Global Change in Interest toward Yoga for Mental Health Ailments during Coronavirus Disease-19 Pandemic: A Google Trend Analysis.

BACKGROUND: With coronavirus disease (COVID)-19 pandemic, society is gripped with uncertainty and fear, inclining them toward Yoga to prevent mental health issues. Google Trends (GT) depicts the public interest of the community which may vary due to evolving policy dynamics of the COVID-19 pandemic. AIM: The aim was to study global public interest in Yoga for mental health during the COVID-19 pandemic. MATERIAL AND METHODS: Global time trends were obtained for Yoga, Anxiety, and Depression from November 1, 2019 to May 31, 2020 using GT. The time series analysis was done in three different time periods - pre-COVID-19 phase, transition period, and COVID-19 pandemic phase. Cross-correlation, Spearman rho, Friedman ANOVA test, and forecasting were used for analysis. RESULTS: GT found a global change in the search queries for Yoga, anxiety, and depression during the three time periods. High burden COVID-19 countries - Italy, Spain, Russia, and Brazil had an increasing search trend for Yoga. During the COVID-19 phase, there was a significant positive correlation between the search trends of Yoga with depression (r = 0.232; P < 0.05) and anxiety (r = 0.351; P < 0.05), but higher anxiety and depression searches lead to lower Yoga searches at lag +6. Forecast projected a continuous increase in Yoga searches and anxiety queries. CONCLUSION: Google Trends captured a significant rise in interest of Yoga among the global community but diminished with time. Hence, the need for interventions to promote Yoga to be part of routine life and for making sure that people adhere to the Yoga practices on a continuous basis.

Truncated Hemoglobin O Carries an Autokinase Activity and Facilitates Adaptation of Mycobacterium tuberculosis Under Hypoxia.

Aims: Although the human pathogen, Mycobacterium tuberculosis (Mtb), is strictly aerobic and requires efficient supply of oxygen, it can survive long stretches of severe hypoxia. The mechanism responsible for this metabolic flexibility is unknown. We have investigated a novel mechanism by which hemoglobin O (HbO), operates and supports its host under oxygen stress. Results: We discovered that the HbO exists in a phospho-bound state in Mtb and remains associated with the cell membrane under hypoxia. Deoxy-HbO carries an autokinase activity that disrupts its dimeric assembly into monomer and facilitates its association with the cell membrane, supporting survival and adaptation of Mtb under low oxygen conditions. Consistent with these observations, deletion of the glbO gene in Mycobacterium bovis bacillus Calmette-Guerin, which is identical to the glbO gene of Mtb, attenuated its survival under hypoxia and complementation of the glbO gene of Mtb rescued this inhibition, but phosphorylation-deficient mutant did not. These results demonstrated that autokinase activity of the HbO modulates its physiological function and plays a vital role in supporting the survival of its host under hypoxia. Innovation and Conclusion: Our study demonstrates that the redox-dependent autokinase activity regulates oligomeric state and membrane association of HbO that generates a reservoir of oxygen in the proximity of respiratory membranes to sustain viability of Mtb under hypoxia. These results thus provide a novel insight into the physiological function of the HbO and demonstrate its pivotal role in supporting the survival and adaptation of Mtb under hypoxia.

Mechanistic insight into the enzymatic reduction of truncated hemoglobin N of Mycobacterium tuberculosis: role of the CD loop and pre-A motif in electron cycling.

Many pathogenic microorganisms have evolved hemoglobin-mediated nitric oxide (NO) detoxification mechanisms, where a globin domain in conjunction with a partner reductase catalyzes the conversion of toxic NO to innocuous nitrate. The truncated hemoglobin HbN of Mycobacterium tuberculosis displays a potent NO dioxygenase activity despite lacking a reductase domain. The mechanism by which HbN recycles itself during NO dioxygenation and the reductase that participates in this process are currently unknown. This study demonstrates that the NADH-ferredoxin/flavodoxin system is a fairly efficient partner for electron transfer to HbN with an observed reduction rate of 6.2 µM/min(-1), which is nearly 3- and 5-fold faster than reported for Vitreoscilla hemoglobin and myoglobin, respectively. Structural docking of the HbN with Escherichia coli NADH-flavodoxin reductase (FdR) together with site-directed mutagenesis revealed that the CD loop of the HbN forms contacts with the reductase, and that Gly(48) may have a vital role. The donor to acceptor electron coupling parameters calculated using the semiempirical pathway method amounts to an average of about 6.4 10(-5) eV, which is lower than the value obtained for E. coli flavoHb (8.0 10(-4) eV), but still supports the feasibility of an efficient electron transfer. The deletion of Pre-A abrogated the heme iron reduction by FdR in the HbN, thus signifying its involvement during intermolecular interactions of the HbN and FdR. The present study, thus, unravels a novel role of the CD loop and Pre-A motif in assisting the interactions of the HbN with the reductase and the electron cycling, which may be vital for its NO-scavenging function.