Journal of biotechnology最新文献

{"title":"High-throughput flow cytometry-based titration of a live attenuated rotavirus vaccine","authors":"Mafalda M. Dias ,&nbsp;Sofia B. Carvalho ,&nbsp;Jean-Philippe Matheise ,&nbsp;Guillaume Van Beersel ,&nbsp;Isabelle Knott ,&nbsp;Patrícia Gomes-Alves ,&nbsp;Paula M. Alves","doi":"10.1016/j.jbiotec.2025.07.004","DOIUrl":"10.1016/j.jbiotec.2025.07.004","url":null,"abstract":"<div><div>Vaccine potency is a critical quality attribute to ensure vaccine’s safety and efficacy. The standard potency assay for vaccines is the traditional cell culture infectious dose 50 % (CCID₅₀). However, this method often yields highly variable results, presenting low sensitivity and requiring a lengthy analysis. Here, we report a flow cytometry-based method for potency assessment of the Rotarix rotavirus vaccine. This method quantifies infected cells by detecting VP7 viral protein in MA104 cells, integrating fluorescence-automated cell counting with a high-throughput system. Determination of adequate cell seeding timepoint, target cell concentration and endpoint after infection are key parameters for the precision, robustness, and accuracy of titer determination. We established optimized assay conditions for lyophilized and final vaccine formulations. Data from both workflows are in line with the CCID₅₀ range of concentrations. The coefficient of variation for inter- and intra-assay for both formulations is ≈ 2 %. Moreover, the flow cytometry method reduced the hands-on and analysis time by at least 4 days, offering a rapid high-throughput alternative tool to streamline the challenges associated with potency testing for viral-based vaccines, impacting therapeutics time to market.</div></div>","PeriodicalId":15153,"journal":{"name":"Journal of biotechnology","volume":"406 ","pages":"Pages 91-98"},"PeriodicalIF":4.1,"publicationDate":"2025-07-03","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144567470","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Improved methanol utilization of Komagataella phaffii by rebuilding metabolic network based on new alcohol-aldehyde transformation system","authors":"Kang Li ,&nbsp;Xiuxia Liu ,&nbsp;Chunli Liu ,&nbsp;Zhonghu Bai ,&nbsp;Shaojie Yang ,&nbsp;Yankun Yang","doi":"10.1016/j.jbiotec.2025.06.013","DOIUrl":"10.1016/j.jbiotec.2025.06.013","url":null,"abstract":"<div><div>Bioconversion based on methanol holds promise for advancing global carbon neutrality and mitigating the global food crisis. However, the limited efficiency of methanol utilization hampers methanol-based biomanufacturing in microorganisms. This study focuses on enhancing methanol utilization efficiency in <em>Komagataella phaffii</em> through the implementation of a novel alcohol-aldehyde conversion system based on the Adh900 protein. Results indicate a notable 14 % increase in biomass compared to the wild-type strain. Furthermore, analysis of the amino acid metabolism pathway underscores the significance of histidine in facilitating the methanol utilization pathway (MUTP). By combination of adding 120 mg/L histidine to the medium and optimizing promoter strategies, the dry cell weight (DCW) was up to 4.33 g DCW/L, which was increased by 63 %. The combination of these strategies has important research significance for methanol-based biological metabolism, and will further promote the microbial application of methanol. These findings are poised to advance the development of methanol-nutritive cell factories, thereby propelling the evolution of methanol biomanufacturing technology.</div></div>","PeriodicalId":15153,"journal":{"name":"Journal of biotechnology","volume":"406 ","pages":"Pages 60-70"},"PeriodicalIF":4.1,"publicationDate":"2025-07-02","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144557586","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Characterisation of chikungunya virus neutralising monoclonal antibodies expressed in tobacco plants","authors":"Catherine M. Moore ,&nbsp;Mathew J. Paul ,&nbsp;Elizabeth Pinneh ,&nbsp;Balamurugan Shanmugaraj ,&nbsp;James Ashall ,&nbsp;Sathishkumar Ramalingam ,&nbsp;Roger Hewson ,&nbsp;Michael S. Diamond ,&nbsp;Julie M. Fox ,&nbsp;Julian K.