Applied Microbiology and Biotechnology最新文献

{"title":"Candida albicans: the current status regarding vaginal infections","authors":"Margarida Faustino,&nbsp;Carlos M. H. Ferreira,&nbsp;Ana Margarida Pereira,&nbsp;Ana P. Carvalho","doi":"10.1007/s00253-025-13478-2","DOIUrl":"10.1007/s00253-025-13478-2","url":null,"abstract":"<p>Vaginal infections caused by <i>Candida albicans</i> are a significant global health concern due to their recurrence and negative impact on quality of life. This review examines the pathogenesis of <i>C. albicans</i> infections, emphasizing critical virulence factors such as biofilm formation, adherence, and phenotypic switching. Risk factors include immune system suppression, antibiotic use, and hormonal changes, all of which can lead to fungal overgrowth and infection. Current prevention and/or treatment strategies primarily rely on antifungal therapies, personal hygiene practices, and probiotics. However, challenges like antifungal resistance, recurrence, and limited treatment efficacy highlight the need for innovative approaches. Therefore, emerging methods such as novel antifungal agents, vaccines, and nanotechnology-based delivery systems offer promising advancements to improve infection control. Additionally, the immune system plays a key role in preventing <i>C. albicans</i> infections, with both innate and adaptive immunity acting to restrict fungal colonization and growth. Commercially available products, such as antifungal creams, vaginal probiotics, and hygiene solutions, are practical options but often lack long-term efficacy. Persistent challenges, including resistance, patient noncompliance, and restricted access to emerging therapies, hinder comprehensive prevention and treatment efforts. Thus, future research should focus on promoting interdisciplinary approaches, integrating personalized medicine, and enhancing healthcare accessibility. This review intends to present the current state of the art within the abovementioned issues and to enhance the understanding of the multifactorial nature of <i>C. albicans</i> infections and advanced prevention strategies, which are essential to reduce the burden of vaginal candidiasis worldwide and improve patient quality of life outcomes.</p><p>• <i>Candida albicans pathogenesis involves biofilms, adherence, and phenotypic switching.</i></p><p>• <i>Vaccines, nanotechnology, and new drugs offer improved prevention and treatment.</i></p><p>• <i>Addressing antifungal resistance and patient compliance is key for prevention success.</i></p>","PeriodicalId":8342,"journal":{"name":"Applied Microbiology and Biotechnology","volume":"109 1","pages":""},"PeriodicalIF":3.9,"publicationDate":"2025-04-10","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://link.springer.com/content/pdf/10.1007/s00253-025-13478-2.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143818291","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Novel processes to obtain pneumococcal surface proteins for vaccines","authors":"Viviane Maimoni Gonçalves","doi":"10.1007/s00253-025-13440-2","DOIUrl":"10.1007/s00253-025-13440-2","url":null,"abstract":"<p>Current pneumococcal vaccines are based on the protection offered by capsular polysaccharides from only a few from &gt; 100 serotypes; therefore, serotype-independent vaccines composed of pneumococcal surface proteins are being developed. Despite the immense number of publications on the discovery, characterization, and evaluation of new pneumococcal vaccine candidates, there are very few that describe the bioprocess development, which is an essential step to generate material for pre-clinical and clinical tests, to obtain enough protein amount for physical–chemical, biochemical, and biological characterization, and to understand critical product and process attributes. Here, aspects of production and purification processes of pneumococcal surface proteins are reviewed, the most common bioreactor cultivation strategies are discussed, and important features of the purification process are explored to bring new insights about the correlation between protein structure and chromatography. The process development oriented to an industrial scale is an essential step for the success of novel protein-based pneumococcal vaccines and can preclude problems that could be hardly identified at flask scale production. Moreover, the early bioprocess development should favor a smooth scale-up and transfer of the process to GMP facilities for future production of new pneumococcal vaccines.