Mosquito-borne diseases in India over the past 50 years and their Global Public Health Implications: A Systematic Review.

Mosquito-borne diseases (MBDs) pose a significant public health concern globally, and India, with its unique eco-sociodemographic characteristics, is particularly vulnerable to these diseases. This comprehensive review aims to provide an in-depth overview of MBDs in India, emphasizing their impact and potential implications for global health. The article explores distribution, epidemiology, control or elimination, and economic burden of the prevalent diseases such as malaria, dengue, chikungunya, Japanese encephalitis, and lymphatic filariasis, which collectively contribute to millions of cases annually. It sheds light on their profound effects on morbidity, mortality, and socioeconomic burdens and the potential for international transmission through travel and trade. The challenges and perspectives associated with controlling mosquito populations are highlighted, underscoring the importance of effective public health communication for prevention and early detection. The potential for these diseases to spread beyond national borders is recognized, necessitating a holistic approach to address the challenge. A comprehensive literature search was conducted, covering the past five decades (1972-2022), utilizing databases such as Web of Science, PubMed, and Google Scholar, in addition to in-person library consultations. The literature review analyzed 4,082 articles initially identified through various databases. After screening and eligibility assessment, 252 articles were included for analysis. The review focused on malaria, dengue, chikungunya, Japanese encephalitis, and lymphatic filariasis. The included studies focused on MBDs occurrence in India, while those conducted outside India, lacking statistical analysis, or published before 1970 were excluded. This review provides valuable insights into the status of MBDs in India and underscores the need for concerted efforts to combat these diseases on both national and global scales through consilience.

Computational analysis and structure predictions of CHH-related peptides from Litopenaeus vannamei.

The crustaceans produce several related peptides that belong to the crustacean hyperglycemic hormone (CHH) family. While these peptides have similar amino acid sequences, they have diverse biological functions that must arise, in part, from differences in the 3D shape of these peptides. However, it is generally accepted that peptides with a high degree of sequence similarity also have a similar 3-D structure. We used the solution structure of one peptide in the crustacean hyperglycemic hormone family, the molt-inhibiting hormone of the kuruma prawn (Marsupenaeus japonicus), to predict the shape of the five known peptides related to CHH in the Pacific white shrimp, Litopenaeus vannamei. The high similarity of the 3-D structures of these peptides suggests a common fold for the entire family. Nevertheless, minor differences in the shape of these peptides were observed, which may be the basis for their different biological properties.

Computational analysis of the structural basis of ligand binding to the crustacean retinoid X receptor.

Homodimerization of the retinoid X receptor (RXR) occurs upon binding of ligands to the receptor, but little is known about structural mechanisms involved in RXR ligand binding. In the present study, binding of known ligands (5-Hydroxytryptamine, dopamine and naloxone) to the Celuca pugilator RXR was modeled computationally using the human RXR-α as a homology template. Docking scores calculated for these ligands showed reasonably good binding interactions to C. pugilator RXR. Furthermore, RXR is the receptor that mediates the different activities of neurotransmitters and opioid against naloxone in crustaceans and possibly other species. These results indicate that 5-hydroxytryptamine and naloxone might have similar functions. These also results suggest a 3-D model of C. pugilator RXR that describes the binding of ligands at a single RXR receptor binding site and offers further insight into the binding of structurally diverse ligands to this receptor. Further, computational studies showed that crustacean RXRs might be closer to vertebrate RXR than to insect RXR. The predicted binding models for C. pugilator RXR may allow for better design of experimental studies, such as site-directed mutagenesis and affinity labeling studies that may yield valuable information concerning structure-activity relationship studies of RXR and its ligands.