-C. Ma","doi":"10.1016/j.jbiotec.2025.06.014","DOIUrl":"10.1016/j.jbiotec.2025.06.014","url":null,"abstract":"<div><div>Chikungunya virus (CHIKV) causes a debilitating musculoskeletal disease, characterised by flu-like symptoms, rash, and severe joint pain, which can last for months, even after the resolution of infection. Although the first CHIKV vaccine was approved in the USA in 2023 for use in adults, there is currently no specific antiviral therapy for infection. While neutralising antibody-based prophylactic and therapeutic agents have been considered, affordability and accessibility are major barriers to global regions where Chikungunya disease is epidemic. Here, we expressed five anti-CHIKV neutralising IgG monoclonal antibodies (mAbs) in <em>N. benthamiana</em> plants to investigate the potential use of this manufacturing platform. Plants produced IgG mAbs that compared favourably to mammalian cell-expressed antibodies, including for binding kinetics to CHIKV antigens and neutralisation activity. The yields of mAbs from plants were variable, as three of the antibodies’ yields would need further expression optimisation to warrant future development. The successful expression of these antibodies in <em>N. benthamiana</em> plants supports the growing pipeline of Global Health product targets that could be developed using a highly transferable, low-cost, low-tech plant production platform in resource-poor countries.</div></div>","PeriodicalId":15153,"journal":{"name":"Journal of biotechnology","volume":"406 ","pages":"Pages 53-59"},"PeriodicalIF":4.1,"publicationDate":"2025-07-02","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144557574","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Enhanced cascade biosynthesis of D-phenyllactic acid using metal-organic framework-encapsulated co-expressing E. coli","authors":"Xi Luo ,&nbsp;Yufeng Zhou ,&nbsp;Yaping Yang ,&nbsp;Gaowei Hu ,&nbsp;Fengwei Yin ,&nbsp;Longfei Yin ,&nbsp;Yingying Zhang ,&nbsp;Yongqian Fu","doi":"10.1016/j.jbiotec.2025.06.015","DOIUrl":"10.1016/j.jbiotec.2025.06.015","url":null,"abstract":"<div><div>Phenylpyruvic acid, as a versatile organic acid, has attracted widespread attention in the fields of food, feed, pharmaceuticals, and cosmetics for its synthetic methods. In this study, we co-expressed L-amino acid oxidase, D-lactate dehydrogenase, and glucose dehydrogenase in <em>Escherichia coli</em>. The resulting recombinant whole-cell biocatalysts exhibited high efficiency in the cascade enzymatic synthesis of D-phenyllactic acid from L-phenylalanine. However, their limitations in operational stability and reusability have impeded their broader application. To address this issue, the co-expressing bacteria was immobilized on the metal-organic framework (MOF) ZIF-90. The encapsulation rate of the immobilized <em>E</em>. <em>coli</em> cells (<em>E</em>. <em>coli</em>@ZIF-90) and the recovery rate of their catalytic activity were 94.8 % and 92.7 %, respectively. The physical and biochemical properties of the <em>E</em>. <em>coli</em>@ZIF-90 were subsequently studied in detail. Compared with free cells, <em>E</em>. <em>coli</em>@ZIF-90 demonstrates superior stability under acidic and alkaline conditions, enhanced thermal stability, and increased tolerance to metal ions and organic reagents. After storage at 4°C for 8 days, the residual enzyme activity of the immobilized cells is still over 75 %, which is about 1.7 times that of free cells. Following 10 cycles of biocatalytic reactions, the immobilized cells maintained over 80 % of their enzyme activity, contrasting with the 58.6 % residual activity observed in free cells. In the enzyme cascade reaction catalyzed by <em>E</em>. <em>coli</em>@ZIF-90, 25 g·l⁻¹ L-PHE was completely reacted to produce D-PLA 17.8 g·l⁻¹, with an enantiomeric excess (<em>e</em>.<em>e</em>.) greater than 99.5 %. This study provides a promising method for obtaining efficient and robust biocatalysts for the biosynthesis of D-PLA. Additionally, it provides essential insights that are extendable to the synthesis of a broader range of compounds.