High-throughput single-cell analysis reveals Omp38-specific monoclonal antibodies that protect against Acinetobacter baumannii infection
Infections caused by Acinetobacter baumannii (A. baumannii) have emerged as a global public health concern because of high pathogenicity of this bacterium. Monoclonal antibodies (mAbs) have a lower likelihood of promoting drug resistance and offer targeted treatment, thereby reducing potential adver...
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Taylor & Francis Group
2025-12-01
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| Series: | Emerging Microbes and Infections |
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| Online Access: | https://www.tandfonline.com/doi/10.1080/22221751.2024.2437243 |
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| author | Yiwei Zhang Hao Cheng Peng Yu Shufeng Wang Hui Dong Song Lu Ruiqi Yang Baiqing Li Jie Luo Ruihan Mao Zhaohui Zhang Yong Qi Xiaohua Chen Jinya Ding Zemin He Jingbo Zhang Tingting Zhao Xiangmei Chen Rong Lin Haibo Li Yi Tian Yuzhang Wu |
| author_facet | Yiwei Zhang Hao Cheng Peng Yu Shufeng Wang Hui Dong Song Lu Ruiqi Yang Baiqing Li Jie Luo Ruihan Mao Zhaohui Zhang Yong Qi Xiaohua Chen Jinya Ding Zemin He Jingbo Zhang Tingting Zhao Xiangmei Chen Rong Lin Haibo Li Yi Tian Yuzhang Wu |
| author_sort | Yiwei Zhang |
| collection | DOAJ |
| description | Infections caused by Acinetobacter baumannii (A. baumannii) have emerged as a global public health concern because of high pathogenicity of this bacterium. Monoclonal antibodies (mAbs) have a lower likelihood of promoting drug resistance and offer targeted treatment, thereby reducing potential adverse effects; however, the therapeutic potential of mAbs targeting A. baumannii has not been fully characterized. In this study, mAbs against the outer membrane proteins (OMPs) of A. baumannii were isolated in a high-throughput manner. The ability of Omp38-specific mAbs to bind to A. baumannii strains from diverse sources was confirmed via enzyme-linked immunosorbent assay (ELISA). Intravenous administration of the Omp38-specific mAbs significantly improved the survival rate and reduced the bacterial load in a mouse model of lethal A. baumannii infection. Flow cytometry and ELISA confirmed that immune cell infiltration and cytokine production, respectively, decreased in a mouse model of sublethal A. baumannii infection. In addition, analysis of the Omp38-mAb C3 binding conformation revealed the potential mechanism of broad-spectrum binding activity of this mAb against A. baumannii. Taken together, these findings indicate that mAbs against Omp38 facilitate bacterial clearance from host, minimize inflammatory mediator release and reduce host damage, highlighting the potential of Omp38-specific mAbs in the clinical treatment of A. baumannii infection. |
| format | Article |
| id | doaj-art-66147598e0af47c3a28f4a8d7c8f209b |
| institution | OA Journals |
| issn | 2222-1751 |
| language | English |
| publishDate | 2025-12-01 |
| publisher | Taylor & Francis Group |
| record_format | Article |
| series | Emerging Microbes and Infections |
| spelling | doaj-art-66147598e0af47c3a28f4a8d7c8f209b2025-08-20T01:58:22ZengTaylor & Francis GroupEmerging Microbes and Infections2222-17512025-12-0114110.1080/22221751.2024.2437243High-throughput single-cell analysis reveals Omp38-specific monoclonal antibodies that protect against Acinetobacter baumannii infectionYiwei Zhang0Hao Cheng1Peng Yu2Shufeng Wang3Hui Dong4Song Lu5Ruiqi Yang6Baiqing Li7Jie Luo8Ruihan Mao9Zhaohui Zhang10Yong Qi11Xiaohua Chen12Jinya Ding13Zemin He14Jingbo Zhang15Tingting Zhao16Xiangmei Chen17Rong Lin18Haibo Li19Yi Tian20Yuzhang Wu21Institute of Immunology, Third Military Medical University (Army Medical University), Chongqing, People’s Republic of ChinaDepartment of Microbiology and Biochemical Pharmacy, National Engineering Research Center of Immunological Products, College of Pharmacy, Third Military Medical University (Army Medical University), Chongqing, People’s Republic of ChinaChongqing International Institute for Immunology, Chongqing, People’s Republic of ChinaInstitute of Immunology, Third Military Medical University (Army Medical University), Chongqing, People’s Republic of ChinaInstitute of Immunology, Third Military Medical University (Army Medical University), Chongqing, People’s Republic of ChinaChongqing International Institute for Immunology, Chongqing, People’s Republic of ChinaChongqing International Institute for Immunology, Chongqing, People’s Republic of ChinaInstitute of Immunology, Third Military Medical University (Army Medical University), Chongqing, People’s Republic of ChinaThe First Affiliated Hospital, Third Military Medical University (Army Medical University), Chongqing, People’s Republic of ChinaInstitute of Immunology, Third Military Medical University (Army