Background and Purpose: Klebsiella pneumoniae and Klebsiella oxytoca are the two most common pathogens causing nosocomial infections in humans and are of great concern for developing multidrug resistance. In the present study, K. pneumoniae and K. oxytoca from clinical samples were evaluated for their antibiotic sensitivity patterns against commonly used antibiotics and production of extended-spectrum beta-lactamase (ESBL). Ampicillin, Amoxicillin, Ceftriaxone, Ciprofloxacin, Gentamicin, Nalidixic acid, Tetracycline was 100%, 90%, 45%, 40%, 45%, 25%, 50%, 35% respectively. Multidrug resistance was found more common in K. pneumoniae (56%) than in K. oxytoca (50%). Prevalence rate of ESBL producing Klebsiella was found 45% among which K. pneumoniae (50%) were found more prominent than K. oxytoca (25%). All the ESBL producing Klebsiella isolates were found to be multidrug resistant, showing 100% resistance to Ampicillin, Amoxicillin, Ceftriaxone and Ciprofloxacin. Materials and Methods:

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Herpes simplex virus type 1 (HSV-1) and 2 (HSV-2) cause a variety of infections including oral-facial infections, genital herpes, herpes keratitis, cutaneous infection and so on. To date, FDA-approved licensed HSV vaccine is not available yet. Hence, the study was conducted to identify and characterize an effective epitope based polyvalent vaccine against both types of Herpes Simplex Virus through targeting six viral proteins. The selected proteins were retrieved from viralzone and assessed to design highly antigenic epitopes by binding analyses of the peptides with MHC class-I and class-II molecules, antigenicity screening, transmembrane topology screening, allergenicity and toxicity assessment, population coverage analysis and molecular docking approach. The final vaccine was constructed by the combination of top CTL, HTL and BCL epitopes from each protein along with suitable adjuvant and linkers. Physicochemical and secondary structure analysis, disulfide engineering, molecular dynamic simulation and codon adaptation were further employed to develop a unique multi-epitope peptide vaccine. Docking analysis of the refined vaccine structure with different MHC molecules and human immune TLR-2 receptor demonstrated higher interaction. Complexed structure of the modeled vaccine and TLR-2 showed minimal deformability at molecular level. Moreover, translational potency and microbial expression of the modeled vaccine was analyzed with pET28a(+) vector for E. coli strain strain K12. The study enabled design of a novel chimeric polyvalent vaccine to confer broad range immunity against both HSV serotypes. However, further wet lab based research using model animals are highly recommended to experimentally validate our findings.

This research work was designed to attempt and propose the first report on production and biochemical characterization of fermented tea flower petal decoction or simply tea petal wine. The tea petal decoction and brewer’s yeast or Saccharomyces cerevisiae were co-cultured for fermentation. Antioxidant activity and chromatographic separation of potential candidates were assessed. Primary investigations for qualitative characters on this fermented broth revealed the presence of steroids, tannin, flavonoids, phenol, cardiac glycosides, coumarin, caffeine etc. Our manufactured fermented broth showed high free radical scavenging activity after 2 months of aging. High DPPH scavenging activities were also observed in solvent fractions of acetone, ethanol and methanol. The antioxidant activity, alcohol percentage and other qualities were seen to be gradually increased during aging. Gas chromatography-mass spectrometry analysis revealed the presence of 44 compounds including many potential antioxidant molecules and other bioactive agents. Hopefully, presence of alcohol with medicinally active compounds and antioxidant activity will make it as acceptable as a good wine and tea flower as economically functional. Graphical abstract

Herpes simplex virus type 1 (HSV-1) and 2 (HSV-2) cause a variety of infections including oral-facial infections, genital herpes, herpes keratitis, cutaneous infection and so on. To date, FDA-approved licensed HSV vaccine is not available yet. Hence, the study was conducted to identify and characterize an effective epitope based polyvalent vaccine against both types of Herpes Simplex Virus through targeting six viral proteins. The selected proteins were retrieved from viralzone and assessed to design highly antigenic epitopes by binding analyses of the peptides with MHC class-I and class-II molecules, antigenicity screening, transmembrane topology screening, allergenicity and toxicity assessment, population coverage analysis and molecular docking approach. The final vaccine was constructed by the combination of top CTL, HTL and BCL epitopes from each protein along with suitable adjuvant and linkers. Physicochemical and secondary structure analysis, disulfide engineering, molecular dynamic simulation and codon adaptation were further employed to develop a unique multi-epitope peptide vaccine. Docking analysis of the refined vaccine structure with different MHC molecules and human immune TLR-2 receptor demonstrated higher interaction. Complexed structure of the modeled vaccine and TLR-2 showed minimal deformability at molecular level. Moreover, translational potency and microbial expression of the modeled vaccine was analyzed with pET28a(+) vector for E. coli strain strain K12. The study enabled design of a novel chimeric polyvalent vaccine to confer broad range immunity against both HSV serotypes. However, further wet lab based research using model animals are highly recommended to experimentally validate our findings.

