numerous models and factors have been used to estimate predictions of the prevalence and severity of COVID-19 infections around the globe. While many factors play a role in the spread of COVID-19, climate and weather conditions are considered key elements in the transmission of COVID-19. Many researchers believe that recent increases in COVID-19 cases correlate strongly with local temperatures and factors (such as humidity, weather conditions, etc.) related to it. In this manuscript we test the hypothesis that SARS-CoV-2 spread is temperature-dependent by using the available data derived from Pakistan. The present review focuses on the relationship between temperature and COVID-19, examining the virus's viability and infectivity under various conditions. Our findings indicate that the trough and crest of the COVID-19 wave observed in 2020 are likely to repeat in the summer and winter of 2021, respectively. In Pakistan, temperatures, and humidity significantly affect the COVID-19 transmission and incidence. Like other types of beta-coronaviruses (ß-CoVs), the spread of COVID-19 may depend upon a great deal on temperature.

In silico analysis of Naegleria fowleri cathepsin B paralogs: important drug targets.

Naegleria fowleri is a deadly human pathogen that causes primary amoebic meningoencephalitis (PAM). In this study, in silico investigations of two important N. fowleri cathepsin B paralogs, i.e., copies of genes resulting from a gene duplication event, were carried out using comparative modeling and molecular dynamics (MD) simulations. Comparative models of both paralogs showed significant architectural similarity with their template, i.e., rat cathepsin B. However, in N. fowleri cathepsin B (UniProt ID: X5D761) and putative cathepsin B (UniProt ID: M1HE19) enzymes, eleven and fifteen residues in the occluding loop regions were deleted, respectively, suggesting that these enzymes have a short occluding loop. Thus, it is concluded that N. fowleri cathepsin B and putative cathepsin B enzymes lack exopeptidase activity but possess enhanced endopeptidase activity and an affinity for macromolecular inhibitors. MD simulations further confirmed that prosegments (macromolecular inhibitors) bond more tightly with both enzymes than with wild-type cathepsin B. Additionally, a mutation was identified at an important N-glycosylation site; this mutation is believed to affect cathepsin B targeting inside the cell and make cathepsin B available in the extracellular environment. Due to this important N-glycosylation site mutation, these enzymes are secreted in the extracellular environment via an alternative, still unknown, posttranslational processing strategy. The present study is the first to predict the three-dimensional folds of N. fowleri cathepsin B paralogous enzymes, including a detailed description of the active site architecture and information about propeptide binding mode. This information can contribute to the discovery of novel and selective treatments that are effective against N. fowleri.