</p><p>• <i>Early bioprocess development is crucial to advancing pneumococcal protein vaccines.</i></p><p>• <i>Bioreactor cultivation can help to identify possible process bottlenecks.</i></p><p>• <i>Structural features of similar proteins can orient purification process development.</i></p>","PeriodicalId":8342,"journal":{"name":"Applied Microbiology and Biotechnology","volume":"109 1","pages":""},"PeriodicalIF":3.9,"publicationDate":"2025-04-10","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://link.springer.com/content/pdf/10.1007/s00253-025-13440-2.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143818289","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Production and application of peptidyl-lys metalloendopeptidase: advances, challenges, and future perspectives","authors":"Uzair Ahmed,&nbsp;Katrin Ochsenreither,&nbsp;Thomas Eisele","doi":"10.1007/s00253-025-13473-7","DOIUrl":"10.1007/s00253-025-13473-7","url":null,"abstract":"<div><p>Peptidyl-lys metalloendopeptidases (PKMs) are enzymes that selectively cleave peptide bonds at the N-terminus of lysine residues present in the P1′ position, making them valuable tools in proteomics. This mini-review presents an overview of PKMs, covering their traditional production from native sources, recent advances in recombinant production, and the current limitations in availability. The historical and current applications of PKMs in proteomics are discussed, highlighting their role in protein sequencing, peptide mapping, and mass spectrometry-based studies. Advances in recombinant technology now enable tailored modifications to PKM, allowing it to function not only as a sister enzyme to LysC but also to trypsin, thereby enhancing its suitability for specific analytical applications. The mini-review concludes with a forward-looking statement on PKM research, emphasizing the potential to broaden its use in novel proteomic methods and other applications.</p></div>","PeriodicalId":8342,"journal":{"name":"Applied Microbiology and Biotechnology","volume":"109 1","pages":""},"PeriodicalIF":3.9,"publicationDate":"2025-04-10","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://link.springer.com/content/pdf/10.1007/s00253-025-13473-7.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143809221","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Application of a replicative targetable vector system for difficult-to-manipulate streptomycetes","authors":"Juan Pablo Gomez-Escribano,&nbsp;Alina Zimmermann,&nbsp;Shu-Ning Xia,&nbsp;Meike Döppner,&nbsp;Julia Moschny,&nbsp;Chambers C. Hughes,&nbsp;Yvonne Mast","doi":"10.1007/s00253-025-13477-3","DOIUrl":"10.1007/s00253-025-13477-3","url":null,"abstract":"<p>The low frequency of homologous recombination together with poor efficiency in introducing DNA into the cell are the main factors hampering genetic manipulation of some bacterial strains. We faced this problem when trying to construct mutants of <i>Streptomyces iranensis</i> DSM 41954, a strain in which conjugation is particularly inefficient, and suicidal vectors had failed to yield any exconjugants. In this work, we report the construction and application of a conjugative replicative vector, pDS0007, which allows selection of exconjugants even with poor conjugation efficiency. The persistence of the construct inside the cell for as long as required facilitates the homologous recombination events leading to single and double crossovers. While it was confirmed that the vector is frequently lost without selection, the recognition sequence for the I-SceI endonuclease was included in the backbone of pDS0007. The presence of a I-SceI recognition sequence would allow to force the loss of the vector and the appearance of double crossover recombinants by introducing a second construct (e.g. pIJ12742) that expresses a <i>Streptomyces</i> codon–optimised gene encoding the I-SceI endonuclease. To facilitate screening for vector-free clones, the construct also carries a <i>Streptomyces</i> codon–optimised <i>gusA</i> gene encoding the β-glucuronidase expressed from a constitutive promoter. We prove the usefulness of this vector and strategy with the strain <i>S. iranensis</i> DSM 41954, in which we could readily delete an essential gene of a newly discovered biosynthetic pathway for a phosphonate-containing natural product, which led to loss of phosphonate production according to ³¹P NMR spectroscopy.