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Teneberg, S.

Publications and source records attributed to Teneberg, S..

2 recordsLinked to original sources

Dual human milk oligosaccharide-fibre utilisation drives gut microbiome selection during weaning

Gut microbiome (GM) maturation in early life follows organised taxonomic successions. How weaning impacts these trajectories remains underexplored. Here, we sampled faeces from seven mother-infant dyads at pre-, early and late weaning. Enrichment cultures (n=306) and metagenomic (n=108) analyses revealed an unexpected prevalence of fibre degradation genes and the growth of the pre-weaning infant GM on common dietary fibres. Utilisation of both human milk oligosaccharides (HMOs) and dietary fibres was revealed as a metabolic hallmark of the weaning GM. We showed that HMO-utilisation is retained beyond weaning, by analyses of maternal GM and HMO utilisation in 137 maternal isolates. Our findings highlight dual HMO-dietary fibre utilisation as a hitherto unrecognised driver that potentially orchestrates the selection of distinct adult GM species during weaning. This work outlines a plausible mechanism underlying the organised GM maturation in early life and highlights a previously overlooked role of HMOs during the weaning transition.

microbiology↗

The binding mechanism of Streptococcus suis accessory virulence factor and adhesin SadP to globotetraosylceramide

Streptococcus suis is part of the pig commensal microbiome and a major pathogen causing pneumonia and meningitis in pigs and occasionally also zoonotic meningitis. According to genomic analysis, S. suis is divided into asymptomatic carriage, respiratory and systemic strains with distinct genomic signatures. The virulence factor S. suis adhesin P (SadP) recognizes the galabiose Gal1-4Gal-oligosaccharide. Based on its oligosaccharide fine specificity, SadP can be divided into subtypes PN and PO. We show here that subtype PN is distributed in the systemic strains that cause meningitis, whereas type PO is found in asymptomatic carriage and respiratory strains. Both types of SadP are shown to predominantly bind to pig lung globotriaosylceramide (Gb3). However, SadP adhesin from systemic subtype PN strain also binds to globotetraosylceramide (Gb4). Mutagenesis studies of the galabiose-binding domain of type PN SadP adhesin showed that the amino acid asparagine-285, which is replaced by an aspartate residue in type Po SadP, was required for binding to Gb4 and, strikingly, it was also required for interaction with the glycomimetic inhibitor phenylurea-galabiose. Molecular dynamics simulations provided further insight into the role of Asn-285 for Gb4 and phenylurea-galabiose binding, suggesting additional hydrogen bonding to terminal GalNAc of Gb4 and urea-group. Thus, the Asn-285-mediated molecular mechanism of type PN SadP binding to Gb4 could be used as a candidate to selectively target S. suis in invasive systemic disease without interfering with commensal strains, which may open up new venues for developing intervention strategies against this pathogen.

microbiology↗