生物信息学辅助探索人类肠道副杆菌 GH29 粘多糖酶的功能。

IF 3.4 3区 生物学 Q2 BIOCHEMISTRY & MOLECULAR BIOLOGY
Haiyang Wu, Qingxin Li, Jin Chuan Wu
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引用次数: 0

摘要

肠道微生物产生的α-l-岩藻糖苷酶对利用人乳寡糖、粘膜糖和膳食糖至关重要。尽管肠道副杆菌因其对宿主健康和疾病的影响而备受关注,但对其 CAZymes 的研究仍然很少。对 11 株肠道副杆菌属类型菌株的 CAZome 分析表明,它们具有降解粘蛋白 O 型聚糖的能力。它们丰富的 GH29 褐藻糖苷酶引起了我们的注意,我们利用硅学方法预测了 46 种 GH29 褐藻糖苷酶的功能特征。我们的研究结果显示了不同的连接特异性和物种特异性分布,其中一半以上的GH29酶作为α1,3/4岩藻糖苷酶发挥作用,这对于作用于粘蛋白O型糖的路易斯抗原表位至关重要。我们进一步通过酶切验证了 4 个来自特征不明显群体的新型 GH29 序列。PgoldGH29A(cluster37 GH29BERT,GH29:75.1 CUPP)不作用于测试的天然底物。PgoldGH29B(cluster1 GH29BERT,GH29:84.1 CUPP)作为严格的α1,3/4岩藻糖苷酶发挥作用。PgoldGH29C(cluster14 GH29BERT,GH29:29.1 CUPP)对α1,2/3/4 二糖具有前所未有的底物特异性。PgoldGH29D(cluster4 GH29BERT,GH29:6.2 CUPP)对α1,2/3/4/6连接的作用类似于来自 GH29:6.1 CUPP 的酶,但更喜欢二糖而不是三糖。这些结果表明,PgoldGH29B和PgoldGH29D可分别通过其α1,3/4和α1,2岩藻糖苷酶活性促进粘蛋白O-糖的降解,而PgoldGH29A和PgoldGH29C的天然底物可能与宿主糖无关。这些发现加深了我们对肠道副杆菌栖息的生态位的了解,并可能指导我们对其他有趣的肠道微生物物种进行类似的探索。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
Bioinformatics-aided function exploration of GH29 fucosidases from human gut Parabacteroides.

Gut microbes produce α-l-fucosidases critical for utilizing human milk oligosaccharides, mucosal and dietary glycans. Although gut Parabacteroides have garnered attention for their impact on host health and disease, their CAZymes remain poorly studied. CAZome analysis of eleven gut Parabacteroides type strains revealed their capacity to degrade mucin O-glycans. Their abundance of GH29 fucosidases caught our attention, and we predicted the functional profiles of 46 GH29 fucosidases using in silico approaches. Our findings showed diverse linkages specificities and species-specific distributions, with over half of GH29 enzymes functioning as α1,3/4 fucosidases, essential for acting on Lewis antigen epitopes of mucin O-glycans. We further enzymatically validated 4 novel GH29 sequences from poorly characterized groups. PgoldGH29A (cluster37 GH29BERT, GH29:75.1 CUPP) does not act on tested natural substrates. PgoldGH29B (cluster1 GH29BERT, GH29:84.1 CUPP) functions as a strict α1,3/4 fucosidase. PgoldGH29C (cluster14 GH29BERT, GH29:29.1 CUPP) displays unprecedented substrate specificity for α1,2/3/4 disaccharides. PgoldGH29D (cluster4 GH29BERT, GH29:6.2 CUPP) acts on α1,2/3/4/6 linkages similar to enzymes from GH29:6.1 CUPP but prefers disaccharides over trisaccharides. These results suggest that PgoldGH29B and PgoldGH29D can contribute to mucin O-glycan degradation via their α1,3/4 and α1,2 fucosidase activity, respectively, while the natural substrates of PgoldGH29A and PgoldGH29C may be irrelevant to host-glycans. These insights enhance our understanding of the ecological niches inhabited by gut Parabacteroides and may guide similar exploration in other intriguing gut microbial species.

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来源期刊
Glycobiology
Glycobiology 生物-生化与分子生物学
CiteScore
7.50
自引率
4.70%
发文量
73
审稿时长
3 months
期刊介绍: Established as the leading journal in the field, Glycobiology provides a unique forum dedicated to research into the biological functions of glycans, including glycoproteins, glycolipids, proteoglycans and free oligosaccharides, and on proteins that specifically interact with glycans (including lectins, glycosyltransferases, and glycosidases). Glycobiology is essential reading for researchers in biomedicine, basic science, and the biotechnology industries. By providing a single forum, the journal aims to improve communication between glycobiologists working in different disciplines and to increase the overall visibility of the field.
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