</div></div>","PeriodicalId":15153,"journal":{"name":"Journal of biotechnology","volume":"406 ","pages":"Pages 71-81"},"PeriodicalIF":4.1,"publicationDate":"2025-07-02","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144564832","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Integrative in-silico models for mammalian cell cultures in single-use bioreactors: Bridging hydrodynamics, kinetics, and process control across scales","authors":"Aparajita Dasgupta ,&nbsp;John Thomas ,&nbsp;Alaina Anand ,&nbsp;Brian DeVincentis ,&nbsp;Madelynn McCahill ,&nbsp;Aishwarya Sood ,&nbsp;Jonathan Kinross ,&nbsp;Aravindan Rajendran","doi":"10.1016/j.jbiotec.2025.06.012","DOIUrl":"10.1016/j.jbiotec.2025.06.012","url":null,"abstract":"<div><div>This study presents a novel hybrid computational fluid dynamics (CFD) model that integrates hydrodynamics, kinetics, and auxiliary control systems for a mammalian bioprocess across scales. The CFD model simulates the entire 14-day bioprocess at three different scales (250 mL, 1000 L, and 2000 L). The combination of hydrodynamic and kinetic assessment at each timestep allows for an optimization of feed delivery and implementation of feed control systems, with PID parameters tuned within the simulation, resulting in computational methods for bioreactor optimization. Using this model and CHO fed-batch experimental data, this study reveals the cell growth profile was minimally sensitive to glucose concentration, while glutamine concentration had a large impact. This model’s scale-up utility is demonstrated by showing similar cell growth profiles across scales by tuning feeding rates. This assessment was completed in one-tenth of the time typically required to simulate such a process by leveraging the time scale difference between “fast” fluid dynamics and “slow” cell kinetics.</div></div>","PeriodicalId":15153,"journal":{"name":"Journal of biotechnology","volume":"406 ","pages":"Pages 42-52"},"PeriodicalIF":4.1,"publicationDate":"2025-06-19","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144340145","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Efficient production of Ergothioneine via an optimized allogenous assembly of the ERG synthesis pathway in Escherichia coli BL21","authors":"Liang Li,&nbsp;Shanshan Xu,&nbsp;Yanjun Jiang","doi":"10.1016/j.jbiotec.2025.06.009","DOIUrl":"10.1016/j.jbiotec.2025.06.009","url":null,"abstract":"<div><div>Ergothioneine (ERG) is a potent antioxidant with applications in nutrition, pharmaceuticals, dermatology, and related fields. However, its large-scale production is constrained by low yields and high costs linked to extraction and chemical synthesis. Microbial fermentation offers a promising alternative. In this study, a truncated NcEgt1–1 from <em>Neurospora crassa</em> and CtEgtB from <em>Chloracidobacterium thermophilum</em> were fused to convert L-histidine and L-cysteine into hercynylcysteine sulfoxide, subsequently catalyzed by MsEgtE from <em>Mycobacterium smegmatis</em> to produce ERG. Initial expression in <em>Escherichia coli</em> yielded 87.02 mg/L of ERG. With the use of a rigid linker-EAAAK, the ERG titer increased to 144 mg/L. Further amino acid modifications in NcEgt1–1 resulted in the mutant strain M3–02, producing 325 mg/L of ERG. Fed-batch fermentation in a 5-L bioreactor achieved an ERG yield of 790 mg/L with a productivity of 9 mg/L/h. Iterative mutations of CtEgtB further increased ERG production to 478 mg/L in shake flasks and 790 mg/L in the bioreactor, with productivity rising to 14.9 mg/L/h. This study presents an engineered strain with significant ERG production potential, suitable for industrial application.