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The National Genomics Data Center (NGDC), part of the China National Center for Bioinformation (CNCB), provides a family of database resources to support global academic and industrial communities. With the explosive accumulation of multi-omics data generated at an unprecedented rate, CNCB-NGDC constantly expands and updates core database resources by big data archive, integrative analysis and value-added curation. In the past year, efforts have been devoted to integrating multiple omics data, synthesizing the growing knowledge, developing new resources and upgrading a set of major resources. Particularly, several database resources are newly developed for infectious diseases and microbiology (MPoxVR, KGCoV, ProPan), cancer-trait association (ASCancer Atlas, TWAS Atlas, Brain Catalog, CCAS) as well as tropical plants (TCOD). Importantly, given the global health threat caused by monkeypox virus and SARS-CoV-2, CNCB-NGDC has newly constructed the monkeypox virus resource, along with frequent updates of SARS-CoV-2 genome sequences, variants as well as haplotypes. All the resources and services are publicly accessible at https://ngdc.cncb.ac.cn.

RNase-resistant, noninfectious virus-like particles containing exogenous RNA sequences (armored RNA) are good candidates as RNA controls and standards in RNA virus detection. However, the length of RNA packaged in the virus-like particles with high efficiency is usually less than 500 bases. In this study, we describe a method for producing armored L-RNA. Armored L-RNA is a complex of MS2 bacteriophage coat protein and RNA produced in Escherichia coli by the induction of a two-plasmid coexpression system in which the coat protein and maturase are expressed from one plasmid and the target RNA sequence with modified MS2 stem-loop (pac site) is transcribed from another plasmid. A 3V armored L-RNA of 2,248 bases containing six gene fragmentshepatitis C virus, severe acute respiratory syndrome coronavirus (SARS-CoV1, SARS-CoV2, and SARS-CoV3), avian influenza virus matrix gene (M300), and H5N1 avian influenza virus (HA300)-was successfully expressed by the two-plasmid coexpression system and was demonstrated to have all of the characteristics of armored RNA. We evaluated the 3V armored L-RNA as a calibrator for multiple virus assays. We used the WHO International Standard for HCV RNA (NIBSC 96/790) to calibrate the chimeric armored L-RNA, which was diluted by 10-fold serial dilutions to obtain samples containing 10 6 to 10 2 copies. In conclusion, the approach we used for armored L-RNA preparation is practical and could reduce the labor and cost of quality control in multiplex RNA virus assays. Furthermore, we can assign the chimeric armored RNA with an international unit for quantitative detection.Armored RNA is a complex of MS2 bacteriophage coat protein and RNA produced in Escherichia coli by the induction of an expression plasmid that encodes the bacteriophage sequence consisting of the maturase, the coat protein, the pac site, and an exogenous RNA sequence. This method produces recombinant virus-like particles that are noninfectious and contain predefined RNA (2-6, 8, 11, 12, 15, 16, 28). These armored RNAs are RNase resistant by virtue of their encapsulation within an MS2 coat protein, and they have been widely used as controls, standards, or calibrators for the detection of hepatitis C virus (HCV) (11,12,28), human immune-deficiency virus (11, 15), severe acute respiratory syndrome coronavirus (SARS-CoV) (3, 11), enterovirus (2, 5), avian influenza virus 5 (4), and West Nile virus (6) using reverse transcription-PCR (RT-PCR), real-time RT-PCR, and branched DNA assays (2-6, 11, 12, 15, 28).The MS2 bacteriophage consists of 180 U of the bacteriophage coat protein that encapsulates the bacteriophage genome (25). The MS2 phage RNA genome comprises a single plus-sense strand encoding 3,569 nucleotides. The genes are organized from the 5Ј end as follows: the maturase or A protein, the bacteriophage coat protein, a 75-amino-acid lysis protein, and a replicase subunit. Packaging of the RNA genome by coat protein is initiated by high-specificity binding to a unique site on the RNA, a single stem-loop structure, containi...