A Horizontally Transferred Alginate Metabolism Gene Cluster in the Human Gut Genus Bacteroides.

IF 1.5 Q4 BIOCHEMISTRY & MOLECULAR BIOLOGY
Journal of applied glycoscience Pub Date : 2025-11-20 eCollection Date: 2025-01-01 DOI:10.5458/jag.7204106
Yuki Miyamoto, Natsuko Katsuhiro, Kenji Okumura, Ryuichi Takase, Daisuke Watanabe, Kohei Ogura, Wataru Hashimoto
{"title":"A Horizontally Transferred Alginate Metabolism Gene Cluster in the Human Gut Genus <i>Bacteroides</i>.","authors":"Yuki Miyamoto, Natsuko Katsuhiro, Kenji Okumura, Ryuichi Takase, Daisuke Watanabe, Kohei Ogura, Wataru Hashimoto","doi":"10.5458/jag.7204106","DOIUrl":null,"url":null,"abstract":"<p><p>Alginate, a heteropolysaccharide composed of α-L-guluronic acid (G) and β-D-mannuronic acid (M), comprises poly-G, poly-M, and mixed poly-MG regions. Alginate lyases, classified within the polysaccharide lyase (PL) family, degrade alginate into unsaturated saccharides via β-elimination. Due to the abundance of alginate in brown algae, various marine bacteria produce alginate lyases for its assimilation. Recently, alginate lyases have also been identified in gut bacteria such as those of the genus <i>Bacteroides</i>. In this study, we purified an alginate lyase from enrichment culture supernatants containing alginate, using a human fecal sample, and isolated <i>B. xylanisolvens</i> strain MK6803, which can grow on alginate as a sole carbon source-unlike the type strain <i>B. xylanisolvens</i> XB1A. Draft genome sequencing of strain MK6803 revealed an alginate-metabolizing gene cluster encoding three alginate lyases belonging to PL6_1, PL17_2, and PL38, along with a putative oxidoreductase. This gene cluster was shared with <i>B. ovatus</i> CP926 and <i>B. xylanisolvens</i> CL11T00C41, but not with the type strain XB1A. <i>Bacteroides</i> species lacking this gene cluster exhibited no alginate assimilation, even if they possessed genes encoding one or more of the three alginate lyases. This suggests that the presence of the putative oxidoreductase, alongside the lyases, is essential for alginate assimilation in <i>Bacteroides</i> species. Phylogenetic analysis indicated horizontal gene transfer within the genus <i>Bacteroides</i>. These findings highlight the role of alginate metabolism in the adaptation of human gut microbiota.</p>","PeriodicalId":14999,"journal":{"name":"Journal of applied glycoscience","volume":"72 4","pages":"7204106"},"PeriodicalIF":1.5000,"publicationDate":"2025-11-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12678894/pdf/","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Journal of applied glycoscience","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.5458/jag.7204106","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"2025/1/1 0:00:00","PubModel":"eCollection","JCR":"Q4","JCRName":"BIOCHEMISTRY & MOLECULAR BIOLOGY","Score":null,"Total":0}
引用次数: 0

Abstract

Alginate, a heteropolysaccharide composed of α-L-guluronic acid (G) and β-D-mannuronic acid (M), comprises poly-G, poly-M, and mixed poly-MG regions. Alginate lyases, classified within the polysaccharide lyase (PL) family, degrade alginate into unsaturated saccharides via β-elimination. Due to the abundance of alginate in brown algae, various marine bacteria produce alginate lyases for its assimilation. Recently, alginate lyases have also been identified in gut bacteria such as those of the genus Bacteroides. In this study, we purified an alginate lyase from enrichment culture supernatants containing alginate, using a human fecal sample, and isolated B. xylanisolvens strain MK6803, which can grow on alginate as a sole carbon source-unlike the type strain B. xylanisolvens XB1A. Draft genome sequencing of strain MK6803 revealed an alginate-metabolizing gene cluster encoding three alginate lyases belonging to PL6_1, PL17_2, and PL38, along with a putative oxidoreductase. This gene cluster was shared with B. ovatus CP926 and B. xylanisolvens CL11T00C41, but not with the type strain XB1A. Bacteroides species lacking this gene cluster exhibited no alginate assimilation, even if they possessed genes encoding one or more of the three alginate lyases. This suggests that the presence of the putative oxidoreductase, alongside the lyases, is essential for alginate assimilation in Bacteroides species. Phylogenetic analysis indicated horizontal gene transfer within the genus Bacteroides. These findings highlight the role of alginate metabolism in the adaptation of human gut microbiota.

人类肠道拟杆菌属水平转移藻酸盐代谢基因簇。
海藻酸盐是由α- l -古鲁醛酸(G)和β- d -甘露醛酸(M)组成的杂多糖,包括聚G区、聚M区和混合聚mg区。海藻酸酯裂解酶属于多糖裂解酶(PL)家族,通过β-消除将海藻酸酯降解为不饱和糖。由于褐藻中含有丰富的海藻酸盐,各种海洋细菌产生海藻酸盐裂解酶对其进行同化。最近,在肠道细菌如拟杆菌属中也发现了海藻酸盐裂解酶。在这项研究中,我们利用人类粪便样本从含有海藻酸盐的富集培养上清中纯化了一种海藻酸盐裂解酶,并分离出了木聚糖溶解B.菌株MK6803,它可以以海藻酸盐作为唯一的碳源生长,而不像B. xylanisolvens型菌株XB1A。菌株MK6803的初步基因组测序显示了一个海藻酸代谢基因簇,该基因簇编码三种海藻酸裂解酶,分别为PL6_1, PL17_2和PL38,以及一个推定的氧化还原酶。该基因簇与卵形双歧杆菌CP926和溶木双歧杆菌CL11T00C41共有,而与型菌株XB1A不共有。缺乏这一基因簇的拟杆菌类即使拥有编码三种海藻酸分解酶中的一种或多种的基因,也没有表现出海藻酸盐的同化。这表明,假定的氧化还原酶的存在,以及裂解酶,是必不可少的海藻酸盐同化在拟杆菌种。系统发育分析表明拟杆菌属内存在水平基因转移。这些发现强调了海藻酸盐代谢在人类肠道微生物群适应中的作用。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
求助全文
约1分钟内获得全文 求助全文
来源期刊
Journal of applied glycoscience
Journal of applied glycoscience BIOCHEMISTRY & MOLECULAR BIOLOGY-
自引率
9.10%
发文量
13
×
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:604180095
Book学术官方微信
小红书