通过磷酸胆碱介导的相互作用,单克隆 IgA(TEPC15-IgA)对肠道细菌具有广泛的特异性。

IF 1.1 4区 农林科学 Q3 VETERINARY SCIENCES
Journal of Veterinary Medical Science Pub Date : 2024-07-02 Epub Date: 2024-06-04 DOI:10.1292/jvms.23-0441
Saeka Koyama, Kaori Ito, Katsuki Usami, Shino Wada, Tsukasa Yamashita, Wakako Ikeda-Ohtsubo, Haruki Kitazawa, Ryota Hirakawa, Jahidul Islam, Mutsumi Furukawa, Tomonori Nochi
{"title":"通过磷酸胆碱介导的相互作用,单克隆 IgA(TEPC15-IgA)对肠道细菌具有广泛的特异性。","authors":"Saeka Koyama, Kaori Ito, Katsuki Usami, Shino Wada, Tsukasa Yamashita, Wakako Ikeda-Ohtsubo, Haruki Kitazawa, Ryota Hirakawa, Jahidul Islam, Mutsumi Furukawa, Tomonori Nochi","doi":"10.1292/jvms.23-0441","DOIUrl":null,"url":null,"abstract":"<p><p>Immunoglobulin A (IgA) is notable for its broad specificity toward multiple bacteria. Phosphorylcholine (PC) plays a role in the infection of pathogenic bacteria carrying PC and in the induction of IgA responses in the host immune system. The commercially available mouse monoclonal IgA, TEPC15-IgA, is a distinctive antibody with specificity for PC, warranting further exploration of its response to PC-bearing enteric bacteria. In this study, using 17 different enteric bacteria, including 3 aerobic and 14 anerobic bacteria that could be cultured in vitro, we confirmed that TEPC15-IgA recognizes 4 bacterial species: Lactobacillus taiwanensis, Limosilactobacillus frumenti, Streptococcus infantis, and Escherichia coli, although reactivity varied. Interestingly, TEPC15-IgA did not react with four of six Lactobacillus species used. Moreover, distinct target molecules associated with PC in L. taiwanensis and L. frumenti were evident, differing in molecular weight. These findings suggest that the natural generation of PC-specific IgA could prevent PC-mediated infections and potentially facilitate the formation of a microflora rich in indigenous bacteria with PC, particularly in the gastrointestinal tract.</p>","PeriodicalId":49959,"journal":{"name":"Journal of Veterinary Medical Science","volume":null,"pages":null},"PeriodicalIF":1.1000,"publicationDate":"2024-07-02","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11251817/pdf/","citationCount":"0","resultStr":"{\"title\":\"Broad specificity of monoclonal IgA (TEPC15-IgA) for enteric bacteria via phosphorylcholine-mediated interaction.\",\"authors\":\"Saeka Koyama, Kaori Ito, Katsuki Usami, Shino Wada, Tsukasa Yamashita, Wakako Ikeda-Ohtsubo, Haruki Kitazawa, Ryota Hirakawa, Jahidul Islam, Mutsumi Furukawa, Tomonori Nochi\",\"doi\":\"10.1292/jvms.23-0441\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>Immunoglobulin A (IgA) is notable for its broad specificity toward multiple bacteria. Phosphorylcholine (PC) plays a role in the infection of pathogenic bacteria carrying PC and in the induction of IgA responses in the host immune system. The commercially available mouse monoclonal IgA, TEPC15-IgA, is a distinctive antibody with specificity for PC, warranting further exploration of its response to PC-bearing enteric bacteria. In this study, using 17 different enteric bacteria, including 3 aerobic and 14 anerobic bacteria that could be cultured in vitro, we confirmed that TEPC15-IgA recognizes 4 bacterial species: Lactobacillus taiwanensis, Limosilactobacillus frumenti, Streptococcus infantis, and Escherichia coli, although reactivity varied. Interestingly, TEPC15-IgA did not react with four of six Lactobacillus species used. Moreover, distinct target molecules associated with PC in L. taiwanensis and L. frumenti were evident, differing in molecular weight. These findings suggest that the natural generation of PC-specific IgA could prevent PC-mediated infections and potentially facilitate the formation of a microflora rich in indigenous bacteria with PC, particularly in the gastrointestinal tract.</p>\",\"PeriodicalId\":49959,\"journal\":{\"name\":\"Journal of Veterinary Medical Science\",\"volume\":null,\"pages\":null},\"PeriodicalIF\":1.1000,\"publicationDate\":\"2024-07-02\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11251817/pdf/\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Journal of Veterinary Medical Science\",\"FirstCategoryId\":\"97\",\"ListUrlMain\":\"https://doi.org/10.1292/jvms.23-0441\",\"RegionNum\":4,\"RegionCategory\":\"农林科学\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"2024/6/4 0:00:00\",\"PubModel\":\"Epub\",\"JCR\":\"Q3\",\"JCRName\":\"VETERINARY SCIENCES\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Journal of Veterinary Medical Science","FirstCategoryId":"97","ListUrlMain":"https://doi.org/10.1292/jvms.23-0441","RegionNum":4,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"2024/6/4 0:00:00","PubModel":"Epub","JCR":"Q3","JCRName":"VETERINARY SCIENCES","Score":null,"Total":0}
引用次数: 0

