bioRxiv ScienceSearch

Biology subjects

Satpathy, S.

Publications and source records attributed to Satpathy, S..

3 recordsLinked to original sources

Isolation and molecular identification of pectinase producing Aspergillus species from different soil samples of Bhubaneswar regions

With the significant improvement of human civilization there is a spur in the urban, rural and industrial development, which has a profound effect on the surrounding natural environment. Increased utilization of natural resources is often associated with accumulation of waste materials whose management is crucial for sustainable development of life. Availability of different microorganisms in the soil facilitates the degradation of wastes through their potential enzymatic activities. Pectinase seems to be one of the important enzymes produced by a wide variety of microorganisms contained in the soil. It is mainly involved in maceration and rotting of plant extracts and debris by hydrolysis of 1,4-alpha glycosidic bonds of de-esterified pectate of plant call wall. In this paper we report molecular identification of some pectinase producing Aspergillus species selected from soil samples of five different zones of Bhubaneswar city using molecular biology and computational techniques. Among fifteen fungal isolates studied from these five zones Aspergillus parvisclerotigenus was potent for pectinase production next to Aspergillus niger in form of halozone of 0.6 mm. Its 28S rDNA sequence also had some significant identity (>90%) with different subspecies of Aspergillus. We hope that our findings will helpful in genetic manipulation for improvement of fungal strains of isolates. Again large scale use of the improved Aspergillus strains can degrade plant biomass & diverse industrial wastes which will reduce environmental pollution of capital urban like Bhubaneswar.

microbiology

Microscaled Proteogenomic Methods for Precision Oncology

Cancer proteogenomics integrates genomics, transcriptomics and mass spectrometry (MS)-based proteomics to gain insights into cancer biology and treatment efficacy. A proteogenomics approach was therefore developed for frozen core biopsies using tissue-sparing specimen processing with a \"microscaled\" proteomics workflow. For technical proof-of-principle, biopsies from ERBB2 positive breast cancers before and 48-72 hours after the first dose of neoadjuvant trastuzumab-based chemotherapy were analyzed. ERBB2 protein and phosphosite levels, as well as mTOR target phosphosites, were significantly more suppressed upon treatment in cases associated with pathological complete response, suggesting MS-based pharmacodynamics is achievable. Furthermore, integrated analyses indicated potential causes of treatment resistance including the absence of ERBB2 amplification (false-ERBB2 positive) and insufficient ERBB2 activity for therapeutic sensitivity despite ERBB2 amplification (pseudo-ERBB2 positive). Candidate resistance features in true-ERBB2+ cases, including androgen receptor signaling, mucin expression and an inactive immune microenvironment were observed. Thus, proteogenomic analysis of needle core biopsies is feasible and clinical utility should be investigated.

cancer biology

UbiFast, a rapid and deep-scale ubiquitylation profiling approach for biology and translational research

Protein ubiquitylation is involved in a plethora of cellular processes. Defects in the ubiquitin system are at the root of many acquired and hereditary diseases. While antibodies directed at ubiquitin remnants (K-{varepsilon}-GG) have improved the ability to monitor ubiquitylation using mass spectrometry, methods for highly-multiplexed measurement of ubiquitylation in tissues and primary cells using sub-milligram amounts of sample remains a challenge. Here we present a highly-sensitive, rapid and multiplexed protocol for quantifying [~]10,000 ubiquitylation sites from as little as 500 ug peptide per sample from cells or tissue in a TMT10 plex in ca. 5 hr. High-field Asymmetric Ion Mobility Spectrometry (FAIMS) is used to improve quantitative accuracy for posttranslational modification analysis. We use the approach to rediscover substrates of the E3 ligase targeting drug lenalidomide and to identify proteins modulated by ubiquitylation in models of basal and luminal human breast cancer. The sensitivity and speed of the UbiFast method makes it suitable for large-scale studies in primary tissue samples.

biochemistry