</div></div>","PeriodicalId":15153,"journal":{"name":"Journal of biotechnology","volume":"406 ","pages":"Pages 13-23"},"PeriodicalIF":4.1,"publicationDate":"2025-06-14","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144309955","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Substitution of the 5′-untranslated region in the alcohol oxidase 1 promoter of Komagataella phaffii alleviated the repression in the presence of glycerol","authors":"Ziwei Zhou,&nbsp;Aibo Feng,&nbsp;Wenjie Cong,&nbsp;Mingxuan Wang,&nbsp;Hualan Zhou,&nbsp;Jianguo Zhang","doi":"10.1016/j.jbiotec.2025.06.011","DOIUrl":"10.1016/j.jbiotec.2025.06.011","url":null,"abstract":"<div><div><em>Komagataella phaffii (K. phaffii)</em> alcohol oxidase 1 promoter (<em>P</em>_{<em>AOX1</em>}) is repressed in the presence of glycerol, and induced by methanol when methanol is the only carbon source, which is considered as the core feature of this cell factory for recombinant protein production. It was generally accepted that the 5´ untranslated region (5´ UTR) was involved in post-transcription processing and RNA transport. In this study, the 5′ UTR of <em>P</em>_{<em>AOX1</em>} was replaced by 5´ UTR of constitutive glyceraldehyde-3-phosphate dehydrogenase promoter (<em>P</em>_<em>GAP</em>) which was not inhibited by glycerol. Modification of <em>P</em>_{<em>AOX1</em>} alleviated its repression at the condition of mixed carbon sources of glycerol and methanol, especially at 0.67 – 1 % glycerol addition and 1 % methanol. Presence of protein encoded by <em>PAS_chr4_0626</em> was considered as the key part of <em>P</em>_{<em>AOX1</em>} repression in glycerol according to sequence analysis by JASPAR. Therefore, the substitution of the 5´ UTR or knock out of <em>PAS_chr4_0626</em> attenuated <em>P</em>_{<em>AOX1</em>} inhibition by glycerol, demonstrating the potential application of heterologous protein production under the condition of mixed carbon sources of methanol and glycerol.</div></div>","PeriodicalId":15153,"journal":{"name":"Journal of biotechnology","volume":"405 ","pages":"Pages 299-307"},"PeriodicalIF":4.1,"publicationDate":"2025-06-14","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144297694","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Conventional to bacteria-based cancer therapy through bacterial components and drug delivery approaches: Pre-clinical, clinical, and future progression","authors":"Romi Shreshtha,&nbsp;Vishal Kumar Deb,&nbsp;Ankita Ghosh,&nbsp;Nidhi Chauhan,&nbsp;Utkarsh Jain","doi":"10.1016/j.jbiotec.2025.06.010","DOIUrl":"10.1016/j.jbiotec.2025.06.010","url":null,"abstract":"<div><div>Cancer is one of the current unwinnable battles, despite the abundance of treatments available. Traditional treatments like chemotherapy, radiation therapy, and surgery have been used for many years, but they are insufficient against advanced tumors. Small molecules, supramolecular complexes, modified immune cells, and plant-based molecules have all contributed to significant improvements in cancer therapy. However, certain undesirable activities and obstacles are on the horizon. To overcome such problems, research into bacterial strain-based cancer therapy has recently begun in both preclinical and clinical settings. In this context, many bacterial strains are used after genetic modification or as an innovative and smart delivery system. In this review, we have discussed several bacterial components with anti-cancerous properties, immunotherapeutic properties, and their products, such as endotoxins, peptides, etc., as well as genetically modified bacterial strains as therapeutic drug-delivery agents in cancer treatments. Herein, state-of-the-art advances, shortcomings of these therapies, and future advancements in bacteria-based therapies have also been discussed.</div></div>","PeriodicalId":15153,"journal":{"name":"Journal of biotechnology","volume":"406 ","pages":"Pages 24-41"},"PeriodicalIF":4.1,"publicationDate":"2025-06-13","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144302168","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Branched-chain polyamine beads for sensitive recovery and detection of low-copy DNA in aqueous solutions","authors":"Shinsuke Fujiwara ,&nbsp;Emi Kawamori ,&nbsp;Himari Aoki ,&nbsp;Yukiko Nakura ,&nbsp;Yuri Ishii ,&nbsp;Sadahiro Masuo ,&nbsp;Kiyoshi Yasukawa ,&nbsp;Itaru Yanagihara","doi":"10.1016/j.jbiotec.2025.06.008","DOIUrl":"10.1016/j.jbiotec.2025.06.008","url":null,"abstract":"<div><div><em>N</em>⁴-bis(aminopropyl)spermidine (BCPA), a branched-chain polyamine, is uniquely found in hyperthermophiles