</p><p><i>• pDS0007 is a new vector for gene-targeting in difficult-to-manipulate streptomycetes.</i></p><p><i>• pDS0007 is self-replicative but easy to cure, targetable and allows visual screening.</i></p><p><i>• pDS0007 was used to prove the discovery of a novel phosphonate biosynthetic pathway.</i></p>","PeriodicalId":8342,"journal":{"name":"Applied Microbiology and Biotechnology","volume":"109 1","pages":""},"PeriodicalIF":3.9,"publicationDate":"2025-04-10","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://link.springer.com/content/pdf/10.1007/s00253-025-13477-3.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143818290","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Identification of chicken-derived antibodies targeting the Candida albicans Als3 protein","authors":"Chi-Hsin Lee,&nbsp;Chao-Jung Wu,&nbsp;Fang-Yi Yen,&nbsp;Jia-Yun Chiang,&nbsp;Ting-Jing Shen,&nbsp;Sy-Jye Leu,&nbsp;Chuang-Rung Chang,&nbsp;Hsiu-Jung Lo,&nbsp;Bor-Yu Tsai,&nbsp;Yan-Chiao Mao,&nbsp;Valencia Andriani,&nbsp;Priskila Cherisca Thenaka,&nbsp;Wei-Chu Wang,&nbsp;Yu-Pin Chao,&nbsp;Yi-Yuan Yang","doi":"10.1007/s00253-025-13469-3","DOIUrl":"10.1007/s00253-025-13469-3","url":null,"abstract":"<p><i>Candida albicans</i> is a major opportunistic pathogen, responsible for nearly half of clinical candidemia cases. The rising prevalence of azole-resistant <i>Candida</i> species represents a significant clinical challenge, underscoring the urgent need for alternative therapeutic strategies. Monoclonal antibody-based therapies have emerged as a promising and cost-effective approach to combating <i>Candida</i> infections. Agglutinin-like sequence protein 3 (Als3), a key cell surface protein of <i>C. albicans</i>, plays a pivotal role in adherence and biofilm formation, both of which are essential for its pathogenesis. In this study, recombinant Als3 protein was purified and utilized to immunize chickens, resulting in the production of Als3-specific immunoglobulin Y (IgY) antibodies. Two single-chain variable fragment (scFv) antibody libraries were subsequently constructed using phage display technology, yielding transformant counts of 5.3 × 10⁷ and 2.8 × 10⁷, respectively. Phage-based enzyme-linked immunosorbent assay (ELISA) revealed enhanced signals following bio-panning, enabling the identification and sequence validation of three scFv antibodies. These scFv antibodies exhibited strong binding activities to Als3, as confirmed through ELISA and western blot analyses. Binding affinities were determined to be ~ 10⁻⁸ M via serial titration ELISA and competitive ELISA. Additionally, the selected scFv antibodies specifically recognized endogenous Als3 protein in <i>C. albicans</i>, as demonstrated by western blot and cell-based ELISA assays. In conclusion, this study successfully generated and characterized high-affinity scFv antibodies targeting Als3, which exhibited exceptional specificity and binding activity. These findings highlight their potential as promising immunotherapeutic candidates for the treatment of <i>C. albicans</i> infections.</p><p>• <i>The Als3 protein of C. albicans is a critical biomarker and therapeutic target</i></p><p>• <i>Chicken-derived scFv antibodies against Als3 were developed via phage display</i></p><p>• <i>The scFv antibodies showed strong binding to endogenous Als3 in C. albicans</i></p>","PeriodicalId":8342,"journal":{"name":"Applied Microbiology and Biotechnology","volume":"109 1","pages":""},"PeriodicalIF":3.9,"publicationDate":"2025-04-08","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://link.springer.com/content/pdf/10.1007/s00253-025-13469-3.