{"title":"Distinct 5′ UTR Requirements for Translation of the Bicistronic X/P mRNA Among Avian Orthobornaviruses","authors":"Meng-Chi Wu, Takehiro Kanda, Ryo Komorizono, Madoka Sakai, Alexander Leacy, Leonardo Susta, Akiko Makino, Keizo Tomonaga","doi":"10.1111/1348-0421.70031","DOIUrl":"10.1111/1348-0421.70031","url":null,"abstract":"<p>Orthobornaviruses express X and the phosphoprotein (P) from a bicistronic X/P mRNA, and these proteins regulate polymerase activity. In mammalian orthobornaviruses, the 5′ untranslated region (5′ UTR) of the X/P mRNA controls the translational balance between X and P and thereby promotes efficient replication. Avian bornaviruses (ABVs) belong to two clades, clade-2 and -3, that differ in the structure and length of the 5′ UTR of the X/P mRNA. However, the functional consequences of these differences remain unclear. Using reverse genetics, we generated chimeric viruses by reciprocally exchanging the 5′ UTR of the X/P mRNA among clade 2 parrot bornavirus 5 (PaBV-5) and aquatic bird bornavirus 1 (ABBV-1) and clade 3 PaBV-4. In PaBV-5, a long 5′ UTR with a stem–loop and an upstream ORF was required to maintain the X-to-P translational balance. On the other hand, replacing the 5′ UTR of the X/P mRNA from PaBV-5 with that from PaBV-4 reduced X expression and markedly impaired viral growth. However, PaBV-4 tolerated the 5′ UTR of the X/P mRNA from PaBV-5 without detectable effects on translation or replication, which suggests that translation of PaBV-4 X/P mRNA does not depend on the origin of the 5′ UTR. Furthermore, ABBV-1 replicated efficiently with the 5′ UTR of the X/P mRNA from PaBV-5 but was strongly attenuated with that from PaBV-4. Taken together, these results demonstrate a clade-dependent requirement for the 5′ UTR for translation of the X/P mRNA and provide novel insights into the evolution of translational control in orthobornaviruses.</p>","PeriodicalId":18679,"journal":{"name":"Microbiology and Immunology","volume":"70 2","pages":"80-90"},"PeriodicalIF":1.8,"publicationDate":"2025-12-07","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12868937/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145701070","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Bordetella BcrH1 and BcrH2 Are Specific Chaperones for the Pore-Forming Complex","authors":"Yuya Kishino, Toshinobu Ogawa, Hiroko Sato, Akio Abe, Asaomi Kuwae","doi":"10.1111/1348-0421.70030","DOIUrl":"10.1111/1348-0421.70030","url":null,"abstract":"<p><i>Bordetella</i> has a type III secretion system that secretes virulence proteins crucial to the establishment of infection. The genes encoding components of the <i>Bordetella</i> type III secretion system are located in the <i>bsc</i> region on the chromosome. This region includes the <i>bcrH1</i> and <i>bcrH2</i> genes, which respectively encode the proteins BcrH1 and BcrH2. In this study, we analyzed the functions of BcrH1 and BcrH2 in the <i>Bordetella</i> type III secretion system. First, we created a BcrH1-deficient strain and a BcrH2-deficient strain. We analyzed the amounts of the type III secreted proteins BopB and BopD, which make a complex that forms pores in the host membrane, in bacterial cells of each protein-deficient strain. The results showed that the BopB and BopD signals were weakened in the whole cell fraction of the BcrH1-deficient strain and the BcrH2-deficient strain, respectively. The hemolytic activity and cell toxicity of each BcrH protein-deficient strain were significantly lower than those of the wild-type strain. When anti-BcrH1 and anti-BcrH2 antibodies were used for the immunoprecipitation assay, the BopB and BopD signals were detected in the precipitated fractions, respectively. These results strongly suggest that BcrH1 and BcrH2 are specific chaperones for maintaining the stability of BopB and BopD, respectively.</p>","PeriodicalId":18679,"journal":{"name":"Microbiology and Immunology","volume":"70 2","pages":"57-67"},"PeriodicalIF":1.8,"publicationDate":"2025-12-07","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12868935/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145701021","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Recovery of Infectious Oz Virus From Cloned cDNA","authors":"Tofazzal Md Rakib, Lipi Akter, Hiroshi Shimoda, Yudai Kuroda, Hiromichi Matsugo, Shuzo Urata, Yusuke Matsumoto","doi":"10.1111/1348-0421.70029","DOIUrl":"10.1111/1348-0421.70029","url":null,"abstract":"<div>\u0000 \u0000 <p>Oz virus (OZV) is a tick-borne, six-segmented, negative-strand RNA virus in the genus <i>Thogotovirus</i>, family <i>Orthomyxoviridae</i>. A fatal human infection was reported in Japan in 2023. In this study, we established a reverse genetics system to generate infectious recombinant OZV. Six plasmids encoding the full-length OZV genome segments under the control of a murine RNA polymerase I promoter, together with four plasmids expressing viral proteins essential for polymerase activity, were cotransfected into murine cells. This approach enabled efficient recovery of infectious OZV. The recovered recombinant virus exhibited replication kinetics comparable to wild-type OZV. This system provides a platform for molecular studies of OZV.