Protein expression and purification最新文献

{"title":"Expression, purification and characterization of a novel triple fusion protein developed for the immunotherapy of survivin positive cancers","authors":"Ambreen Rashid ,&nbsp;Mohammad Azad ,&nbsp;Anuja Krishnan ,&nbsp;Jagdish C. Gupta ,&nbsp;G.P. Talwar","doi":"10.1016/j.pep.2024.106614","DOIUrl":"10.1016/j.pep.2024.106614","url":null,"abstract":"<div><div>Survivin is an inhibitor of apoptosis, and expressed in a large number of cancers. As Survivin expression is very low in normal tissues, it assumes significance as a prominent target for tumor diagnosis, prognosis and developing anti-cancer therapies. We report development of a novel triple fusion protein for a prospective vaccine against Survivin in targeted cancer immunotherapy. A gene was synthesized by combining the nucleotides encoding human origin Survivin and heat-labile enterotoxin of <em>Escherichia coli</em> (LTB). Further, nucleotides corresponding to single chain variable fragment (scFv) of a monoclonal having affinity for DEC205 receptor present on dendritic cells, were also incorporated into the gene sequence. This complete gene was expressed to a triple fusion recombinant protein using a bacterial expression vector under the control of robust bacteriophage T7 promoter. The recombinant _DCSurvivin-LTB protein, with a size of approximately 60 kDa, was purified from the inclusion bodies using affinity based Ni-NTA columns. The purified protein was confirmed by the Western blot, and further characterized with circular dichroism, fluorescence spectroscopy and mass spectroscopy. This molecularly adjuvanted Survivin fusion protein designed to deliver to the dendritic cells for better antigen processing, elicited a stronger anti-Survivin immune response compared to Survivin protein alone. It can be an effective vaccine in active and passive immunotherapies for Survivin expressing cancer cells.</div></div>","PeriodicalId":20757,"journal":{"name":"Protein expression and purification","volume":"226 ","pages":"Article 106614"},"PeriodicalIF":1.4,"publicationDate":"2024-10-11","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142473255","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"N-linked glycosylation affects catalytic parameters and fluctuation of the active center of Aspergillus awamori exo-inulinase","authors":"Anna Dotsenko ,&nbsp;Yury Denisenko ,&nbsp;Ivan Zorov ,&nbsp;Aleksandra Rozhkova ,&nbsp;Igor Shashkov","doi":"10.1016/j.pep.2024.106613","DOIUrl":"10.1016/j.pep.2024.106613","url":null,"abstract":"<div><div>Heterogeneous expression of enzymes allows large-scale production with reduced costs. Changes in glycosylation often occur due to changes in the expression host. In the study, the catalytic and biochemical properties of <em>Aspergillus awamori</em> exo-inulinase 1 are compared for <em>A. awamori</em> and <em>Penicillium verruculosum</em> expression hosts. The tertiary structure contains seven sites of <em>N</em>-glycosylation, with two of them located near the active center. If expressed in <em>P. verruculosum</em>, the enzyme was four times less glycosylated and two times more active toward sucrose, raffinose, and stachyose due to an increase in <em>k</em>_<em>cat</em>. These substrates with a short chain of 2–4 monosaccharide units were used to characterize the interaction of the substrate with the amino acid residues in the active center while preventing the interaction of the substrate with <em>N</em>-linked glycans. Molecular dynamics simulations showed an increase in the fluctuation of the active center with an increase in the length of <em>N</em>-linked glycans. The fluctuation of the residues N40 and Q57, which interact with the hydroxyl group O5 of the fructose unit in the −1 subsite of the active center, was increased by 1.6 times. The fluctuation of the residue W335, which interacts with the hydroxyl group O1 of the fructose unit together with the catalytic residue D41 and affects the torsion angle geometry of the substrate molecules, was increased by 1.5 times. The residue R188, which analogously to W335 affects the torsion angle geometry of the substrate molecules, was also among the affected residues with a 1.2-fold increase in the fluctuation.