Protein expression and purification最新文献

{"title":"Characterization of a novel GH5 β-mannanase from Hahella sp. CR1 and its synergistic role in degradation of spent coffee grounds","authors":"Melvin Chun Yun Tan,&nbsp;Kok Jun Liew,&nbsp;Faezah Mohd Salleh,&nbsp;Chun Shiong Chong","doi":"10.1016/j.pep.2025.106863","DOIUrl":"10.1016/j.pep.2025.106863","url":null,"abstract":"<div><div>An efficient enzymatic degradation of plant biomass is essential for agricultural waste valorization and biofuel production. β-Mannanase is a key lignocellulolytic enzyme that targets mannan, a major component in plant cell walls. <em>Hahella</em> spp. are known to produce cellulolytic enzymes, but no β-mannanase was characterized from this genus up to date. In this study, a gene encoding for β-mannanase (<em>HcrMan1</em>) was identified and isolated from the genome of <em>Hahella</em> sp. CR1. <em>HcrMan1</em> encodes a multidomain enzyme comprising a GH5 subfamily 8 catalytic domain, an immunoglobulin-like (Ig) linker domain, and a CBM2 substrate-binding domain. The presence of the rare Ig-like linker and a structurally distinct CBM2 makes its domain architecture unique compared to homologs. To investigate their contributions in the enzyme reaction, the wild-type HcrMan1 and two truncated variants (HcrMan1ΔCBM2 and HcrMan1ΔIgΔCBM2) were heterologously expressed and purified. Results revealed that the removal of Ig-like linker domain significantly affected protein solubility, whereas the deletion of CBM2 reduced the substrate-binding affinity but enhanced catalytic efficiency (K_cat/K_m) from 18.08 to 22.45. Truncated HcrMan1ΔCBM2 demonstrated a higher specific activity against locust bean gum (LBG) at optimal conditions (50 °C, pH 8.0) compared to its wild type. Furthermore, HcrMan1ΔCBM2 exhibited enhanced enzymatic performance when combined with the commercial cellulase CTec2 in saccharifying spent coffee grounds (SCG), achieving significant increase in reducing sugar release after alkali, ammonia and sonication pretreatment compared to CTec2 alone. These noteworthy findings highlight the compatibility and industrial relevance of engineered HcrMan1 in applications that involved with the utilization of lignocellulosic biomass.</div></div>","PeriodicalId":20757,"journal":{"name":"Protein expression and purification","volume":"239 ","pages":"Article 106863"},"PeriodicalIF":1.2,"publicationDate":"2026-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145654828","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":"Comparative analysis of SUMO and his-tag fusion for soluble expression of the SARS-CoV-2 omicron RBD in E. coli","authors":"Sadegh Zargan ,&nbsp;Saba Mesdaghinia ,&nbsp;Hasan Jalili ,&nbsp;Bahareh Dabirmanesh ,&nbsp;Khosro Khajeh","doi":"10.1016/j.pep.2025.106869","DOIUrl":"10.1016/j.pep.2025.106869","url":null,"abstract":"<div><div>The soluble expression of the SARS-CoV-2 Receptor-Binding Domain (RBD) is fundamental for manufacturing protein-based countermeasures. Although <em>E. coli</em> is a favored host for rapid production, its utility is often constrained by the formation of insoluble aggregates, thereby limiting the supply for vaccine and diagnostic development. Given the persistent threat of emerging SARS-CoV-2 variants, the need for reliable, high-yield expression platforms to overcome this solubility challenge remains critical. This study aimed to achieve soluble expression of the Omicron RBD variant in <em>E. coli</em> using a computationally guided strategy. To support solubility-enhancing tag selection, a machine learning–based tool (TagSolver), trained on the UESolDS dataset, predicted a 61.98 % solubility probability for the SUMO–RBD. Two constructs were designed: one containing a SUMO tag and a His-tagged RBD as a control. Both were expressed in <em>E. coli</em> SHuffle® T7 cells, and solubility was assessed by SDS–PAGE after 8 h of induction at 22 °C. The SUMO–RBD was expressed in a soluble form, whereas the His-tagged RBD was insoluble. Following purification and SUMO protease cleavage, FTIR analysis indicated a native-like secondary structure enriched in β-sheets. These findings demonstrate, for the first time, the soluble expression of the SARS-CoV-2 Omicron RBD in <em>E. coli</em> and establish a refolding-free strategy for producing this antigen. Furthermore, the TagSolver predictor was introduced, which may accelerate the selection of solubility-enhancing tags.