</p>\u0000 </div>","PeriodicalId":18679,"journal":{"name":"Microbiology and Immunology","volume":"70 2","pages":"125-128"},"PeriodicalIF":1.8,"publicationDate":"2025-12-03","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145661562","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Issue Information – Cover","authors":"","doi":"10.1111/1348-0421.70028","DOIUrl":"https://doi.org/10.1111/1348-0421.70028","url":null,"abstract":"<p><b>Cover photograph</b>: METTL3 Regulated Skeletal Muscle Atrophy in CKD-Associated Sarcopenia via the TLR4/NF-κB Signaling Pathway. HE staining of kidney and gastrocnemius muscle tissues to assess histopathological changes. <i>Microbiol Immunol: 69:608-618</i>. Article link here\u0000 \u0000 <figure>\u0000 <div><picture>\u0000 <source></source></picture><p></p>\u0000 </div>\u0000 </figure></p>","PeriodicalId":18679,"journal":{"name":"Microbiology and Immunology","volume":"69 12","pages":"i-ii"},"PeriodicalIF":1.8,"publicationDate":"2025-12-02","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://onlinelibrary.wiley.com/doi/epdf/10.1111/1348-0421.70028","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145652409","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Nantaporn Kaewaroon, Sara Yoshimoto, Luthfi Muawan, Shintaro Shichinohe, Tokiko Watanabe
{"title":"Hydroxypropyl Cellulose Enhances Immune Responses to the Current Seasonal Influenza Vaccine in Mice","authors":"Nantaporn Kaewaroon, Sara Yoshimoto, Luthfi Muawan, Shintaro Shichinohe, Tokiko Watanabe","doi":"10.1111/1348-0421.70026","DOIUrl":"10.1111/1348-0421.70026","url":null,"abstract":"<p>Influenza A and B viruses cause annual epidemics and continue to pose global public health concerns. The most effective approach to preventing or mitigating the severity of influenza is vaccination. Inactivated split influenza HA vaccines are commonly used worldwide due to their strong safety profile and broad range of target groups; however, their efficacy is suboptimal, especially in the elderly. Adjuvants are used to enhance the effectiveness of some influenza vaccines, but few adjuvants have been approved for human vaccines. Previously, we identified hydroxypropyl cellulose as a promising adjuvant for the split influenza HA vaccine for the 2015–2016 and 2016–2017 influenza seasons. Here, we evaluated whether hydroxypropyl cellulose could enhance the efficacy of the quadrivalent split HA vaccine for the 2023–2024 influenza season, which contains the HA proteins of A/Victoria/4897/2022 (H1N1)pdm09 and three other strains. Using a mouse model, we performed immunogenicity studies and assessed protective efficacy against challenges with homologous and heterologous H1N1pdm09 virus strains. We found that hydroxypropyl cellulose in combination with the HA vaccine generated higher virus-specific IgG antibody titers compared to the vaccine alone. The adjuvanted vaccine provided complete protection against homologous challenge and enhanced viral clearance from respiratory organs. Notably, the adjuvanted vaccine demonstrated cross-protective efficacy against heterologous H1N1pdm09 virus challenge, improving survival rates compared to vaccine alone. Our results demonstrate that hydroxypropyl cellulose has potential as an adjuvant for current seasonal influenza vaccines.