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143801224","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Characterization of β-glucosidase activity of a Lactiplantibacillus plantarum 6-phospho-β-glucosidase","authors":"Ravish Godse,&nbsp;Joyleen M. Fernandes,&nbsp;Ram Kulkarni","doi":"10.1007/s00253-025-13472-8","DOIUrl":"10.1007/s00253-025-13472-8","url":null,"abstract":"<p>β-Glucosidases are useful for hydrolysis of glycosidically-bound volatiles (GBV), thereby facilitating the release of aroma chemicals from the fruit matrices. In this study, 10 putative glycosyl hydrolases belonging to GH1 family from <i>Lactiplantibacillus plantarum</i> NCIM 2903 were cloned and recombinantly expressed. Interestingly, only one (LpBgl5) of the nine soluble proteins, previously characterized as a 6-phospho-β-glucosidase showed β-glucosidase activity which was further characterized. The enzyme had an optimum pH and temperature of 6 and 40°C, respectively, and was categorized as aryl-β-glucosidase due to its ability to hydrolyze different natural as well as synthetic glucosides except cellobiose. The enzyme exhibited functional activity across multiple substrates, with relative activity decreasing sequentially from β-xylosidase to β-glucosidase and finally β-mannosidase. The β-xylosidase and β-glucosidase activities of LpBgl5 were stimulated up to 300% and 700% in the presence of 4 M xylose and 4 M glucose, respectively. The enzyme could also hydrolyze GBV from mango. To our knowledge, this is the first recombinant β-glucosidase/β-xylosidase/β-mannosidase from <i>L. plantarum</i> to have potential for aroma enhancement in fruit products.</p><p>•<i> A recombinant β-glycosidase from Lactiplantibacillus plantarum was characterized.</i></p><p>•<i> The enzyme showed higher β-xylosidase activity than β-glucosidase activity.</i></p><p>•<i> The enzyme could also hydrolyze glycosidically bound volatiles from mango.</i></p>","PeriodicalId":8342,"journal":{"name":"Applied Microbiology and Biotechnology","volume":"109 1","pages":""},"PeriodicalIF":3.9,"publicationDate":"2025-04-08","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://link.springer.com/content/pdf/10.1007/s00253-025-13472-8.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143801222","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Efficient genes identification via quantitative trait loci analysis by crossbreeding of sake and laboratory yeast","authors":"Muneyoshi Kanai,&nbsp;Tomoko Shibata,&nbsp;Yan Zhou,&nbsp;Risa Hayashi,&nbsp;Ikuko Fukuba,&nbsp;Takayuki Kochi,&nbsp;Satoko Teramoto,&nbsp;Hitoshi Shimoi,&nbsp;Hidekazu Takahashi,&nbsp;Takeshi Akao","doi":"10.1007/s00253-025-13470-w","DOIUrl":"10.1007/s00253-025-13470-w","url":null,"abstract":"<p><i>Saccharomyces cerevisiae</i>, a unicellular eukaryotic microorganism, includes various strains used in alcoholic beverage production, like sake, shochu/awamori, and wine yeasts. Despite being the same “<i>Saccharomyces cerevisiae</i>”, each strain has unique genes and mutations that make them suitable for specific production processes. We focused on sake yeast, <i>Saccharomyces cerevisiae,</i> suitable for sake making. To identify genes and mutations contributing to sake yeast’s characteristics more efficiently, we improved the quantitative trait loci (QTL) analysis system. This genetic statistical method used spore-separating haploid strains (F1 segregant haploids) from crossing sake yeast and laboratory yeast haploid strains. We increased the number of F1 segregant haploids for QTL analysis from 100 to 400 and set DNA markers uniformly across the genome (approximately 12 Mbp) at 5,267 locations using single nucleotide polymorphisms (SNPs) spaced about 3 kb apart. Additionally, a small-scale sake making test using 400 F1 segregant haploids and QTL analysis of ethanol concentration in sake sample identified the <i>PBS2</i> gene and its causative mutation (amino acid substitution at position 545). The <i>PBS2</i> gene was also implicated in producing organic acids (fumaric, succinic, and malic acids) and inorganic acids (phosphoric acid) for sake. These findings validated the improved QTL analysis system as effective genes screening method.