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Seasonal outbreaks of febrile illness with eschar have been occurring in Bishnupur district of Manipur since 2001. The aetiology of these outbreaks was unknown. We investigated a similar outbreak in 2007 in order to confirm the aetiology and identify its risk factors. We identified 38 patients who met the case definition (attack rate: 3.4/1000), including two deaths (case fatality ratio = 5.3%). Half of the female patients had eschar on the perineal area. The clinical picture and Weil-Felix positivity suggested that the outbreak was due to scrub typhus. The disease was more common among individuals who defecated or urinated in the jungle or bushy areas from a squatting position. We recommended educating the community about the common symptoms of the disease, encouraging them to seek early treatment from public health facilities and suggested that they be taught to avoid defecating/urinating from a squatting position in the jungle.

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An excessive amount of fat deposition in the body leads to obesity which is a complex disease and poses a generic threat to human health. It increases the risk of various other diseases like diabetes, cardiovascular disease, and multiple types of cancer. Genomic studies have shown that the expression of the fat mass obesity (FTO) gene was highly altered and identified as one of the key biomarkers for obesity. This study has been undertaken to investigate the mutational profile of the FTO gene and elucidates its effect on the protein structure and function. Harmful effects of various missense mutations were predicted using different independent tools and it was observed that all mutations were highly pathogenic. Molecular dynamics (MD) simulations were performed to study the structure and function of FTO protein upon different mutations and it was found that mutations decreased the structure stability and affected protein conformation. Furthermore, a protein residue network analysis suggested that the mutations affected the overall residues bonding and topology. Finally, molecular docking coupled with MD simulation suggested that mutations affected FTO substrate binding by changing the protein-ligand affinity. Hence, the results of this finding would help in an in-depth understanding of the molecular biology of the FTO gene and its variants and lead to the development of effective therapeutics against associated diseases and disorders.