D614G genotype of SARS-CoV-2 virus is highly infectious and responsible for almost all infection for 2 nd wave. However, there are currently no reports with D614G as vaccine candidate. Here we report the development of an mRNA-LNP vaccine with D614G variant and characterization in animal model. We have used special mRNA-architecture and formulation that provides suitable response of the product. The surface plasmon resonance (SPR) data with spike protein (S) revealed that immunization generated specific antibody pools against the whole extracellular domain (RBD and S2) of the spike protein. The anti-sera and purified IgGs from immunized mice neutralized SARS-CoV-2-pseudoviruses in ACE2-expressing HEK293 cells in a dose dependent manner. Importantly, single-dose immunization protected mice-lungs from homotypic-pseudovirus entry and cytopathy. The immunologic responses have been implicated by a balanced and stable population of CD4+ cells with a Th1 bias. The data suggested great promise for immediate translation of the technology to the clinic.

Raksi, a fermented distilled alcoholic beverage, is an ethnic drink consumed in high altitude regions of Singalila Ridge of the Himalayas and in adjoining high altitude places in Nepal, northern and north eastern part of India and Tibetan plateau. Like jaanr, tongba, nigar, chhyang, and other fermented ethnic beverages, raksi is considered as an element of ethnopharmacology of high altitude with claims of medicinal properties. An ethnobiological survey was done in the study area prior to collection and identification of raksi samples. In this research, two raksi samples (khokim raksi and chimphing raksi) of Singalila Ridge of the Himalayas were investigated by metabolite profiling using gas chromatography-mass spectrometry analysis. Results of the experiment showed presence of several respiratory protective, cardioprotective, neuroprotective, anti-inflammatory, and antioxidant components which have properties to prevent various high altitude illnesses. Moreover, large quantities of bioactive terpenoids, fatty acid derivatives, coumarins, and peptides were detected whose chemotaxonomy and biosynthesis pathways were further studied. This metabolomics investigation not only affirmed Raksi as a remedy for high-altitude sickness but also helped in understanding the importance of this type of ethnic foods in high altitude ethnoecology. This research on raksi in the fields of ethnobiology and metabolomics is a cumulative approach which has opened the door for in-depth investigations on similar ethnic foods. However, further experiments on raksi are surely needed in ethnobiology, microbiology, biochemistry, and food technology.

Background and Purpose: Klebsiella pneumoniae and Klebsiella oxytoca are the two most common pathogens causing nosocomial infections in humans and are of great concern for developing multidrug resistance. In the present study, K. pneumoniae and K. oxytoca from clinical samples were evaluated for their antibiotic sensitivity patterns against commonly used antibiotics and production of extended-spectrum beta-lactamase (ESBL). Materials and Methods: The isolates were obtained from tracheal swabs, sputum, wound swabs, pus, blood and urine samples of hospitalized patients. Klebsiella pneumoniae and Klebsiella oxytoca were identified by cultural and biochemical methods. Antibiotic sensitivity test was performed by modified Kirby-Bauer disc diffusion technique. ESBL production in Klebsiella spp. was confirmed by double disc synergy test.Results and Conclusion: Out of 500 clinical isolates, 120 were found positive for Klebsiella among which 108 were K. pneumoniae and 12 were K. oxytoca based on indole test. Prevalence rate of Klebsiella was found more prominent in males aged over 50 years, mostly in urine samples. Overall resistance pattern of Klebsiella isolates to Ampicillin, Amoxicillin, Ceftriaxone, Ciprofloxacin, Co-trimoxazole, Gentamicin, Nalidixic acid, Tetracycline was 100%, 90%, 45%, 40%, 45%, 25%, 50%, 35% respectively. Multidrug resistance was found more common in K. pneumoniae (56%) than in K. oxytoca (50%). Prevalence rate of ESBL producing Klebsiella was found 45% among which K. pneumoniae (50%) were found more prominent than K. oxytoca (25%). All the ESBL producing Klebsiella isolates were found to be multidrug resistant, showing 100% resistance to Ampicillin, Amoxicillin, Ceftriaxone and Ciprofloxacin. Keywords: Multi-drug resistant, Klebsiella, extended-spectrum beta-lactamase.