Identification of WxL and S-Layer Proteins from <i>Lactobacillus brevis</i> with the Ability to Bind Cellulose and Xylan
Xylanase releases xylo-oligosaccharides from dietary xylan, which stimulate the growth of the gut bacteria lactobacilli. Many lactobacilli adhere to dietary fibers, which may facilitate the assimilation of xylo-oligosaccharides and help them gain competence in the gut, but the underlying mechanisms...
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MDPI AG
2022-04-01
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| Series: | International Journal of Molecular Sciences |
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| Online Access: | https://www.mdpi.com/1422-0067/23/8/4136 |
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| author | Zhenzhen Hao Wenjing Zhang Xiaolu Wang Yuan Wang Xing Qin Huiying Luo Huoqing Huang Xiaoyun Su |
| author_facet | Zhenzhen Hao Wenjing Zhang Xiaolu Wang Yuan Wang Xing Qin Huiying Luo Huoqing Huang Xiaoyun Su |
| author_sort | Zhenzhen Hao |
| collection | DOAJ |
| description | Xylanase releases xylo-oligosaccharides from dietary xylan, which stimulate the growth of the gut bacteria lactobacilli. Many lactobacilli adhere to dietary fibers, which may facilitate the assimilation of xylo-oligosaccharides and help them gain competence in the gut, but the underlying mechanisms remain elusive. Herein we report, from the highly abundant transcripts of <i>Lactobacillus brevis</i> cultured in wheat arabinoxylan supplemented with a xylanase, the identification of genes encoding four putative cell-surface WxL proteins (Lb630, Lb631, Lb632, and Lb635) and one S-layer protein (Lb1325) with either cellulose- or xylan-binding ability. The repetitively occurring WxL proteins were encoded by a gene cluster, among which Lb630 was chosen for further mutational studies. The analysis revealed three aromatic residues (F30, W61, and W156) that might be involved in the interaction of the protein with cellulose. A homology search in the genome of <i>Enterococcus faecium</i> identified three WxL proteins with conserved counterparts of these three aromatic residues, and they were also found to be able to bind cellulose and xylan. The findings suggested a role of the cell-surface WxL and S-layer proteins in assisting the cellular adhesion of <i>L. brevis</i> to plant cell wall polysaccharides. |
| first_indexed | 2024-03-09T13:34:15Z |
| format | Article |
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| institution | Directory Open Access Journal |
| issn | 1661-6596 1422-0067 |
| language | English |
| last_indexed | 2024-03-09T13:34:15Z |
| publishDate | 2022-04-01 |
| publisher | MDPI AG |
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| series | International Journal of Molecular Sciences |
| spelling | doaj.art-6ecbeb58776e4a64a454bef49aa642ce2023-11-30T21:14:19ZengMDPI AGInternational Journal of Molecular Sciences1661-65961422-00672022-04-01238413610.3390/ijms23084136Identification of WxL and S-Layer Proteins from <i>Lactobacillus brevis</i> with the Ability to Bind Cellulose and XylanZhenzhen Hao0Wenjing Zhang1Xiaolu Wang2Yuan Wang3Xing Qin4Huiying Luo5Huoqing Huang6Xiaoyun Su7State Key Laboratory of Animal Nutrition, Institute of Animal Sciences, Chinese Academy of Agricultural Sciences, Beijing 100193, ChinaState Key Laboratory of Animal Nutrition, Institute of Animal Sciences, Chinese Academy of Agricultural Sciences, Beijing 100193, ChinaState Key Laboratory of Animal Nutrition, Institute of Animal Sciences, Chinese Academy of Agricultural Sciences, Beijing 100193, ChinaState Key Laboratory of Animal Nutrition, Institute of Animal Sciences, Chinese Academy of Agricultural Sciences, Beijing 100193, ChinaState Key Laboratory of Animal Nutrition, Institute of Animal Sciences, Chinese Academy of Agricultural Sciences, Beijing 100193, ChinaState Key Laboratory of Animal Nutrition, Institute of Animal Sciences, Chinese Academy of Agricultural Sciences, Beijing 100193, ChinaState Key Laboratory of Animal Nutrition, Institute of Animal Sciences, Chinese Academy of Agricultural Sciences, Beijing 100193, ChinaState Key Laboratory of Animal Nutrition, Institute of Animal Sciences, Chinese Academy of Agricultural Sciences, Beijing 100193, ChinaXylanase releases xylo-oligosaccharides from dietary xylan, which stimulate the growth of the gut bacteria lactobacilli. Many lactobacilli adhere to dietary fibers, which may facilitate the assimilation of xylo-oligosaccharides and help them gain competence in the gut, but the underlying mechanisms remain elusive. Herein we report, from the highly abundant transcripts of <i>Lactobacillus brevis</i> cultured in wheat arabinoxylan supplemented with a xylanase, the identification of genes encoding four putative cell-surface WxL proteins (Lb630, Lb631, Lb632, and Lb635) and one S-layer protein (Lb1325) with either cellulose- or xylan-binding ability. The repetitively occurring WxL proteins were encoded by a gene cluster, among which Lb630 was chosen for further mutational studies. The analysis revealed three aromatic residues (F30, W61, and W156) that might be involved in the interaction of the protein with cellulose. A homology search in the genome of <i>Enterococcus faecium</i> identified three WxL proteins with conserved counterparts of these three aromatic residues, and they were also found to be able to bind cellulose and xylan. The findings suggested a role of the cell-surface WxL and S-layer proteins in assisting the cellular adhesion of <i>L. brevis</i> to plant cell wall polysaccharides.https://www.mdpi.com/1422-0067/23/8/4136gut bacteria<i>Lactobacillus brevis</i>WxL proteinS-layer proteinxylanasecell adhesion |
| spellingShingle | Zhenzhen Hao Wenjing Zhang Xiaolu Wang Yuan Wang Xing Qin Huiying Luo Huoqing Huang Xiaoyun Su Identification of WxL and S-Layer Proteins from <i>Lactobacillus brevis</i> with the Ability to Bind Cellulose and Xylan International Journal of Molecular Sciences gut bacteria <i>Lactobacillus brevis</i> WxL protein S-layer protein xylanase cell adhesion |
| title | Identification of WxL and S-Layer Proteins from <i>Lactobacillus brevis</i> with the Ability to Bind Cellulose and Xylan |
| title_full | Identification of WxL and S-Layer Proteins from <i>Lactobacillus brevis</i> with the Ability to Bind Cellulose and Xylan |
| title_fullStr | Identification of WxL and S-Layer Proteins from <i>Lactobacillus brevis</i> with the Ability to Bind Cellulose and Xylan |
| title_full_unstemmed | Identification of WxL and S-Layer Proteins from <i>Lactobacillus brevis</i> with the Ability to Bind Cellulose and Xylan |
| title_short | Identification of WxL and S-Layer Proteins from <i>Lactobacillus brevis</i> with the Ability to Bind Cellulose and Xylan |
| title_sort | identification of wxl and s layer proteins from i lactobacillus brevis i with the ability to bind cellulose and xylan |
| topic | gut bacteria <i>Lactobacillus brevis</i> WxL protein S-layer protein xylanase cell adhesion |
| url | https://www.mdpi.com/1422-0067/23/8/4136 |
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