Medical University), Chongqing, People’s Republic of ChinaInstitute of Immunology, Third Military Medical University (Army Medical University), Chongqing, People’s Republic of ChinaThe Second Affiliated Hospital, Third Military Medical University (Army Medical University), Chongqing, People’s Republic of ChinaThe Second Affiliated Hospital, Third Military Medical University (Army Medical University), Chongqing, People’s Republic of ChinaThe Second Affiliated Hospital, Third Military Medical University (Army Medical University), Chongqing, People’s Republic of ChinaThe Second Affiliated Hospital, Third Military Medical University (Army Medical University), Chongqing, People’s Republic of ChinaGeneral Hospital of Central Theater Command, Wuhan, Hubei, People’s Republic of ChinaChongqing International Institute for Immunology, Chongqing, People’s Republic of ChinaDepartment of Nephrology, Chinese PLA General Hospital, Chinese PLA Institute of Nephrology, National Key Laboratory of Kidney Diseases, National Clinical Research Center for Kidney Diseases, Beijing, People’s Republic of ChinaSanya People's Hospital, Sanya, People’s Republic of ChinaDepartment of Microbiology and Biochemical Pharmacy, National Engineering Research Center of Immunological Products, College of Pharmacy, Third Military Medical University (Army Medical University), Chongqing, People’s Republic of ChinaInstitute of Immunology, Third Military Medical University (Army Medical University), Chongqing, People’s Republic of ChinaInstitute of Immunology, Third Military Medical University (Army Medical University), Chongqing, People’s Republic of ChinaInfections caused by Acinetobacter baumannii (A. baumannii) have emerged as a global public health concern because of high pathogenicity of this bacterium. Monoclonal antibodies (mAbs) have a lower likelihood of promoting drug resistance and offer targeted treatment, thereby reducing potential adverse effects; however, the therapeutic potential of mAbs targeting A. baumannii has not been fully characterized. In this study, mAbs against the outer membrane proteins (OMPs) of A. baumannii were isolated in a high-throughput manner. The ability of Omp38-specific mAbs to bind to A. baumannii strains from diverse sources was confirmed via enzyme-linked immunosorbent assay (ELISA). Intravenous administration of the Omp38-specific mAbs significantly improved the survival rate and reduced the bacterial load in a mouse model of lethal A. baumannii infection. Flow cytometry and ELISA confirmed that immune cell infiltration and cytokine production, respectively, decreased in a mouse model of sublethal A. baumannii infection. In addition, analysis of the Omp38-mAb C3 binding conformation revealed the potential mechanism of broad-spectrum binding activity of this mAb against A. baumannii. Taken together, these findings indicate that mAbs against Omp38 facilitate bacterial clearance from host, minimize inflammatory mediator release and reduce host damage, highlighting the potential of Omp38-specific mAbs in the clinical treatment of A. baumannii infection.https://www.tandfonline.com/doi/10.1080/22221751.2024.2437243Acinetobacter baumanniiouter membrane proteinmonoclonal antibodyBeacon |
| spellingShingle | Yiwei Zhang Hao Cheng Peng Yu Shufeng Wang Hui Dong Song Lu Ruiqi Yang Baiqing Li Jie Luo Ruihan Mao Zhaohui Zhang Yong Qi Xiaohua Chen Jinya Ding Zemin He Jingbo Zhang Tingting Zhao Xiangmei Chen Rong Lin Haibo Li Yi Tian Yuzhang Wu High-throughput single-cell analysis reveals Omp38-specific monoclonal antibodies that protect against Acinetobacter baumannii infection Emerging Microbes and Infections Acinetobacter baumannii outer membrane protein monoclonal antibody Beacon |
| title | High-throughput single-cell analysis reveals Omp38-specific monoclonal antibodies that protect against Acinetobacter baumannii infection |
| title_full | High-throughput single-cell analysis reveals Omp38-specific monoclonal antibodies that protect against Acinetobacter baumannii infection |
| title_fullStr | High-throughput single-cell analysis reveals Omp38-specific monoclonal antibodies that protect against Acinetobacter baumannii infection |
| title_full_unstemmed | High-throughput single-cell analysis reveals Omp38-specific monoclonal antibodies that protect against Acinetobacter baumannii infection |
| title_short | High-throughput single-cell analysis reveals Omp38-specific monoclonal antibodies that protect against Acinetobacter baumannii infection |
| title_sort | high throughput single cell analysis reveals omp38 specific monoclonal antibodies that protect against acinetobacter baumannii infection |
| topic | Acinetobacter baumannii outer membrane protein monoclonal antibody Beacon |
| url | https://www.tandfonline.com/doi/10.1080/22221751.2024.2437243 |
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