https://journals.umt.edu.pk/index.php/BSR/issue/feed 2024-09-24T08:15:07+00:00 Dr. M. Sohail Afzal [email protected] Open Journal Systems <p style="text-align: justify;">BioScientific Review (BSR) is an open-access peer-reviewed journal published on a quarterly basis. It provides a modern and multidisciplinary platform for free and fast publications broadly covering all aspects of life sciences. Research in the field of life sciences has grown at a bewildering pace during the last decade and BSR intends to publish momentous advances in all specialized areas of life sciences and bring them to light.&nbsp;</p> https://journals.umt.edu.pk/index.php/BSR/article/view/5832 2024-09-24T08:15:07+00:00 Nimra Hanif [email protected] Sehrish Arshad [email protected] Aqsa [email protected] Muhammad Asim [email protected] Amna Sadaqat Nadeem [email protected] Tanzeel ur Rehman [email protected] Nimra shafique [email protected] Raees Ahmad khan [email protected] Moeez manzor [email protected]

<p><strong>Background.</strong> <em>Streptococcus</em> <em>pneumoniae</em> is a major human pathogen responsible for serious infections such as pneumonia. Despite extensive research, many proteins in S. <em>pneumoniae</em>, including hypothetical proteins, remain uncharacterized, limiting the understanding of the bacterium's pathogenic mechanisms.</p> <p><strong>Methods. </strong>This study utilizes <em>in silico</em> tools to characterize the hypothetical protein AZJ53_10480 from S. pneumoniae. Sequence alignment and phylogenetic analysis were conducted using BLASTp and ClustalW, while PSIPRED and I-TASSER predicted the protein’s secondary and tertiary structures. Molecular docking studies were performed with AutoDock Vina to assess potential interactions with the antiviral drug sofosbuvir</p> <p><strong>Results. </strong>The <em>in silico</em> analysis revealed that the hypothetical protein AZJ53_10480 shares structural and functional similarities with viral capsid proteins of the hepatitis C virus. The protein was found to have a mixed localization, suggesting potential multifunctionality within the bacterial cell. Molecular docking studies indicated a strong binding affinity between AZJ53_10480 and sofosbuvir, suggesting that this protein could be a potential target for therapeutic intervention.</p> <p><strong>Conclusion. </strong>This study highlights structural properties and functional roles of hypothetical protein AZJ53_10480 in <em>S</em>. <em>pneumoniae</em> of . The findings suggest that AZJ53_10480 may play a role in the pathogenicity of <em>&nbsp;</em>this bacterium and could serve as a novel target for therapeutic development. Further experimental studies are needed to validate these findings and explore the protein's potential as a drug target.</p> <p><strong>Highlights</strong></p> <ul> <li><em>In silico</em> analysis reveals structural similarities between the hypothetical protein AZJ53_10480 and viral capsid proteins.</li> <li>Docking studies suggest AZJ53_10480 as a potential target for antiviral drugs like sofosbuvir.</li> <li>The study provides new insights into the possible pathogenic role of hypothetical proteins in <em>Streptococcus pneumoniae.</em></li> </ul>

2024-09-23T05:54:02+00:00 Copyright (c) 2024 Nimra Hanif, Sehrish Arshad, Aqsa , Muhammad Asim, Amna Sadaqat Nadeem, Tanzeel ur Rehman, Nimra shafique, Raees Ahmad khan, Moeez manzor