</p>","PeriodicalId":18679,"journal":{"name":"Microbiology and Immunology","volume":"70 2","pages":"68-79"},"PeriodicalIF":1.8,"publicationDate":"2025-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12868939/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145653282","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Immunostimulatory Activity of Solubilized Peptidoglycan Derivatives Prepared From Lactic Acid Bacteria","authors":"Sho Noguchi, Momoko Nakayama, Masahiro Eguchi, Sakura Onoue, Hiroaki Kouzai, Kazuyoshi Kawahara","doi":"10.1111/1348-0421.70025","DOIUrl":"10.1111/1348-0421.70025","url":null,"abstract":"<div>\u0000 \u0000 <p>To develop vaccine adjuvants from bacterial peptidoglycan (PG) the immunostimulatory activity of lysozyme-solubilized PG derived from <i>Levilactobacillus brevis</i> and <i>Lactiplantibacillus plantarum</i> was investigated. Solubilized PG from both bacteria induced IL-8 in THP-1 cells, and periodate oxidation of <i>L. plantarum</i> PG reduced the activity, suggesting that muramyl dipeptide was partially destroyed. Periodate-oxidized <i>L. plantarum</i> PG showed reduced IL-8 inducing activity in NOD2-expressing cells, while it remained in NOD1-expressing cells, suggesting that γ-<span>d</span>-glutamyl-<i>meso</i>-diaminopimelic acid structure was maintained. All PG preparations stimulated RAW264.7 cells to proliferate, suggesting that they could be potent candidates for vaccine adjuvants.</p>\u0000 </div>","PeriodicalId":18679,"journal":{"name":"Microbiology and Immunology","volume":"70 1","pages":"47-51"},"PeriodicalIF":1.8,"publicationDate":"2025-11-26","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145635992","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Takashi Tominaga, Hideharu Yukitake, Paul D. Veith, Dhana G. Gorasia, Takao Ayuse, Takuro Sanuki, Eric C. Reynolds, Koji Nakayama, Mariko Naito, Mikio Shoji
{"title":"OmpA_C-Like Domain of PorE Is Essential for PorE Function in the Type IX Secretion System (T9SS) of Porphyromonas gingivalis and Some T9SS Cargo Proteins Are Secreted in a PorE-Independent Manner","authors":"Takashi Tominaga, Hideharu Yukitake, Paul D. Veith, Dhana G. Gorasia, Takao Ayuse, Takuro Sanuki, Eric C. Reynolds, Koji Nakayama, Mariko Naito, Mikio Shoji","doi":"10.1111/1348-0421.70023","DOIUrl":"10.1111/1348-0421.70023","url":null,"abstract":"<p>The periodontal pathogen <i>Porphyromonas gingivalis</i> secretes gingipains, highly hydrolytic proteases, to the cell surface or external environment via a type IX secretion system (T9SS). PorE is one of the T9SS component proteins essential for gingipain secretion. It consists of four domains: TPR, WD40, CRD, and OmpA_C-like. In this study, we investigated the contribution and function of these PorE domains to gingipain secretion by generating PorE mutants with domain deletions and residue substitutions. We found that (i) the OmpA_C-like domain is essential for gingipain secretion, (ii) the peptidoglycan binding sites (Asp<sup>576</sup> and Asn<sup>584</sup>) in the OmpA_C-like domain are a necessity for gingipain secretion, (iii) the WD40 domain is likely involved in interaction with PorP, and (iv) the CRD domain is not essential for gingipain secretion. The function of the TPR domain could not be assessed because no PorE protein of the predicted molecular mass was detected in the TPR domain-deleted PorE mutant. We also demonstrated that some T9SS cargo proteins, such as PorA and Hbp35, do not require the PorE-PorP complex for secretion, suggesting that the PorE–PorP complex may occupy a unique position within the T9SS that is distinct from other components.</p>","PeriodicalId":18679,"journal":{"name":"Microbiology and Immunology","volume":"70 1","pages":"15-26"},"PeriodicalIF":1.8,"publicationDate":"2025-11-19","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://onlinelibrary.wiley.com/doi/epdf/10.1111/1348-0421.70023","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145557357","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Development of a Porcine Cell Line Stably Expressing Ephrin-B2 for Nipah Virus Research and Diagnostic Testing","authors":"Hui Zhang, Akatsuki Saito","doi":"10.1111/1348-0421.70022","DOIUrl":"10.1111/1348-0421.70022","url":null,"abstract":"<p>Nipah virus (NiV) is a highly pathogenic zoonotic virus transmitted from bats to humans through pigs as a crucial intermediate host. NiV outbreaks pose significant public health and economic threats, especially for pig farmers. Although the World Organization for Animal Health recommends African green monkey-derived Vero cells for NiV isolation, pig-derived cell lines could represent an optimal platform for propagating pig-origin NiV, as signs and symptoms of NiV infection differ among different hosts. In this study, we generated and evaluated pig-derived PK-15 cells stably expressing pig-derived ephrin-B2 (PK-15/Ephrin-B2 cells), the primary receptor for NiV. NiV pseudovirus infectivity was increased by > 1000-fold in PK-15/Ephrin-B2 cells compared with that in wild-type PK-15 cells, whereas virus susceptibility was higher in PK-15/Ephrin-B2 cells than in Vero cells (> 30-fold). Furthermore, <i>Stat2</i>-knockout PK-15/Ephrin-B2 cells exhibited stable viral infectivity in the presence of type I interferon, making it particularly suitable for clinical sample testing. Moreover, PK-15/Ephrin-B2 cells proved useful for neutralization tests using anti-NiV hyperimmune ascitic fluid. Therefore, PK-15 cells expressing pig ephrin-B2 could represent an efficient tool for virus isolation, vaccine development, and virological studies of NiV and related henipaviruses.