Artikel: Understanding the adhesion mechanism of a mucin binding domain from Lactobacillus fermentum and its role in enteropathogen exclusion
International journal of biological macromolecules. 2017,
2017
Abstract: Lactobacillus species possesses surface exposed Mucin Binding Protein (MucBP) which plays a role in adhesion to gastrointestinal mucin. MucBP contains one or more mucin binding domain (MBD), the functionality of which has yet not been characterized ... ...
| Abstract | Lactobacillus species possesses surface exposed Mucin Binding Protein (MucBP) which plays a role in adhesion to gastrointestinal mucin. MucBP contains one or more mucin binding domain (MBD), the functionality of which has yet not been characterized thoroughly. Here, we have characterized a 93-amino acid MBD (MBD93) of MucBP (LAF_0673) from Lactobacillus fermentum. Multiple sequence alignment of L. fermentum MBD93 exhibited â¼60% sequence homology with MBDs from other Lactobacillus species. Further, we cloned, expressed and purified MBD93 from Escherichia coli as N-terminal histidine-tagged protein (6X His-MBD93). The purified MBD93 was able to bind to mucin and showed strong affinity towards the terminally expressed mucin glycans viz. N-acetylgalactosamine (GalNAc), N-acetylglucosamine (GlcNAc), Galactose (Gal), and Sialic acid (N-acetylneuraminic acid; Neu5Ac). In silico experiments further confirmed the interaction between homology modeled MBD93 to mucin glycans through hydrogen-bonding with its surface amino acid residues Ser57, Pro58, Ile60, Tyr63 and Ala65. We also have demonstrated that MBD93 was able to inhibit the adhesion of enteric pathogens, including E. coli, Salmonella Paratyphi A, Shigella sonnei and Proteus vulgaris to mucin. Our results suggested that L. fermentum MBD93 is a functionally sufficient unit to act as an adhesin and to protect from invading enteric pathogens. |
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| Schlagwörter | adhesins ; adhesion ; amino acids ; binding proteins ; enteropathogens ; Escherichia coli ; galactose ; gastrointestinal system ; hydrogen bonding ; Lactobacillus fermentum ; mucins ; N-acetylglucosamine ; polysaccharides ; Proteus vulgaris ; Salmonella Paratyphi A ; sequence alignment ; sequence homology ; Shigella sonnei ; sialic acid | |||||
| Sprache | Englisch | |||||
| Umfang | p. . | |||||
| Erscheinungsort | Elsevier B.V. | |||||
| Dokumenttyp | Artikel | |||||
| Anmerkung | Pre-press version | |||||
| ZDB-ID | 282732-3 | |||||
| ISSN | 1879-0003 ; 0141-8130 | |||||
| ISSN (online) | 1879-0003 | |||||
| ISSN | 0141-8130 | |||||
| DOI | 10.1016/j.ijbiomac.2017.10.107 | |||||
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| Datenquelle | NAL Katalog (AGRICOLA) |
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