</p><p><i>• A new QTL analysis system was constructed using sake and laboratory yeast.</i></p><p><i>• PBS2 gene involved in the ethanol-producing capacity of Saccharomyces cerevisiae was identified.</i></p><p><i>• PBS2 gene was also involved in the organic acid concentration in sake.</i></p>","PeriodicalId":8342,"journal":{"name":"Applied Microbiology and Biotechnology","volume":"109 1","pages":""},"PeriodicalIF":3.9,"publicationDate":"2025-04-08","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://link.springer.com/content/pdf/10.1007/s00253-025-13470-w.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143793269","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Engineering Bacopa monnieri for improved bacoside content and its neurological evaluation","authors":"Gajendra Singh Jeena,&nbsp;Sunil Kumar,&nbsp;Sachi Bharti,&nbsp;Neeti Singh,&nbsp;Ashutosh Joshi,&nbsp;Vaibhavi Lahane,&nbsp;Roshni Meghani,&nbsp;Akhilesh Kumar Yadav,&nbsp;Shubha Shukla,&nbsp;Vineeta Tripathi,&nbsp;Rakesh Kumar Shukla","doi":"10.1007/s00253-025-13453-x","DOIUrl":"10.1007/s00253-025-13453-x","url":null,"abstract":"<p>Bacosides are triterpenoidal saponins with numerous pharmacological benefits. One of the significant drawbacks is the low availability of these bacosides. The bacoside pathway is not well elucidated, and there is no prior report of a metabolic engineering approach in this plant. In this study, we have over-expressed the active isoform of <i>Bacopa monnieri</i> squalene synthase (<i>BmSQS1-OE</i>) and silenced the <i>B. monnieri G10H (BmG10H-1-KD)</i>, the competitive metabolic pathway, to divert the flux towards triterpene biosynthesis. Absolute quantification of bacosides in these <i>BmSQS1</i>(OE)<i>-BmG10H1</i>(KD) lines has identified improved content of bacoside A3, bacopaside II, and bacoside A. Moreover, the engineered plant extract was also found to have better efficacy on locomotor activity, neuromuscular coordination, and social interaction in a 6-hydroxydopamine (6-OHDA)-induced rat model of Parkinson’s disease (PD). Immunohistochemistry of the brain tissues indicates that an extract of enhanced bacoside contents reduces 6-OHDA-induced dopaminergic depletion, implying a potential utility in neurological disorders.</p><p><i>• The engineered Bacopa monnieri extract has improved amounts of various bacoside.</i></p><p><i>• The engineered Bacopa extract has shown enhanced effectiveness in a 6-hydroxydopamine (6-OHDA)-induced rat model of Parkinson’s disease (PD).</i></p>","PeriodicalId":8342,"journal":{"name":"Applied Microbiology and Biotechnology","volume":"109 1","pages":""},"PeriodicalIF":3.9,"publicationDate":"2025-04-07","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://link.springer.com/content/pdf/10.1007/s00253-025-13453-x.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143793105","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Optimization of methods for isolation and purification of outer membrane vesicles (OMVs) from Neisseria lactamica","authors":"Ronaldo Moraes Preto,&nbsp;Vithória Carolyna Trindade dos Santos,&nbsp;Marcos Vinicius Santos Lordelo,&nbsp;Getúlio Henrique Ferreira Pereira,&nbsp;Luciana Cezar de Cerqueira Leite,&nbsp;Viviane Maimoni Gonçalves,&nbsp;Giovana Cappio Barazzone","doi":"10.1007/s00253-025-13460-y","DOIUrl":"10.1007/s00253-025-13460-y","url":null,"abstract":"<p>Outer membrane vesicles (OMVs) are nanoparticles released by Gram-negative bacteria during growth, mainly under stress conditions. OMV-based vaccines have played an important role in vaccination against <i>Neisseria meningitidis</i> serogroup B (MenB), stimulating research into novel approaches for developing more effective vaccines. OMVs released by the bacterium <i>Neisseria lactamica</i> have emerged as a promising platform for new vaccine development, especially as carriers in subunit vaccines. Despite their importance, some challenges remain in obtaining and purifying OMVs. The most commonly employed methods for OMV isolation and purification