I53-50 is a computationally designed, self-assembling protein nanoparticle (NP) that forms a stable icosahedral structure composed of 120 protein subunits coordinated through precise interfacial interactions. Through unique intelligent regulation, I53-50 exhibits sensitivity to environmental signals and display multimodal “nano-smart” properties. I53-50 has a variety of modifiable surface-active sites, which facilitates precise chemical modification, gene fusion, tag coupling, and other functionalizations, thereby promoting effective lymphatic uptake and optimizing the immune response. I53-50 NPs show great potential in vaccine development, drug delivery, and biomaterials, representing a model fusion of computational biology and nanomedicine and offering a versatile tool for precision medicine.

16S rRNA gene amplicon sequencing is the most widely used approach for characterizing microbial communities, yet analyzing such data requires navigating a fragmented landscape of bioinformatics tools with distinct installation requirements, parameter settings, and data formats. Here we present 16S-Pipeline, an open-source, web-based platform that provides a complete workflow from raw FASTQ files to publication-ready statistical analyses. 16S-Pipeline automatically detects sequencing type (paired-end, single-end, long-read), variable region, and sequencing platform (Illumina, PacBio HiFi, Nanopore), then performs quality filtering, primer trimming, amplicon sequence variant (ASV) inference via DADA2, taxonomy assignment against SILVA v138.1, phylogenetic tree construction, and optional functional prediction via PICRUSt2. Downstream analyses include alpha and beta diversity, taxonomic composition visualization, differential abundance testing using five complementary methods (ALDEx2, DESeq2, ANCOM-BC2, LinDA, MaAsLin2) with consensus reporting, and KEGG pathway mapping. Built-in NCBI SRA integration enables downloading public datasets for re-analysis and generates submission metadata spreadsheets for data deposition. The interactive web interface built on FastAPI and Plotly Dash enables researchers to perform complex microbiome analyses without command-line expertise. 16S-Pipeline is freely available at https://github.com/tatsu1207/16S-Pipeline under the MIT License.

Three Gram-stain-negative, strictly aerobic, motile bacterial strains, designated IMCC44359^T, IMCC44632^T, and IMCC44653, were isolated from coastal surface seawater collected near Jangbong Island in the Yellow Sea. Phylogenetic analyses based on 16S rRNA gene and whole-genome sequences assigned the isolates to the genus Aliikangiella. Strains IMCC44632^T and IMCC44653 shared identical 16S rRNA gene sequences and exhibited high genomic relatedness (99.0% average nucleotide identity and 92.0% digital DNA-DNA hybridization), indicating that they represent a single species. In contrast, strain IMCC44359^T showed low genomic relatedness to these strains and to previously validly published Aliikangiella species, supporting its recognition as a distinct species. The genome of IMCC44359^T (5.95 Mbp; 36.5 mol% G + C) is substantially larger than those of IMCC44632^T and IMCC44653 (~3.75 Mbp; 40.1–40.2 mol% G + C), and all genomes encode aerobic chemoorganotrophic metabolism and biochemical capacities consistent with adaptation to marine environments. The isolates grew under mesophilic and moderately halophilic conditions typical of coastal seawater bacteria, with growth occurring at ranges at 10–40℃, pH 6.0–9.0, and 0.5–7.5% NaCl (optimum, 30℃, pH 7.0–8.0, and 2.0–3.0% NaCl). All strains contained ubiquinone-8 (Q-8) as the sole respiratory quinone, and phosphatidylethanolamine, phosphatidylglycerol, and diphosphatidylglycerol were the major polar lipids. The dominant cellular fatty acids were iso-C_15:0 and summed feature 9 (iso-C_17:1 ω9c and/or C_16:0 10-methyl). Integrated phylogenetic, genomic, phenotypic evidence supported the recognition of two novel species within the genus Aliikangiella, for which the names Aliikangiella litoralis sp. nov. (type strain IMCC44359^T = KCTC 18089^T = JCM 37879^T = HNIBRBA19635^T) and Aliikangiella aequoris sp. nov. (type strain IMCC44632^T = KCTC 18090^T = JCM 37880^T = HNIBRBA19636^T) are proposed.

