Insights into physiological traits of Bifidobacterium animalis subsp. lactis BB-12 through membrane proteome analysis

Gilad, Ofir; Hjernø, Karin; Østerlund, Eva Christina; Margollés, Abelardo; Svensson, Birte; Stuer‐Lauridsen, Birgitte; Møller, Anders Hauer; Jacobsen, Susanne

doi:10.1016/j.jprot.2011.10.031

Cited by 11 publications

(7 citation statements)

References 43 publications

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“…In addition, part of an oligosaccharide ATP-binding cassette (ABC) transporter encoding a solute-binding protein (SBP) (Balac_1565), and an ATP-binding protein associated with oligosaccharide uptake by ABC transporters (Balac_1610) were both found, linking catabolic adaptation to the primary physiological functions of B. lactis Bl-04. These findings correlate with previously proposed molecular functions related to probiotic mechanisms in B. lactis [29]. …”

Section: Resultssupporting

confidence: 91%

Transcriptional analysis of oligosaccharide utilization by Bifidobacterium lactisBl-04

et al. 2013

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BackgroundProbiotic bifidobacteria in combination with prebiotic carbohydrates have documented positive effects on human health regarding gastrointestinal disorders and improved immunity, however the selective routes of uptake remain unknown for most candidate prebiotics. The differential transcriptomes of Bifidobacterium animalis subsp. lactis Bl-04, induced by 11 potential prebiotic oligosaccharides were analyzed to identify the genetic loci involved in the uptake and catabolism of α- and β-linked hexoses, and β-xylosides.ResultsThe overall transcriptome was modulated dependent on the type of glycoside (galactosides, glucosides or xylosides) utilized. Carbohydrate transporters of the major facilitator superfamily (induced by gentiobiose and β-galacto-oligosaccharides (GOS)) and ATP-binding cassette (ABC) transporters (upregulated by cellobiose, GOS, isomaltose, maltotriose, melibiose, panose, raffinose, stachyose, xylobiose and β-xylo-oligosaccharides) were differentially upregulated, together with glycoside hydrolases from families 1, 2, 13, 36, 42, 43 and 77. Sequence analysis of the identified solute-binding proteins that determine the specificity of ABC transporters revealed similarities in the breadth and selectivity of prebiotic utilization by bifidobacteria.ConclusionThis study identified the differential gene expression for utilization of potential prebiotics highlighting the extensive capabilities of Bifidobacterium lactis Bl-04 to utilize oligosaccharides. Results provide insights into the ability of this probiotic microbe to utilize indigestible carbohydrates in the human gastrointestinal tract.

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Section: Resultssupporting

confidence: 91%

Transcriptional analysis of oligosaccharide utilization by Bifidobacterium lactisBl-04

et al. 2013

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“…Thus, membrane proteins are indispensable for adaptation and survival in the environment [33]. Additionally, membrane proteins are significant in the course of infection for direct contact with host cells [12,34].…”

Section: Resultsmentioning

confidence: 99%

Comparative proteomic analysis of the membrane proteins of two Haemophilus parasuis strains to identify proteins that may help in habitat adaptation and pathogenesis

et al. 2014

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BackgroundHaemophilus parasuis is the causative agent of Glässer’s disease characterized by polyserositis, arthritis, and meningitis in pig, leading to serious economic loss. Despite many years of study, virulence factors and the mechanisms of the entire infection process remain largely unclear. So two-dimensional gel electrophoresis and mass spectrometry were used to search for distinctions at the membrane protein expression level between two H. parasuis isolates aimed at uncovering some proteins potentially involved in habitat adaption and pathogenesis.ResultsA comparative proteomic approach combining two-dimensional gel electrophoresis with mass spectrometry and tandem mass spectrometry was employed to explore the differences among membrane proteomes of a virulent Haemophilus parasuis strain isolated from the lung of a diseased pig and an avirulent strain isolated from the nasal swab of a healthy pig. Differentially expressed protein spots identified by mass spectrometry were annotated and analyzed by bioinformatic interpretation. The mRNA level was determined by quantitative real-time PCR. Proteins representing diverse functional activities were identified. Among them, the tonB-dependent siderophore receptor was a new discovery highlighted for its activity in iron uptake. In addition, periplasmic serine protease and putrescine/spermidine ABC transporter substrate-binding protein were given focus because of their virulence potential. This study revealed that the differentially expressed proteins were important in either the habitat adaption or pathogenesis of H. parasuis.ConclusionsThe outcome demonstrated the presence of some proteins which raise the speculation for their importance in helping in habitat adaption or pathogenesis within the host.