</div></div>","PeriodicalId":20757,"journal":{"name":"Protein expression and purification","volume":"239 ","pages":"Article 106869"},"PeriodicalIF":1.2,"publicationDate":"2026-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145736792","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":"Codon harmonization for improve heterologous expression of human aromatase (CYP19A1) in E. coli cells","authors":"Marina I. Shaladonova,&nbsp;Yaraslau U. Dzichenka,&nbsp;Veronika V. Shchur,&nbsp;Antos B. Sachanka,&nbsp;Sergey A. Usanov","doi":"10.1016/j.pep.2025.106864","DOIUrl":"10.1016/j.pep.2025.106864","url":null,"abstract":"<div><div>CYP19A1 (aromatase) is the key enzyme taking part in the process of the conversion of androgens to estrogens thus considering as a major target for treatment of certain types of tumors, especially hormone dependent breast cancer. The purpose of this study is to achieve human aromatase (CYP19A1) from harmonized sequence and identify structural significance of rare codons, involved in the process of codon harmonization. There are several examples of influence of codon harmonization on the protein production and its activity, but these researches didn't include studying any human CYPs, which are difficult-to-produce membrane proteins. The aim of our study is to combine methods of codon harmonization, usage of optimal expression system and conditions, and modifications to the standard purification protocol in order to increase the yield of purified human recombinant aromatase for further usage of the enzyme for the screening of new inhibitors. In our research the structural significance of rare codons for the formation of the secondary structure is revealed, which is implemented in the algorithm of codon harmonization in human aromatase sequence. The combined approach with codon harmonization technique and one-step purification enables to achieve over 300 nmol of homogeneous, catalytically active human CYP19A1 per Liter of culture. We expect the results obtained will provide valuable information for protein engineering and enzymology.</div></div>","PeriodicalId":20757,"journal":{"name":"Protein expression and purification","volume":"239 ","pages":"Article 106864"},"PeriodicalIF":1.2,"publicationDate":"2026-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145615544","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":"Expression and production of recombinant SARS-CoV-2 RBD protein in E. coli system: comparison of performance, functionality and stability in three strains","authors":"Romina Golafshan ,&nbsp;Mahmoudreza Aghamali ,&nbsp;Mohammad Javad Rasaee","doi":"10.1016/j.pep.2025.106877","DOIUrl":"10.1016/j.pep.2025.106877","url":null,"abstract":"<div><div>The worldwide COVID-19 pandemic caused by severe acute respiratory syndrome coronavirus 2 (SARS-Cov-2). The receptor binding domain (RBD) of SARS-Cov-2 is located on the spike protein, which binds and interacts with ACE2. The RBD serve as a crucial target for the development of virus-neutralizing antibodies, vaccinations, and inhibiting agents. The goal of this study was to synthesis recombinant RBD (rRBD) protein and evaluate its expression, function, and stability in different strains of <em>Escherichia coli</em> (<em>E. coli</em>). The rRBD domain gene sequence was engineered utilizing in silico methodologies. The optimized sequence was inserted into pET-28a vector using <em>Xho</em>I and <em>Eco</em>RI restriction sites. Three <em>E. coli</em> expression strains BL21 (DE3), Rosetta-gami, and Shuffle T7 were chosen for protein synthesis. Cloning of the target gene fragment was confirmed using PCR. The validated recombinant vector was cloned into three <em>E. coli</em> strains. SDS-PAGE and Western blot analysis were used to examine the expression of the rRBD. Far-UV circular dichroism (CD) spectroscopy was used to examine secondary structure. ELISA experiments quantified the interaction of rRBD protein with HRP-conjugated anti-His antibody and serum from COVID-19 patients detected with anti-human immunoglobulin-HRP labeled. Protein stability was assessed under different temperature conditions. The rRBD protein was best expressed in all three bacterial strains at 1 mM concentration of IPTG. A 14 kDa band corresponding to the rRBD protein was identified in all three bacterial strains via Western blot. BL21 had the greatest amount of rRBD expression. The rRBD generated from Rosetta-gami exhibited