</div></div>","PeriodicalId":20757,"journal":{"name":"Protein expression and purification","volume":"226 ","pages":"Article 106613"},"PeriodicalIF":1.4,"publicationDate":"2024-09-30","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142366345","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Heterologous expression and purification of glutamate decarboxylase-1 from the model plant Arabidopsis thaliana: Characterization of the enzyme's in vitro truncation by thiol endopeptidase activity","authors":"Brittany S. Menard ,&nbsp;Kirsten H. Benidickson ,&nbsp;Lee Marie Raytek ,&nbsp;Wayne A. Snedden ,&nbsp;William C. Plaxton","doi":"10.1016/j.pep.2024.106612","DOIUrl":"10.1016/j.pep.2024.106612","url":null,"abstract":"<div><div>Plant glutamate decarboxylase (GAD) is a Ca²⁺-calmodulin (CaM) activated enzyme that produces γ-aminobutyrate (GABA) as the first committed step of the GABA shunt. Our prior research established that <em>in vivo</em> phosphorylation of AtGAD1 (AT5G17330) occurs at multiple N-terminal serine residues following Pi resupply to Pi-starved cell cultures of the model plant <em>Arabidopsis thaliana</em>. The aim of the current investigation was to purify recombinant AtGAD1 (rAtGAD1) following its expression in <em>Escherichia coli</em> to facilitate studies of the impact of phosphorylation on its kinetic properties. However, <em>in vitro</em> proteolytic truncation of an approximate 5 kDa polypeptide from the C-terminus of 59 kDa rAtGAD1 subunits occurred during purification. Immunoblotting demonstrated that most protease inhibitors or cocktails that we tested were ineffective in suppressing this partial rAtGAD1 proteolysis. Although the thiol modifiers N-ethylmaleimide or 2,2-dipyridyl disulfide negated rAtGAD1 proteolysis, they also abolished its GAD activity. This indicates that an essential -SH group is needed for catalysis, and that rAtGAD1 is susceptible to partial degradation either by an <em>E. coli</em> cysteine endopeptidase, or possibly via autoproteolytic activity. The inclusion of exogenous Ca²⁺/CaM facilitated the purification of non-proteolyzed rAtGAD1 to a specific activity of 27 (μmol GABA produced/mg) at optimal pH 5.8, while exhibiting an approximate 3-fold activation by Ca²⁺/CaM at pH 7.3. By contrast, the purified partially proteolyzed rAtGAD1 was &gt;40 % less active at both pH values, and only activated 2-fold by Ca²⁺/CaM at pH 7.3. These results emphasize the need to diagnose and prevent partial proteolysis before conducting kinetic studies of purified regulatory enzymes.</div></div>","PeriodicalId":20757,"journal":{"name":"Protein expression and purification","volume":"226 ","pages":"Article 106612"},"PeriodicalIF":1.4,"publicationDate":"2024-09-27","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142352672","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Evaluation of BVDV E2 proteins based on recombinant baculovirus expression system production as diagnostic antigens and immunogens","authors":"Jinke He ,&nbsp;Xiaoyu Deng ,&nbsp;Xusheng Ma ,&nbsp;Liangjia Yao ,&nbsp;Yiguo Li ,&nbsp;Chuangfu Chen ,&nbsp;Yanhua He","doi":"10.1016/j.pep.2024.106611","DOIUrl":"10.1016/j.pep.2024.106611","url":null,"abstract":"<div><div>Bovine viral diarrhea virus (BVDV) is a significant immunosuppressive pathogen that has a major impact on the global cattle industry. Research efforts are currently focused on the envelope glycoprotein E2 of BVDV to improve immune responses. However, the full-length E2 protein is not ideal as an immune antigen and diagnostic tool, leading to the exploration of alternative strategies. In this study, we optimized the E2 gene using IDEB and ExpOptimizer software, then expressed the E2 gene using both baculovirus and <em>E. coli</em> expression systems. Subsequently, we assessed the immunogenicity of the purified E2 protein in mice and its application in indirect ELISA assays. Our findings showed that the