Adhesion properties of a putative polymorphic fimbrial subunit protein from Bifidobacterium longum subsp. longum

In our previous study, we found that the open reading frame bl0675 in the genome of Bifidobacterium longum subsp. longum isolated from human feces encoded a novel putative fimbrial protein, was highly polymorphic, and had five variants (A, B, C, D, and E types). The aim of this study was to evaluate...

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Main Authors:	SUZUKI, Kenta, NISHIYAMA, Keita, MIYAJIMA, Hiroki, OSAWA, Ro, YAMAMOTO, Yuji, MUKAI, Takao
Format:	Online
Language:	English
Published:	BMFH Press 2015
Online Access:	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4735030/

id	pubmed-4735030
recordtype	oai_dc
spelling	pubmed-47350302016-02-08 Adhesion properties of a putative polymorphic fimbrial subunit protein from Bifidobacterium longum subsp. longum SUZUKI, Kenta NISHIYAMA, Keita MIYAJIMA, Hiroki OSAWA, Ro YAMAMOTO, Yuji MUKAI, Takao Full Paper In our previous study, we found that the open reading frame bl0675 in the genome of Bifidobacterium longum subsp. longum isolated from human feces encoded a novel putative fimbrial protein, was highly polymorphic, and had five variants (A, B, C, D, and E types). The aim of this study was to evaluate the affinity of these variants to porcine colonic mucins (PCMs). Protein-binding properties were examined using the recombinant BL0675 protein containing a C-terminal 6 × His tag (His-BL0675). Surface plasmon resonance analysis demonstrated that the His-BL0675 A type had strong affinity to PCMs (KD = 9.82 × 10−8 M), whereas the B, C, D, and E types exhibited little or no binding. In a competitive enzyme-linked immunosorbent assay, His-BL0675 A type binding was reduced by addition of mucin oligosaccharides, suggesting that the binding occurs via carbohydrate chains of PCMs. The localization of BL0675 to the B. longum subsp. longum cell surface was confirmed by western blot analysis using A type polyclonal antibodies. Bacterial adhesion of B. longum subsp. longum to PCMs was also blocked by A type-specific antibodies; however, its adhesion properties were strain specific. Our results suggest that the BL0675 variants significantly contribute to the adhesion of B. longum subsp. longum strains. The expression and the adhesive properties of this protein are affected by genetic polymorphisms and are specific for B. longum subsp. longum strains. However, further studies are required on the properties of binding of these putative fimbrial proteins to the human gastrointestinal tract. BMFH Press 2015-09-26 2016 /pmc/articles/PMC4735030/ /pubmed/26858927 http://dx.doi.org/10.12938/bmfh.2015-015 Text en BMFH Press http://creativecommons.org/licenses/by-nc-nd/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution Non-Commercial No Derivatives (by-nc-nd) License.
repository_type	Open Access Journal
institution_category	Foreign Institution
institution	US National Center for Biotechnology Information
building	NCBI PubMed
collection	Online Access
language	English
format	Online
author	SUZUKI, Kenta NISHIYAMA, Keita MIYAJIMA, Hiroki OSAWA, Ro YAMAMOTO, Yuji MUKAI, Takao
spellingShingle	SUZUKI, Kenta NISHIYAMA, Keita MIYAJIMA, Hiroki OSAWA, Ro YAMAMOTO, Yuji MUKAI, Takao Adhesion properties of a putative polymorphic fimbrial subunit protein from Bifidobacterium longum subsp. longum
author_facet	SUZUKI, Kenta NISHIYAMA, Keita MIYAJIMA, Hiroki OSAWA, Ro YAMAMOTO, Yuji MUKAI, Takao
author_sort	SUZUKI, Kenta
title	Adhesion properties of a putative polymorphic fimbrial subunit protein from Bifidobacterium longum subsp. longum
title_short	Adhesion properties of a putative polymorphic fimbrial subunit protein from Bifidobacterium longum subsp. longum
title_full	Adhesion properties of a putative polymorphic fimbrial subunit protein from Bifidobacterium longum subsp. longum
title_fullStr	Adhesion properties of a putative polymorphic fimbrial subunit protein from Bifidobacterium longum subsp. longum
title_full_unstemmed	Adhesion properties of a putative polymorphic fimbrial subunit protein from Bifidobacterium longum subsp. longum
title_sort	adhesion properties of a putative polymorphic fimbrial subunit protein from bifidobacterium longum subsp. longum
description	In our previous study, we found that the open reading frame bl0675 in the genome of Bifidobacterium longum subsp. longum isolated from human feces encoded a novel putative fimbrial protein, was highly polymorphic, and had five variants (A, B, C, D, and E types). The aim of this study was to evaluate the affinity of these variants to porcine colonic mucins (PCMs). Protein-binding properties were examined using the recombinant BL0675 protein containing a C-terminal 6 × His tag (His-BL0675). Surface plasmon resonance analysis demonstrated that the His-BL0675 A type had strong affinity to PCMs (KD = 9.82 × 10−8 M), whereas the B, C, D, and E types exhibited little or no binding. In a competitive enzyme-linked immunosorbent assay, His-BL0675 A type binding was reduced by addition of mucin oligosaccharides, suggesting that the binding occurs via carbohydrate chains of PCMs. The localization of BL0675 to the B. longum subsp. longum cell surface was confirmed by western blot analysis using A type polyclonal antibodies. Bacterial adhesion of B. longum subsp. longum to PCMs was also blocked by A type-specific antibodies; however, its adhesion properties were strain specific. Our results suggest that the BL0675 variants significantly contribute to the adhesion of B. longum subsp. longum strains. The expression and the adhesive properties of this protein are affected by genetic polymorphisms and are specific for B. longum subsp. longum strains. However, further studies are required on the properties of binding of these putative fimbrial proteins to the human gastrointestinal tract.
publisher	BMFH Press
publishDate	2015
url	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4735030/
_version_	1613531227285880832

Adhesion properties of a putative polymorphic fimbrial subunit protein from Bifidobacterium longum subsp. longum

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