the most robust affinity for anti-His antibodies. All three expressed proteins exhibited similar secondary structure, characterized by a predominance of random coil and β-sheet content. They also exhibited similar affinity to antibodies against SARS-Cov-2 generated from patients. Storage at −20 °C and 4 °C with suitable glycerol concentrations ensured optimal long-term protein stability. This study reveals that <em>E. coli</em> is still a good and flexible host system to produce functional SARS-Cov-2 RBD protein. Even though the strains had different levels of expression and binding efficacy, all of the proteins they made had comparable structures and antigenic properties. The findings validate the feasibility of using bacterial expression systems for the cost-effective production of RBD-based diagnostic reagents.</div></div>","PeriodicalId":20757,"journal":{"name":"Protein expression and purification","volume":"239 ","pages":"Article 106877"},"PeriodicalIF":1.2,"publicationDate":"2026-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145896848","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":"Expression of recombinant preenzyme Blo t 1 allergen in Escherichia coli and its IgE reactivity","authors":"Chi Linh Thi Nguyen ,&nbsp;Uyen Quynh Nguyen ,&nbsp;Phuong Mai Vu ,&nbsp;Truong Huu Nguyen ,&nbsp;Phuong Hoang Nguyen ,&nbsp;Chi Quynh Thi Do ,&nbsp;Vinh Van Hoang","doi":"10.1016/j.pep.2025.106872","DOIUrl":"10.1016/j.pep.2025.106872","url":null,"abstract":"<div><div><em>Blomia tropicalis</em> is a predominant house dust mite in tropical-subtropical climates, and its allergen Blo t 1 is recognized as a key trigger of allergic responses. This study aimed to express, purify recombinant Blo t 1 from <em>B. tropicalis</em> collected in Vietnam and assess its IgE-binding capacity using Vietnamese allergic sera. The cDNA encoding Blo t 1 was amplified from local samples, cloned into pET32b (+), and expressed in <em>Escherichia coli</em> BL21 (DE3). IgE-binding properties were evaluated through dot blot and Western blot assays. The recombinant Blo t 1 showed anomalous SDS-PAGE migration at ∼63 kDa, comprising ∼38.11 kDa from 333 amino acids of the pre-enzyme form of Blo t 1 and ∼19.47 kDa derived from vector-associated sequences, including His-tag. The protein was successfully expressed and purified using His-tag affinity chromatography. Dot blot analysis showed that 19/30 sera (63.33 %) from <em>B. tropicalis</em>-sensitized patients reacted with the recombinant protein, whereas none of the 24 control sera did. Western blot confirmed IgE-binding specificity. The recombinant Blo t 1 was purified under denaturing conditions, so the native three-dimensional structure is unlikely to be retained, and the observed IgE reactivity mainly reflects linear epitope recognition. Even so, the protein represents a useful research material corresponding to a Blo t 1 variant circulating in Vietnam. Along with expanding the limited molecular and IgE-reactivity data available for <em>B. tropicalis</em> in Southeast Asia, it also provides a basis for studies on allergen structure, epitope features, and early exploratory work related to allergen-specific immunotherapy and SIT-oriented approaches.</div></div>","PeriodicalId":20757,"journal":{"name":"Protein expression and purification","volume":"239 ","pages":"Article 106872"},"PeriodicalIF":1.2,"publicationDate":"2026-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145828358","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":"The advantage of high pH eluting Protein A resins over their regular counterparts in aggregate and host cell protein clearance","authors":"Ziyang Li ,&nbsp;Lixia Hu ,&nbsp;Yifeng Li","doi":"10.1016/j.pep.2025.106859","DOIUrl":"10.1016/j.pep.2025.106859","url":null,"abstract":"<div><div>Protein A affinity chromatography is the most well-established method and gold standard for antibody purification. Typically, low pH (i.e., 3.0–3.5) is required for elution of bound antibodies from a Protein A column. However, for acid-sensitive antibodies, this low pH condition can trigger severe aggregation. Therefore, alternative Protein A resins supporting mild elution are highly desirable. To meet this need, recently Purolite and Cytiva both developed high pH eluting Protein A resins (i.e., Jetted A50 HipH and MabSelect mild elution, respectively). We previously showed that Jetted A50 HipH not only supports mild pH elution but also exhibits improved aggregate separation capability. In the current work, with four case studies, we compared the above-mentioned two high pH eluting Protein A resins with their regular counterparts (i.e., Jetted A50 and MabSelect SuRe LX, respectively) and demonstrated that the two special Protein A resins provided much better aggregate removal and host cell protein (HCP) clearance. Thus, in addition to supporting mild elution, the two high pH eluting Protein A resins also have an edge in terms of impurity clearance.