Bioprocessing of recombinant proteins from Escherichia coli inclusion bodies: insights from structure-function relationship for novel applications.

The formation of inclusion bodies (IBs) during expression of recombinant therapeutic proteins using E. coli is a significant hurdle in producing high-quality, safe, and efficacious medicines. The improved understanding of the structure-function relationship of the IBs has resulted in the development of novel biotechnologies that have streamlined the isolation, solubilization, refolding, and purification of the active functional proteins from the bacterial IBs. Together, this overall effort promises to radically improve the scope of experimental biology of therapeutic protein production and expand new prospects in IBs usage. Notably, the IBs are increasingly used for applications in more pristine areas such as drug delivery and material sciences. In this review, we intend to provide a comprehensive picture of the bio-processing of bacterial IBs, including assessing critical gaps that still need to be addressed and potential solutions to overcome them. We expect this review to be a useful resource for those working in the area of protein refolding and therapeutic protein production.

Analysis of predicted amino acid biosynthesis in Rv3344c in Mycobacterium tuberculosis H37 Rv using bioinformatics tools.

According to World Health Organization (WHO) report, Mycobacterium tuberculosis H37 Rv (M. tuberculosis) affects one-third population of the world. Emergence of effective treatment/research against this disease is need of the hour. Therefore, we present some important aspects of Rv3344c, which is a PE_PGRS protein. Evidence shows that PE_PGRS proteins show fibronectin binding activity. This protein has affinity for calcium and also shows motifs of GTP-binding protein. It also shows the presence of sites for ribose-5-phosphate binding and motifs of aspartate-beta-semialdehyde dehydrogenase, both of which are involved in amino acid biosynthesis. Thus, this protein might be targeted to block the amino acid biosynthesis in M. tuberculosis. This article takes into consideration some important aspects of Rv3344c protein as its function is still unknown. This study includes retrieval of protein sequence database, multiple sequence alignment, protein-protein interaction, epitope prediction, localization, function prediction, phosphorylation site prediction, model building and its validation, ligand-binding prediction along with mutational analysis. Hence, this study might be an important step in the development of new drugs and treatment of tuberculosis.