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“…BXA43 hydrolysed X 2 , X 3 , and X 4 in line with a suggested model for XOS utilisation in BB-12 that includes uptake via an ATP binding cassette (ABC) oligosaccharide transport system whose components were identified in the secreted (secretome) and the membrane proteomes of BB-12 grown on XOS; BB-12 is incapable of growing on xylose as the sole carbon source (Gilad et al 2011; 2012). While an increasing specific activity for X 2 , X 3 , and X 4 (Table 1) is seen for BXA43, this was not reported for GbtXyl43A from G. thermoleovorans IT-08 (Wagschal et al 2009b) and deAX from an uncultured bacterium (Wagschal et al 2009a) which both belong to group IV and have the highest specific activity on X 2 or X 3 , respectively.…”

Section: Discussionmentioning

confidence: 70%

Biochemical and kinetic characterisation of a novel xylooligosaccharide-upregulated GH43 β-d-xylosidase/α-l-arabinofuranosidase (BXA43) from the probiotic Bifidobacterium animalis subsp. lactis BB-12

et al. 2013

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The Bifidobacterium animalis subsp. lactis BB-12 gene BIF_00092, assigned to encode a β-d-xylosidase (BXA43) of glycoside hydrolase family 43 (GH43), was cloned with a C-terminal His-tag and expressed in Escherichia coli. BXA43 was purified to homogeneity from the cell lysate and found to be a dual-specificity exo-hydrolase active on para-nitrophenyl-β-d-xylopyranoside (pNPX), para-nitrophenyl-α-L-arabinofuranoside (pNPA), β-(1 → 4)-xylopyranosyl oligomers (XOS) of degree of polymerisation (DP) 2–4, and birchwood xylan. A phylogenetic tree of the 92 characterised GH43 enzymes displayed five distinct groups (I − V) showing specificity differences. BXA43 belonged to group IV and had an activity ratio for pNPA:pNPX of 1:25. BXA43 was stable below 40°C and at pH 4.0–8.0 and showed maximum activity at pH 5.5 and 50°C. Km and kcat for pNPX were 15.6 ± 4.2 mM and 60.6 ± 10.8 s-1, respectively, and substrate inhibition became apparent above 18 mM pNPX. Similar kinetic parameters and catalytic efficiency values were reported for β-d-xylosidase (XynB3) from Geobacillus stearothermophilus T‒6 also belonging to group IV. The activity of BXA43 for xylooligosaccharides increased with the size and was 2.3 and 5.6 fold higher, respectively for xylobiose and xylotetraose compared to pNPX. BXA43 showed clearly metal inhibition for Zn2+ and Ag+, which is different to its close homologues. Multiple sequence alignment and homology modelling indicated that Arg505Tyr506 present in BXA43 are probably important for binding to xylotetraose at subsite +3 and occur only in GH43 from the Bifidobacterium genus.

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Insights into physiological traits of Bifidobacterium animalis subsp. lactis BB-12 through membrane proteome analysis

Cited by 11 publications

References 43 publications

Transcriptional analysis of oligosaccharide utilization by Bifidobacterium lactisBl-04

Transcriptional analysis of oligosaccharide utilization by Bifidobacterium lactisBl-04

Comparative proteomic analysis of the membrane proteins of two Haemophilus parasuis strains to identify proteins that may help in habitat adaptation and pathogenesis

Biochemical and kinetic characterisation of a novel xylooligosaccharide-upregulated GH43 β-d-xylosidase/α-l-arabinofuranosidase (BXA43) from the probiotic Bifidobacterium animalis subsp. lactis BB-12

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