are ultracentrifugation (UC) and size exclusion chromatography (SEC). However, these techniques could present limitations for large-scale production and often result in low yields. This study investigated techniques such as tangential flow filtration (TFF), membrane chromatography, and mixed-mode (multimodal) chromatography as potential replacements for UC and SEC. Among the TFF methods evaluated, the sample obtained on the membrane with a 300-kDa cutoff showed a profile more similar to UC but with more than double the total protein recovery. Sartobind® Q membrane chromatography was ineffective for OMV purification, in the conditions evaluated, with a recovery of 8.7%. Conversely, multimodal Capto™ Adhere chromatography recovered 59.0%, while Capto™ Core 400 yielded a recovery of 72.0%, proving to be more effective for purification when analyzed by high-performance liquid chromatography (HPLC). Thus, combining TFF with a 300-kDa membrane followed by Capto™ Core 400 chromatography can be applied as strategy for large-scale applications offering high recovery and purity.</p><p><i>• Evaluation of TFF, membrane and multimodal chromatography techniques for OMV purification.</i></p><p><i>• Improved Neisseria lactamica OMV yields combining TFF and multimodal chromatography.</i></p><p><i>• A process for OMV purification from a non-pathogenic organism feasible to scale up.</i></p>","PeriodicalId":8342,"journal":{"name":"Applied Microbiology and Biotechnology","volume":"109 1","pages":""},"PeriodicalIF":3.9,"publicationDate":"2025-04-07","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://link.springer.com/content/pdf/10.1007/s00253-025-13460-y.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143786540","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Monkeypox virus H3L protein as the target antigen for developing neutralizing antibody and serological assay","authors":"I-Hsiang Huang,&nbsp;Guan-Chun Lai,&nbsp;Tai-Ling Chao,&nbsp;Wang-Da Liu,&nbsp;Sui-Yuan Chang,&nbsp;Shih-Chung Chang","doi":"10.1007/s00253-025-13466-6","DOIUrl":"10.1007/s00253-025-13466-6","url":null,"abstract":"<p>The large number of atypical monkeypox (Mpox) cases caused by emerging monkeypox virus (MPXV) strains was recently found in countries and regions where the Mpox was not reported before. Diagnostic tools and therapeutic agents are important countermeasures for preventing Mpox outbreak. H3L protein is the important surface antigen of MPXV for binding to host cell receptors and mediating viral infection. A broad range of murine anti-MPXV H3L monoclonal antibodies (mAbs) recognizing various binding epitopes have been generated in the study. The rapid test composed of the mAbs 4-2A and 3-3F can specifically detect H3L protein and MPXV virion. The mAb 3-3F exhibited strong MPXV neutralizing activity in a complement-dependent manner. Notably, 3-3F binds to a unique epitope within residues 35–89 of H3L protein. The serum samples collected from Mpox patients barely bound to the N-terminal portion of H3L protein ranging from 2 to 89 residues, indicating that the content of the 3-3F-like antibody is very low in Mpox patient sera. In contrast, the seropositivity was mostly observed using the C-terminal portion of H3L protein ranging from 185 to 282 residues as the target antigen in the immunoblot analysis. Taken together, the anti-MPXV H3L mAb can be developed as the Mpox diagnostic and therapeutic agents. Furthermore, H3L protein is the promising biomarker for serological analysis.</p><p>•<i>Anti-H3L mAbs can cross-react with H3L proteins in MPXV and VACV virions.</i></p><p>•<i>The LFIA rapid test using the mAbs 4-2A and 3-3F can specifically detect MPXV.</i></p><p>•<i>MPXV was neutralized by mAb 3-3F in a complement-dependent manner</i></p>","PeriodicalId":8342,"journal":{"name":"Applied Microbiology and Biotechnology","volume":"109 1","pages":""},"PeriodicalIF":3.9,"publicationDate":"2025-04-02","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://link.springer.com/content/pdf/10.1007/s00253-025-13466-6.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143761727","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}