that thrive above 80°C. Compared to linear polyamines such as spermidine and spermine, BCPA induces DNA compaction at significantly lower concentrations and precipitates DNA more efficiently. To harness these properties, BCPA was immobilized onto <em>N</em>-hydroxysuccinimide (NHS)-activated magnetic microbeads, and its DNA recovery efficiency was evaluated using Salmon sperm DNA. BCPA-conjugated beads exhibited superior DNA-binding capacity compared to spermidine-conjugated and conventional silica beads, with bound DNA remaining unreleased upon treatment with 0.5 % sodium dodecyl sulfate (SDS), 2 mM ATP, or 2 mM phosphate (Pi) at pH 8.8. However, efficient DNA release was achieved with 2 mM pyrophosphate (PPi) at pH 8.0 or 1 mM PPi at pH 10.3. This property enables direct DNA amplification without a separate release step, as dNTPs used in PCR generate PPi as a byproduct, facilitating DNA detachment. To assess the beads' applicability for low-copy DNA detection, plasmid DNA containing the <em>Ureaplasma parvum</em> 16S rRNA region was prepared in saline at varying concentrations. BCPA-conjugated beads successfully recovered and directly amplified as few as 10³ copies of plasmid DNA from a 10-mL saline solution, whereas the same amount remained undetectable using conventional magnetic beads ethanol precipitation. These findings demonstrate the potential of BCPA-conjugated beads for efficient DNA capture and direct amplification, with promising applications in clinical diagnostics and environmental DNA monitoring.</div></div>","PeriodicalId":15153,"journal":{"name":"Journal of biotechnology","volume":"405 ","pages":"Pages 290-298"},"PeriodicalIF":4.1,"publicationDate":"2025-06-12","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144293821","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Cellular engineering strategies for soluble and secretory recombinant human insulin production in Pseudomonas fluorescens and batch bioreactor study","authors":"Ansuman Sahoo ,&nbsp;Venkata Dasu Veeranki ,&nbsp;Sanjukta Patra","doi":"10.1016/j.jbiotec.2025.06.007","DOIUrl":"10.1016/j.jbiotec.2025.06.007","url":null,"abstract":"<div><div>One of the main challenges in expressing recombinant human insulin is the formation of inclusion bodies. In our previous study, we successfully expressed insulin in <em>Pseudomonas fluorescens</em>. We observed that lowering the post-induction temperature enhanced the soluble fraction; however, it resulted in lower protein titer. In this study, the individual and synergistic effects of multiple chaperones and signal peptides on soluble protein synthesis are analyzed. A plasmid with a spectinomycin antibiotic resistance encoding gene was constructed for co-expression of chaperones. The combined effect of Disulphide bond protein A (DsbA) and phosphate binding protein (Pbp) resulted in ∼60 % of the fusion protein in soluble form. A comprehensive study was performed to assess the influence of the location of the His-tag on the expression and solubility of the protein. A high-copy origin of replication (ori) produced a lower soluble protein titer and caused a significantly longer lag phase. Under optimal concentration of antibiotics and inducer, inoculation percentage and induction OD₆₀₀, the protein and soluble protein fraction titer increased by ∼58 % and ∼27 %, respectively. In a batch bioreactor, a maximum of 234.58 mg/l fusion protein with 71.59 % solubility and around 15 % of the total soluble protein fraction in the culture supernatant was obtained. Circular dichroism analysis revealed that the secondary structure of the purified insulin was comparable to that of the standard insulin. To the best of our knowledge, this is the first study reporting the combinatorial effect of chaperones and signal peptides on the production of human insulin in the soluble form.</div></div>","PeriodicalId":15153,"journal":{"name":"Journal of biotechnology","volume":"406 ","pages":"Pages 1-12"},"PeriodicalIF":4.1,"publicationDate":"2025-06-11","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144293822","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}