</p>","PeriodicalId":18679,"journal":{"name":"Microbiology and Immunology","volume":"70 1","pages":"36-46"},"PeriodicalIF":1.8,"publicationDate":"2025-11-17","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://onlinelibrary.wiley.com/doi/epdf/10.1111/1348-0421.70022","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145534641","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Correction to “Bifidobacterium Bifidum G9-1 Survives In the Intestinal Environment and Influences the Gut Microbiota Despite the Presence of Antimicrobials”","authors":"","doi":"10.1111/1348-0421.70024","DOIUrl":"10.1111/1348-0421.70024","url":null,"abstract":"<p>Yokota, H., Makizaki, Y., Tanaka, Y. and Ohno, H., “<i>Bifidobacterium bifidum</i> G9-1 Survives in the Intestinal Environment and Influences the Gut Microbiota Despite the Presence of Antimicrobials,” <i>Microbiology and Immunology</i> 69 (2025): 447–456, https://doi.org/10.1111/1348-0421.13230.</p><p>In the originally published version of this article, the Y-axis unit labels in Figures 1-6 through 7 were incorrectly written as “log<sub>10</sub> CFU/mL” or “log<sub>10</sub> CFU/g”. This was a typographical error. The correct units should be “CFU/mL” or “CFU/g”, which stand for colony-forming units per milliliter and colony-forming units per gram, respectively, and accurately reflect the microbiological quantification used in the study. The incorrect units may have caused confusion regarding the interpretation of microbial load. All affected figures have been revised to display the correct units. No changes have been made to the main text of the article.</p><p>We apologize for this error.</p>","PeriodicalId":18679,"journal":{"name":"Microbiology and Immunology","volume":"70 1","pages":"52-55"},"PeriodicalIF":1.8,"publicationDate":"2025-11-17","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://onlinelibrary.wiley.com/doi/epdf/10.1111/1348-0421.70024","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145534580","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Mina Hashimoto, Yoshihiko Tanimoto, Eriko Kage-Nakadai
{"title":"Administration of Lactiplantibacillus brownii Strain MH-1 During the Larval Stage Increases the Resistance Against Staphylococcus aureus subsp. aureus in Caenorhabditis elegans","authors":"Mina Hashimoto, Yoshihiko Tanimoto, Eriko Kage-Nakadai","doi":"10.1111/1348-0421.70020","DOIUrl":"10.1111/1348-0421.70020","url":null,"abstract":"<div>\u0000 \u0000 <p><i>Lactiplantibacillus brownii</i> is a new species of lactic acid bacteria discovered in sauerkraut in Russia, first reported in 2023. We previously isolated <i>L. brownii</i> strain MH-1 (MH-1) from homemade pickled Chinese cabbage in Japan and reported that MH-1 prolonged healthspan and improved stress resistance in <i>Caenorhabditis elegans</i>. In the present study, we investigated the effect of feeding MH-1 on resistance to infections in <i>C. elegans</i>. MH-1 failed to increase its resistance to infection with <i>Staphylococcus aureus</i> subsp. <i>aureus</i> (SA) and <i>Salmonella enterica</i> (SE) at the adult stage. However, MH-1 feeding at the larval stage remarkably increased the survival rate of worms infected with SA, but not with SE. Genes related to the innate immune response were significantly upregulated by MH-1 feeding at the larval stage compared with those of the control group. A survival assay using loss-of-function mutants revealed that resistance to SA infection conferred by MH-1 feeding during the larval stage requires <i>daf-16</i> and <i>pmk-1</i>. These results suggest that MH-1 feeding at the larval stage likely confers resistance to SA infection by enhancing host immunity via the insulin/insulin-like growth factor 1 signaling and p38 mitogen-activated protein kinase pathways.</p>\u0000 </div>","PeriodicalId":18679,"journal":{"name":"Microbiology and Immunology","volume":"70 1","pages":"1-8"},"PeriodicalIF":1.8,"publicationDate":"2025-11-03","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145431899","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}