</div></div>","PeriodicalId":20757,"journal":{"name":"Protein expression and purification","volume":"239 ","pages":"Article 106859"},"PeriodicalIF":1.2,"publicationDate":"2026-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145557751","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":"A kaleidoscope of hosts: Expression systems of recombinant antibody reagents for immunological assays","authors":"Jia Xuan Yeoh ,&nbsp;Yee Siew Choong ,&nbsp;Theam Soon Lim","doi":"10.1016/j.pep.2025.106857","DOIUrl":"10.1016/j.pep.2025.106857","url":null,"abstract":"<div><div>Monoclonal antibodies (mAbs) have been shown to be highly promising reagents used in immunological analysis of various diseases and other chronic conditions due to their specific targeting, potency, and stability. Advances in protein engineering and immunology have led to the development of recombinant monoclonal antibodies at a staggering pace. Full-length antibodies IgG are generally the preferred format, but the development of smaller formats like Fab, scFv, and sdAbs opened the floodgates for more variation. This allowed for a more flexible application of mAbs in immunological assays. A diverse set of expression systems have been used to express recombinant mAbs which includes bacterial, yeast, insect, mammalian cells, plant, cell-free and <em>Leishmania</em> each with distinct advantages and disadvantages. This review highlights that the selection of an optimal expression system and antibody format must be guided by the intended application, balancing yield, structural integrity, and cost. While no single host fulfils all criteria, continued advances in host engineering, synthetic design, and AI-driven optimization are expected to streamline recombinant antibody production and expand its applicability across therapeutic and diagnostic fields.</div></div>","PeriodicalId":20757,"journal":{"name":"Protein expression and purification","volume":"239 ","pages":"Article 106857"},"PeriodicalIF":1.2,"publicationDate":"2026-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145542195","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":"Generation of a polyclonal antibody that specifically recognizes the recombinant NS5A protein of bovine viral diarrhea virus","authors":"Weijie Zhou,&nbsp;Yuting Wang,&nbsp;Shaobo Liang,&nbsp;Jingjin Hu,&nbsp;Feng Pang","doi":"10.1016/j.pep.2025.106868","DOIUrl":"10.1016/j.pep.2025.106868","url":null,"abstract":"<div><div>Bovine viral diarrhea virus (BVDV) is an economically important pathogen for causing bovine viral diarrhea (BVD), with a significant detrimental impact on cattle production worldwide. While the BVDV NS5A protein is known to be essential for replication, its function remain incompletely characterized. This study entailed cloning the NS5A gene and subsequently generating the recombinant plasmid pET-28a-NS5A for expression in <em>Escherichia coli</em>. The purified and refolded recombinant NS5A protein was employed to immunize New Zealand white rabbits, resulting in the production of specific polyclonal antibodies. The antibody was then deployed to investigate the expression of the NS5A protein. Our findings confirmed the NS5A protein was successfully produced and purified in a prokaryotic system. The generated anti-NS5A polyclonal antibody in rabbits showed a robust titer of 1:819,200. The antibody specifically detected the NS5A protein expressed in both prokaryotic and eukaryotic systems. With its high specificity and titer, this antibody may serve as a valuable reagent for investigating NS5A's functions in BVDV pathogenesis. It also holds potential for application in developing diagnostic assays and novel control strategies against BVD.