Lymphocystis disease viruses (LCDVs), members of the Lymphocystivirus genus of the Iridoviridae family, infect various freshwater and marine fish species. They cause the chronic disease lymphocystis, which is non-fatal, but substantially reduces the commercial value of the infected fish. To date, four genotypes of LCDV (LCDV1–4) have been identified, all of which encode the viral homologue of B-cell lymphoma 2 (Bcl-2), a key inhibitor of apoptosis. In this study, we performed biochemical and structural analyses of LCDV2 Bcl-2. Binding assays revealed that LCDV2 Bcl-2 exhibits binding selectivity toward BH3 domain-containing zebrafish proteins. It interacted with zBaxA and zNoxa, but not with zBaxB, zBid, or zBeclin 1, distinguishing it from mammalian and herpesviral Bcl-2 proteins. Subsequent structural determination of LCDV2 Bcl-2 in complex with the BH3 domain of zBaxA demonstrated that they interact in a canonical manner, primarily mediated by the BH3 consensus motif residues of zBaxA. In addition, a subpocket formed by two phenylalanine residues in LCDV2 Bcl-2 plays a key role in determining binding selectivity.

Actinobacillus pleuropneumoniae (APP) is the etiological agent of porcine pleuropneumoniae (PP), a high contagious respiratory disease with significant impact on the swine industry in both clinically and economically. Despite of the several attempts to control APP, the emergence of novel serotypes and antimicrobial resistance (AMR) strains highlights the importance of monitoring the genetic characteristics of APP at single nucleotide level. Despite the importance of genomic surveillance of APP to develop effective control strategies, genetic information on the recent Korean isolates of APP is not available at whole genome level. Therefore, in this study, six APP strains were isolated from porcine lungs with characteristic lesions of PP from 2022 to 2024. And their whole genomic sequences, serotypes, virulence factors, and AMR traits were investigated using combined short- and long-read sequencing methods. In silico PCR serotyping identified the isolates as serotype 1, 7, and 15, while one isolate was non-typeable. Multiple AMR genes including Hinf_PBP3_BLA, Ecol_EFTu_PLV, tet(B), tet(O), tetR, sul2, aph(3'')-Ib, aph(6)-Id, and aph(3')-Ia were detected. Also, these genes were located with adjacent to mobile genetic elements, suggesting the possibility of horizontal gene transfer. Phylogenetic comparison with 40 global APP complete genomes, presented that Korean isolates were closely related with China and Switzerland strains. This study provides the whole genome sequences based genetic characterization on the recent Korean isolates of APP, and this study emphasizes that continuous monitoring of APP genomic variation to support effective control of porcine pleuropneumoniae.

Despite the application of H-1 parvovirus as an anticancer drug, the relationship between its specific tropism and oncolytic activity has been unknown. H-1 viral infection induced cytopathic effects in HeLa cells, whereas Kilham rat virus (KRV), similar to H-1 virus, did not. To explore which segments of the viral protein 2 (VP2) capsid protein in the H-1 virus determine susceptibility to human cancer cells, chimeric H-1 viruses with specific gene segments of H-1 VP2 were constructed. Delineation of the VP2 capsid protein revealed a minimum domain (K208–L435 in the H-1 VP2 protein) to determine infectivity in human cancer cells; however, this domain was not sufficient to maintain infectivity. To solve this problem, further construction of chimeric H-1 viruses illustrated the necessity of segments covering both M1-N87 and D104-P206 in the H-1 VP2 protein, based on chimeric H-1 viruses designated as YCH44, YCH45, and YCH46. Both the variable region 4b (VR4b) domains from KRV VP2 and VR8 from H-1 VP2 were required for the same purpose, based on chimeric H-1 viruses designated as YCH-HK8, YCH16, YCH17, YCH18, and YCH19. We confirmed that chimeric viruses carrying these segments infected human lung adenocarcinoma A549 and pancreatic cancer Panc-1 cells, whereas the parental KRV did not. Taken together, these findings indicate that specific domains of the H-1 virus VP2 capsid protein determine infectivity toward human cancer cells.