Draft genome sequence of Lactobacillus plantarum strain DMR17 isolated from homemade cow dahi of Sikkim Himalayan region: an evaluation of lactate fermentation and secondary metabolism

Archives of Microbiology - Lactobacillus plantarum DMR17 was isolated from homemade cow dahi of Sikkim Himalayan region of India. Here, we report the draft genome sequence of this strain. A total...     

Signal transducer and activator of transcription-3 mediated neuroprotective effect of interleukin-6 on cobalt chloride mimetic hypoxic cell death in R28 cells

Molecular Biology Reports - Hypoxic injury to retinal ganglionic cells and adjoining glia is implicated in glaucomatous optic neuropathy. The present study evaluates the effect of IL-6 on R28...     

The SARS-CoV-2 Spike protein has a broad tropism for mammalian ACE2 proteins

SARS Coronavirus 2 (SARS-CoV-2) emerged in late 2019, leading to the Coronavirus Disease 2019 (COVID-19) pandemic that continues to cause significant global mortality in human populations. Given its sequence similarity to SARS-CoV, as well as related coronaviruses circulating in bats, SARS-CoV-2 is thought to have originated in Chiroptera species in China. However, whether the virus spread directly to humans or through an intermediate host is currently unclear, as is the potential for this virus to infect companion animals, livestock, and wildlife that could act as viral reservoirs. Using a combination of surrogate entry assays and live virus, we demonstrate that, in addition to human angiotensin-converting enzyme 2 (ACE2), the Spike glycoprotein of SARS-CoV-2 has a broad host tropism for mammalian ACE2 receptors, despite divergence in the amino acids at the Spike receptor binding site on these proteins. Of the 22 different hosts we investigated, ACE2 proteins from dog, cat, and cattle were the most permissive to SARS-CoV-2, while bat and bird ACE2 proteins were the least efficiently used receptors. The absence of a significant tropism for any of the 3 genetically distinct bat ACE2 proteins we examined indicates that SARS-CoV-2 receptor usage likely shifted during zoonotic transmission from bats into people, possibly in an intermediate reservoir. Comparison of SARS-CoV-2 receptor usage to the related coronaviruses SARS-CoV and RaTG13 identified distinct tropisms, with the 2 human viruses being more closely aligned. Finally, using bioinformatics, structural data, and targeted mutagenesis, we identified amino acid residues within the Spike–ACE2 interface, which may have played a pivotal role in the emergence of SARS-CoV-2 in humans. The apparently broad tropism of SARS-CoV-2 at the point of viral entry confirms the potential risk of infection to a wide range of companion animals, livestock, and wildlife.

A study using a combination of surrogate entry assays and live virus suggests that SARS-CoV-2 may have a broad host-range, revealing that the virus''s spike protein can use a broad range of host ACE2 receptors to enter cells and that the sequence of this protein might have changed during the zoonotic jump into humans.     

Studies on catabolite repression in solid state fermentation for biosynthesis of fungal amylases

Catabolite repression by glucose of the biosynthesis of alpha amylase and amyloglucosidase by Aspergillus niger CFTRI 1105 was studied in a solid state fermentation (SSF) and in submerged fermentation (SMF) systems and the results were compared. The addition of glucose did not enhance the production of alpha-amylase and amyloglucosidase in an earlier fermentation system. However, a drastic reduction in alpha-amylase production was observed in submerged fermentation by the addition of 5·0 mg ml⁻¹ glucose and of amyloglucosidase production by 10 mg ml⁻¹ glucose. Glucose concentrations above 50 mg ml⁻¹ completely suppressed the production of both enzymes in the initial hours. In contrast, in the SSF system the repression was negligible, even when the glucose level was raised to 150 mg g⁻¹ wheat bran for both alpha and amyloglucosidase synthesis.     

Interaction of Estrogen Receptor Associated Protein (ERAP) 140 with ER β Decreases but its Expression Increases in Aging Mouse Cerebral Cortex

Following binding to cognate ligand, estrogen receptor (ER) β interacts with specific responsive elements of the target genes and recruits a host of nuclear proteins for hormone dependent gene regulation. However, it is poorly known which proteins interact with ER β in mouse brain and whether their interaction and expression change with age. In this report, we have used his-tag mouse ER β for interaction with nuclear proteins of cerebral cortex of young (6 ± 1 weeks), adult (25 ± 2 weeks), and old (70 ± 5 weeks) female mice. We have identified estrogen receptor-associated protein (ERAP) 140 as one of the interacting proteins and studied its interaction by pull down immunoblotting, far-Western blotting and immunoprecipitation, and expression by western blotting. The data show that ERAP 140 interacts with ER β and its interaction decreases but its expression increases with age in mouse cerebral cortex, suggesting its role in estrogen-mediated brain functions during aging.     

Nucleosome positioning and periodicity of satellite DNA in the liver of aging rats – Nucleosome positioning and periodicity of satellite DNA

The positioning of nucleosomes has been analysed by comparing the pattern of cutting sites of a probing reagent on chromatin and naked DNA. For this purpose, high molecular weight DNA and nuclei from the liver of young (18±2 weeks) and old (100±5 weeks) Wistar male rats were digested with micrococcal nuclease (MNase) and hybridized with ³²P-labelled rat satellite DNA probe. A comparison of the ladder generated by MNase with chromatin and nuclei indicates long range organization of the satellite chromatin fiber with distinct non-random positioning of nucleosomes. However, the positioning of nucleosomes on satellite DNA does not vary with age. For studying the periodicity and subunit structure of satellite DNA, high molecular weight DNA from the liver of young and old rats were digested with different restriction enzymes. Surprisingly, no noteworthy age-related change is visible in the periodicity and subunit structural organization of the satellite DNA. These results suggest that the nucleosome positioning and the periodicity of liver satellite DNA do not vary with age.