</div></div>","PeriodicalId":20757,"journal":{"name":"Protein expression and purification","volume":"239 ","pages":"Article 106868"},"PeriodicalIF":1.2,"publicationDate":"2026-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145725710","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":"Amino acid chemistry and post-translational modifications underlying marine adhesive proteins: Biochemical insights for designing underwater adhesives","authors":"Taehee Yoon ,&nbsp;Hyung Joon Cha","doi":"10.1016/j.pep.2025.106851","DOIUrl":"10.1016/j.pep.2025.106851","url":null,"abstract":"<div><div>Underwater adhesion remains a complex challenge due to the interference of water with traditional bonding mechanisms. Marine organisms, such as mussels, sandcastle worms, and barnacles, have evolved specialized adhesive proteins that overcome these limitations through functional amino acid motifs. This review highlights how post-translationally derived amino acid motifs, such as 3,4-dihydroxylphenylalanine (DOPA) and phosphoserine, drive interfacial adhesion and the curing process through interfacial binding, metal coordination, and crosslinking. Alongside these, canonical amino acids, such as cysteine, lysine, arginine, histidine, glycine, and proline, contribute to redox buffering, electrostatic interactions, structural flexibility, and fibrillar assembly, which are essential for adhesive structure. The adhesive strategies of mussels, sandcastle worms, and barnacles reflect diverse mechanisms: mussels utilize DOPA-rich proteins with redox-regulation; sandcastle worms employ electrostatically driven coacervation and ion-mediated curing; barnacles generate nanostructured networks stabilized by disulfide bonding and hydrophobic packing. This review presents a unified molecular framework that links amino acid chemistry, biochemical transformations, and structural integration in underwater adhesion. It further discusses synthetic and recombinant approaches that mimic these natural systems, including catechol-functionalized polymers, complex coacervate adhesives, and genetically engineered proteins. These biomimetic platforms demonstrate the potential of translating marine adhesion logic into robust, water-compatible materials for biomedical and industrial applications.</div></div>","PeriodicalId":20757,"journal":{"name":"Protein expression and purification","volume":"239 ","pages":"Article 106851"},"PeriodicalIF":1.2,"publicationDate":"2026-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145524120","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":"The superiority of MabSelect VL, Cytiva's second-generation Protein L resin, over three other affinity resins in purifying a VHH-containing trispecific antibody","authors":"Ruomei Lv ,&nbsp;Wenjing Qi ,&nbsp;Yifeng Li","doi":"10.1016/j.pep.2025.106873","DOIUrl":"10.1016/j.pep.2025.106873","url":null,"abstract":"<div><div>Affinity chromatography is widely utilized for initial product capture in antibody purification. Besides Protein A resins, other affinity resins that bind different subdomains of an antibody have also been developed. For example, Protein L resin, KappaSelect, LambdaFabSelect and Praesto 70 CH1 selectively bind the variable region of kappa light chain (LC), constant region of kappa LC, constant region of lambda LC and CH1 domain of the heavy chain (HC), respectively. Affinity media with distinct specificities provide more options for antibody purification. For a given bispecific antibody (bsAb) purification case, depending on the composition difference between the product and byproducts, one affinity resin may outperform the others for byproduct removal. In the current study, we compared four affinity resins, Praesto Jetted A50 (a Protein A resin), Praesto 70 CH1, KappaSelect and MabSelect VL (Cytiva's second-generation Protein L resin), for their effectiveness in removing byproducts associated with a VHH-containing trispecific antibody (TsAb). The data suggested that the three non-Protein A resins outperformed the Protein A resin for byproduct removal. Among the three non-Protein A resins, MabSelect VL provided the best byproduct clearance, and it removed half-antibody, homodimers and most aggregates. This work reconfirms the necessity of screening different affinity resins with distinct specificities for achieving the best separation.</div></div>","PeriodicalId":20757,"journal":{"name":"Protein expression and purification","volume":"239 ","pages":"Article 106873"},"PeriodicalIF":1.2,"publicationDate":"2026-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145794505","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}