Bac-E2 protein produced by the baculovirus system induced higher levels of antibody production and splenic lymphocyte proliferation in mice compared to the <em>E. coli</em> system. Moreover, the indirect ELISA assay developed using Bac-E2 protein exhibited superior specificity, sensitivity, and accuracy in comparison to the <em>E. coli</em>-expressed E2 ELISA. Overall, our study demonstrates that the optimized E2 protein generated through a baculovirus expression system elicits robust humoral and cellular immune responses in mice, making it a promising candidate for vaccine development. Furthermore, the optimized E2 protein ELISA assay shows enhanced sensitivity and accuracy, suggesting its potential as a valuable diagnostic antigen.</div></div>","PeriodicalId":20757,"journal":{"name":"Protein expression and purification","volume":"226 ","pages":"Article 106611"},"PeriodicalIF":1.4,"publicationDate":"2024-09-22","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142314941","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Anti-biofilm and antibacterial effect of bacteriocin derived from Lactobacillus plantarum on the multidrug-resistant Acinetobacter baumannii","authors":"Kasra Javadi ,&nbsp;Mohammad Reza Emadzadeh ,&nbsp;Seyed Amir Hossein Mohammadzadeh Hosseini Moghri ,&nbsp;Mehrdad Halaji ,&nbsp;Hadi Parsian ,&nbsp;Mehdi Rajabnia ,&nbsp;Abazar Pournajaf","doi":"10.1016/j.pep.2024.106610","DOIUrl":"10.1016/j.pep.2024.106610","url":null,"abstract":"<div><div>This research examines the impact of bacteriocin derived from <em>Lactobacillus plantarum</em> PTCC 1745 on the biofilm formations of <em>A</em>. <em>baumannii</em> isolates. Bacteriocin derived from <em>L</em>. <em>plantarum</em> PTCC 1745 was obtained through ammonium sulfate precipitation, cation-exchange chromatography, and reversed-phase high-performance liquid chromatography (RP-HPLC). Testing for bacteriocin susceptibility has been conducted using the broth dilution method. The anti-biofilm activity of bacteriocin was evaluated using a microtiter plate method. Quantitative real-time PCR assay evaluated <em>bap</em> gene expression in bacteriocin-treated cells. According to SDS-PAGE, bacteriocin from <em>L</em>. <em>plantarum</em> has a 25-kDa apparent molecular weight. The MICs of bacteriocin ranged from 30 to 120 μg/mL, while the MBCs varied between 60 and 120 μg/mL. Compared to the non-treated group, strains bacteriocin-treated isolates had 59 % less ability to form biofilm. The mean relative expression of the <em>bap</em> gene among the MDR <em>A</em>. <em>baumannii</em> isolates decreased by 52 % compared to the untreated control. This study demonstrated that bacteriocin derived from <em>L</em>. <em>plantarum</em> PTCC 1745 had antibacterial and antibiofilm activity against MDR <em>A</em>. <em>baumannii</em> isolates.</div></div>","PeriodicalId":20757,"journal":{"name":"Protein expression and purification","volume":"226 ","pages":"Article 106610"},"PeriodicalIF":1.4,"publicationDate":"2024-09-19","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142293976","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Cloning and characterization of a novel nitric oxide synthase gene from Exiguobacterium profundum and its expression in Escherichia coli","authors":"Xifan Luo,&nbsp;Xinyu Li,&nbsp;Yaru Zhang,&nbsp;Fei Zhao,&nbsp;Jinlong Wang,&nbsp;Jiang Wu","doi":"10.1016/j.pep.2024.106609","DOIUrl":"10.1016/j.pep.2024.106609","url":null,"abstract":"<div><div>The recognition and characterization of gene-encoded nitric oxide synthase (NOS) from <em>Exiguobacterium profundum</em> are reported in this study. A new gene was sequenced and cloned from <em>E. profundum</em> and heterologously expressed in <em>E. coli</em> for functional identification, followed by protein purification using the His-tag. The stability and activity characteristics of the recombinant NOS were evaluated using different concentrations of IPTG at various time points. A band of approximately 42 kDa was observed by SDS-PAGE. The K_m value of NOS, calculated based on the Michaelis-Menten equation was 0.59 μmol/L. Additionally, homologous sequence alignment analysis indicated that the new NOS shared 80.48 % similarity with the same protein from <em>Bacillus subtilis</em> and <em>Umezawaea</em>. The construction of the NOS expression vector and the purification of the recombinant protein provide a foundation for further functional research and inhibitor development.