Objective: This study analyzed the phylogenetics and diversity of antibiotic resistance genes (ARGs) and molecularly identified the source of ARGs in antibiotic-resistant Escherichia coli isolated from pig farms in Banten Province, Indonesia. Methods: Forty-four antibiotic-resistant E. coli isolates from fecal samples from 44 pig farms in Banten Province, Indonesia, were used as samples. The samples were categorized into 14 clusters. Sequencing was performed using the Oxford Nanopore Technologies MinION platform, with barcoding before sequencing with Nanopore Rapid sequencing gDNAbarcoding (SQK-RBK110.96) according to manufacturing procedures. ARG detection was conducted using ResFinder, and the plasmid replicon was determined using PlasmidFinder. Results: Three phylogenetic leaves of E. coli were identified in the pig farming cluster in Banten Province. The E. coli isolates exhibited potential resistance to nine classes of antibiotics. Fiftyone ARGs were identified across all isolates, with each cluster carrying a minimum of 10 ARGs. The ant(3'')-Ia and qnrS1 genes were present in all isolates. ARGs in the E. coli pig farming cluster originated mainly from plasmids, accounting for an average of 89.4%. Conclusions and Relevance: The elevated potential for MDR events, coupled with the dominance of ARGs originating from plasmids, increases the risk of ARG spread among bacterial populations in animals, humans, and the environment.

Objective To characterize proteins and other nutrients in striatin (DLBS0333), a bioactive protein fraction isolated from snakehead fish (Channa striata) and to investigate its wound healing activity. Methods Proteins and other constituents in striatin were characterized by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, two dimension electrophoresis, immunoblotting assay, spectroscopy and high performance liquid chromatography. The wound healing activity of striatin was studied in vitro using 3T3 fibroblast cells and in vivo using wound-induced animal model. Various parameters related to wound healing process were evaluated. Results Striatin contained four major bioactive proteins with approximate molecular weight of 8.3, 10.9, 15.4 and 16.7 kDa. In addition to proteins, striatin also contained amino acids (10 essential and 7 non essential amino acids), fatty acids (palmitic acid, oleic acid, stearic acid, linoleic acid, arachidonic acid), vitamins (vitamin A, vitamin B