摘要

免疫球蛋白 A(IgA)对多种细菌具有广泛的特异性。磷酰胆碱(PC)在携带 PC 的病原菌感染和诱导宿主免疫系统产生 IgA 反应中发挥着作用。市售的小鼠单克隆 IgA TEPC15-IgA 是一种对 PC 具有特异性的独特抗体,因此有必要进一步研究它对携带 PC 的肠道细菌的反应。在本研究中,我们利用 17 种不同的肠道细菌(包括 3 种需氧菌和 14 种厌氧菌)进行体外培养,证实 TEPC15-IgA 可识别 4 种细菌:我们证实 TEPC15-IgA 可识别 4 种细菌:台湾乳杆菌、弗鲁门蒂嗜酸乳杆菌、婴儿链球菌和大肠杆菌,但反应性各不相同。有趣的是,TEPC15-IgA 与六种乳酸杆菌中的四种没有反应。此外,在台湾乳杆菌和弗氏乳杆菌中,与 PC 相关的不同靶分子也很明显,它们的分子量各不相同。这些研究结果表明,自然产生的 PC 特异性 IgA 可以预防 PC 介导的感染,并有可能促进富含 PC 的本地细菌的微生物区系的形成,尤其是在胃肠道。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
Broad specificity of monoclonal IgA (TEPC15-IgA) for enteric bacteria via phosphorylcholine-mediated interaction.

Immunoglobulin A (IgA) is notable for its broad specificity toward multiple bacteria. Phosphorylcholine (PC) plays a role in the infection of pathogenic bacteria carrying PC and in the induction of IgA responses in the host immune system. The commercially available mouse monoclonal IgA, TEPC15-IgA, is a distinctive antibody with specificity for PC, warranting further exploration of its response to PC-bearing enteric bacteria. In this study, using 17 different enteric bacteria, including 3 aerobic and 14 anerobic bacteria that could be cultured in vitro, we confirmed that TEPC15-IgA recognizes 4 bacterial species: Lactobacillus taiwanensis, Limosilactobacillus frumenti, Streptococcus infantis, and Escherichia coli, although reactivity varied. Interestingly, TEPC15-IgA did not react with four of six Lactobacillus species used. Moreover, distinct target molecules associated with PC in L. taiwanensis and L. frumenti were evident, differing in molecular weight. These findings suggest that the natural generation of PC-specific IgA could prevent PC-mediated infections and potentially facilitate the formation of a microflora rich in indigenous bacteria with PC, particularly in the gastrointestinal tract.

求助全文
通过发布文献求助,成功后即可免费获取论文全文。 去求助
来源期刊
Journal of Veterinary Medical Science
Journal of Veterinary Medical Science 农林科学-兽医学
CiteScore
2.30
自引率
8.30%
发文量
230
审稿时长
9-18 weeks
期刊介绍: JVMS is a peer-reviewed journal and publishes a variety of papers on veterinary science from basic research to applied science and clinical research. JVMS is published monthly and consists of twelve issues per year. Papers are from the areas of anatomy, physiology, pharmacology, toxicology, pathology, immunology, microbiology, virology, parasitology, internal medicine, surgery, clinical pathology, theriogenology, avian disease, public health, ethology, and laboratory animal science. Although JVMS has played a role in publishing the scientific achievements of Japanese researchers and clinicians for many years, it now also accepts papers submitted from all over the world.
×
引用
GB/T 7714-2015
复制
MLA
复制
APA
复制
导出至
BibTeX EndNote RefMan NoteFirst NoteExpress
×
提示
您的信息不完整,为了账户安全,请先补充。
现在去补充
×
提示
您因"违规操作"
具体请查看互助需知
我知道了
×
提示
确定
请完成安全验证×
copy
已复制链接
快去分享给好友吧!
我知道了
右上角分享
点击右上角分享
0
联系我们:info@booksci.cn Book学术提供免费学术资源搜索服务,方便国内外学者检索中英文文献。致力于提供最便捷和优质的服务体验。 Copyright © 2023 布克学术 All rights reserved.
京ICP备2023020795号-1
ghs 京公网安备 11010802042870号
Book学术文献互助
Book学术文献互助群
群 号:481959085
Book学术官方微信