</div></div>","PeriodicalId":20757,"journal":{"name":"Protein expression and purification","volume":"226 ","pages":"Article 106609"},"PeriodicalIF":1.4,"publicationDate":"2024-09-18","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142293977","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Characterization of a marine endolysin LysVPB against Vibrio parahaemolyticus","authors":"Juan Chen ,&nbsp;Ziyun Zhao ,&nbsp;Xiaofeng Mu ,&nbsp;Mengxin Wang ,&nbsp;Jun Tang ,&nbsp;Qingqing Bi","doi":"10.1016/j.pep.2024.106608","DOIUrl":"10.1016/j.pep.2024.106608","url":null,"abstract":"<div><p>Currently, there is an urgent to develop safe and environmentally friendly alternatives to antibiotics for combating <em>Vibrio parahaemolyticus</em>. Endolysins are considered promising antibacterial agents due to their desirable range of action and ability to deal with antibiotic-resistant bacteria. While numerous <em>Vibrio</em> phages have been identified, the research on their endolysins is still in its infancy. In this study, a novel endolysin called LysVPB was cloned and expressed in <em>Pichia pastoris</em>. Phylogenetic analysis revealed that LysVPB bears little resemblance to other known endolysins, highlighting its unique nature. Homology modeling identified a putative calcium-binding site in LysVPB. The recombinant LysVPB achieved a lytic activity of 64.8 U/mL and had a molecular weight of approximately 17 kDa. LysVPB exhibited enhanced efficacy at pH 9.0, with 60 % of its maximum activity observed within the broad pH range of 6.0–10.0. The catalytic efficiency of LysVPB peaked at 30 °C but significantly declined beyond 50 °C. Ba²⁺, Co²⁺, and Cu²⁺ showed inhibitory effects on the activity of LysVPB, while Ca²⁺ can boost it to 126.8 %. Furthermore, LysVPB exhibited satisfactory efficacy against strains of <em>V. parahaemolyticus</em>. LysVPB is an innovative phage lysin with good characteristics that are specific to certain hosts. The modular nature of LysVPB allows for efficient domain exchange with alternative lysins as antimicrobial components and fusion with antimicrobial peptides. This opens up possibilities for engineering chimeric lysins in a broader range of target hosts with high antimicrobial effectiveness and strong activity under physiological conditions.</p></div>","PeriodicalId":20757,"journal":{"name":"Protein expression and purification","volume":"226 ","pages":"Article 106608"},"PeriodicalIF":1.4,"publicationDate":"2024-09-16","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142239835","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Insights into the functional mechanism of the non-specific lipid transfer protein nsLTP in Kalanchoe fedtschenkoi (Lavender scallops)","authors":"Dafeng Liu ,&nbsp;Wenrui Dou ,&nbsp;Hongying Song ,&nbsp;Huashui Deng ,&nbsp;Zhu Tian ,&nbsp;Rong Chen ,&nbsp;Zhen Liu ,&nbsp;Ziwei Jiao ,&nbsp;Oren Akhberdi","doi":"10.1016/j.pep.2024.106607","DOIUrl":"10.1016/j.pep.2024.106607","url":null,"abstract":"<div><p>Plant non-specific lipid transfer protein (nsLTP) is able to bind and transport lipids and essential oils, as well as engage in various physiological processes, including defense against phytopathogens. <em>Kalanchoe fedtschenkoi</em> (<em>Lavender Scallops</em>) is an attractive and versatile succulent. To investigate the functional mechanism of <em>Kalanchoe fedtschenkoi</em> nsLTP (Ka-nsLTP), we expressed, purified and successfully obtained monomeric Ka-nsLTP. Mutational experiments revealed that the C6A variant retained the same activity as the wild-type (WT) Ka-nsLTP. Ka-nsLTP showed weak antiphytopathogenic bacterial activity, but inhibited fungal growth. Ka-nsLTP possessed a hydrophobic cavity effectively binding lauric acid. Our results offer novel molecular insights into the functional mechanism of nsLTP, which broadens our knowledge of the biological function of nsLTP in crops and provides a useful locus for genetic improvement of plants.