Biology subjects

Batchu, U. R.

Publications and source records attributed to Batchu, U. R..

3 recordsLinked to original sources

bioRxiv2025

Draft Genome Analysis of Streptomyces sp. IICT-RSP475: Unveiling Novel Biosynthetic Potential

Streptomyces species are ubiquitous bacteria renowned for their prolific production of pharmaceuticals and therapeutic agents. In this study, we explored the draft genome of a novel Streptomyces species, Streptomyces sp. IICT-RSP475, isolated from Talakona, Tirupati, using next-generation sequencing and bioinformatics tools. The draft genome of Streptomyces sp. IICT-RSP475 consists of 4,550,481 base pairs (bp) with a high GC content of >70%. Genome analysis identified 18 biosynthetic gene clusters (BGCs) responsible for the production of ribosomally synthesized and post-translationally modified peptides (RiPPs), polyketide synthases (PKS), non-ribosomal peptide synthetases (NRPS), and other secondary metabolites, including hydrogen cyanide, terpenes, and N1-siderophores. Notably, genome mining using the antiSMASH tool uncovered two novel BGCs classified as RiPP-like clusters. These clusters exhibited unique genetic architectures with previously uncharacterized biosynthetic genes, suggesting the presence of novel bioactive metabolites. Ribotyping analysis, further supported by TYGS (Type Strain Genome Server) and ribosomal MLST (Multilocus Sequence Typing), confirmed the classification of this strain as a novel Streptomyces species. These findings highlight the genomic potential of Streptomyces sp. IICT-RSP475 and warrant further investigation into the expression, structural elucidation, and functional characterization of its novel therapeutic metabolites.

microbiology↗

bioRxiv2024

Draft genome analysis of Delftia tsuruhatensis IICT-RSP4, a strain with uricase potential isolated from soil

Delftia tsuruhatensis IICT-RSP4, an uricase producing bacterium was isolated using i-chip method from soil and characterized. Here, we report the draft genome sequence of D. tsuruhatensis IICT-RSP4. The genome data comprised of 6,627,718bp (6.6 MB) with a GC content of 66.6% with 7 protein encoding genes, 346 sub-systems with 6165 coding sequences and 112 RNAs. The genome revealed five functional secondary metabolite biosynthetic gene clusters viz. terpene, resorcinol, NRP+PKS, T2PKS, and RiPPS related to antimicrobial, anticancer and antimalarial functionality. In vitro, screening studies revealed the uricase potential of the strain D. tsuruhatensis IICT-RSP4. This is the first report on the whole genome sequence of an uricase-producing D. tsuruhatensis IICT-RSP4.

bioinformatics↗

bioRxiv2023

Inhibition of Xanthine oxidase by 1-O-methyl chrysophanol, a hydroxyanthraquinone isolated from Amycolatopsis thermoflava ICTA 103.

Hyperuricemia caused by elevated levels of serum uric acid is responsible for implication of gout and other associated disorders that influence the human health. So far, Xanthine oxidase (XO) inhibitors are the choice of first line drugs for the treatment of hyperuricemia. The objective of the present study was to isolate a potent XO inhibitor from the actinobacteria and to evaluate its inhibitory mechanism. Initially, XO was isolated from bovine milk using standard protocol and enzyme kinetics were evaluated. Thereafter, culture filtrates of actinobacteria (Amycolatopsis thermoflava ICTA 103), Streptomyces luteireticuli ICTA 16, Streptomyces kurssanovii ICTA165 and Amycolatopsis lurida ICTA 194) were screened for XO inhibition using in vitro qualitative NBT plate assay followed by extraction and purification of potent inhibitor 1-O-methyl chrysophanol (OMC), from the culture filtrate of Amycolatopsis thermoflava ICTA 103, which belongs to hydroxy anthraquinones (HAQ) family. Further, in silico molecular model building was performed to study the binding affinity of OMC towards XO followed by quantitative in vitro spectroscopic assays. The molecular building study explored the mechanistic view of binding interaction between inhibitor & enzyme and the results were corroborates with the in vitro kinetic study. The in vitro results revealed the significant enzyme inhibition potential of OMC with an IC50 and Ki value of 24.8 {+/-} 0.072 {micro}M & 2.218 {+/-} 0.3068 {micro}M respectively. These results are comparable to standard allopurinol, however, more significant than its structural analog, chrysophanol. The kinetic analysis revealed that OMC is a reversible slow binding inhibitor and the Lineweaver - Burkplot analysis showed mixed type inhibition of OMC against XO. These results are in agreement with chrysophanol. Findings of this study proposed a new derivative of HAQ in the pipeline of hyperuricemia therapeutic drug candidates.

biochemistry↗