</p></div>","PeriodicalId":20757,"journal":{"name":"Protein expression and purification","volume":"226 ","pages":"Article 106607"},"PeriodicalIF":1.4,"publicationDate":"2024-09-10","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142164833","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Biochemical and structural characterization of a novel L-isoleucine-4-dioxygenase (RaIDO) from Rahnella aquatilis","authors":"Ruida Shan ,&nbsp;Yishu Wang ,&nbsp;Shuxin Cheng ,&nbsp;Xia Li ,&nbsp;Xiaohui Yang ,&nbsp;Dengyue Sun ,&nbsp;Piwu Li","doi":"10.1016/j.pep.2024.106604","DOIUrl":"10.1016/j.pep.2024.106604","url":null,"abstract":"<div><p>The _L-isoleucine-4-dioxygenase converts _L-isoleucine (Ile) into(2<em>S</em>,3<em>R</em>,4<em>S</em>)-4-(OH)-isoleucine (4-HIL), a naturally occurring hydroxyl amino acid, which is a promising compound for drug and functional food development. Here, a novel _L-isoleucine-4-dioxygenase (<em>Ra</em>IDO) from <em>Rahnella aquatilis</em> was cloned, expressed and characterized, as one of only a few reported _L-isoleucine-4-dioxygenases. <em>Ra</em>IDO showed high catalytic efficiency with Ile as the substrate, as well as good stability. HPLC-MS and NMR confirmed that <em>Ra</em>IDO converts Ile into (2<em>S</em>,3<em>R</em>,4<em>S</em>)-4-(OH)-isoleucine. Further, structural analysis of <em>Ra</em>IDO revealed key active site residues, including H159, D161 and H212. The <em>Ra</em>IDO enzyme showed an optimal reaction temperature range of 30°C–45 °C, with the highest catalytic activity observed at 40 °C. Additionally, the enzyme exhibited an optimal pH of 8.0. Thus, the novel _L-isoleucine-4-dioxygenase (<em>Ra</em>IDO) has high catalytic efficiency and good stability, making it a strong candidate for industrial applications.</p></div>","PeriodicalId":20757,"journal":{"name":"Protein expression and purification","volume":"226 ","pages":"Article 106604"},"PeriodicalIF":1.4,"publicationDate":"2024-09-06","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142146096","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Development of an effective method for purifying trypsin using a recombinant inhibitor","authors":"Chen Li ,&nbsp;Zhaoxia Wang ,&nbsp;Zejie Niu ,&nbsp;Jiao Li ,&nbsp;Lanxin Chen ,&nbsp;Xiaodong Cui ,&nbsp;Fang Li","doi":"10.1016/j.pep.2024.106597","DOIUrl":"10.1016/j.pep.2024.106597","url":null,"abstract":"<div><p>A trypsin affinity material was prepared by covalently immobilizing buckwheat trypsin inhibitor (BTI) on epichlorohydrin-activated cross-linked agarose gel (Selfinose CL 6 B). The optimal conditions for activating Selfinose CL 6 B were 15 % epichlorohydrin and 0.8 M NaOH at 40 °C for 2 h. The optimal pH for immobilizing BTI was 9.5. BTI-Sefinose CL 6 B showed a maximum adsorption capacity of 2.25 mg trypsin/(g support). The material also displayed good reusability, retaining over 90 % of its initial adsorption capacity after 30 cycles. High-purity trypsin was obtained from locust homogenate using BTI-Selfinose CL 6 B through one-step affinity chromatography. The molecular mass and <em>K</em>_m value of locust trypsin were determined as 27 kDa and 0.241 mM using N-benzoyl-DL-arginine-nitroanilide as substrate. The optimal temperature and pH of trypsin activity were 55 °C and 9.0, respectively. The enzyme exhibited good stability in the temperature range of 30–50 °C and pH range of 4.0–10.0. BTI-Selfinose CL 6 B demonstrates potential application in the preparation of high-purity trypsin and the discovery of more novel trypsin from various species.</p></div>","PeriodicalId":20757,"journal":{"name":"Protein expression and purification","volume":"225 ","pages":"Article 106597"},"PeriodicalIF":1.4,"publicationDate":"2024-09-02","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142133522","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}