Evidence map›Paper›PMID 42474192›Full record

ArticleApplied and environmental microbiology2026

Linking exocellular polysaccharide structures and biosynthetic genes in lactic acid bacteria by combinatorial optimization.

Kristian Jensen, Vera Kuzina Poulsen, Paula Gaspar, Pedro Lamosa, Ana Rute Neves, Ahmad A Zeidan

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Article in Applied and environmental microbiology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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1 · What the graph read from it

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2 · The registry

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3 · Its place in the literature

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4 · The record

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5 · Who and what money

Authors and funding

6 authors.

Kristian Jensen *Microbe & Culture Research, Novonesis A/S, Hørsholm, Denmark.ORCID 0000-0002-2796-805X
Vera Kuzina Poulsen *Microbe & Culture Research, Novonesis A/S, Hørsholm, Denmark.ORCID 0000-0003-3340-3634
Paula GasparMicrobe & Culture Research, Novonesis A/S, Hørsholm, Denmark.ORCID 0000-0003-0338-3935
Pedro LamosaInstituto de Tecnologia Química e Biológica António Xavier, Universidade Nova de Lisboa, Oeiras, Portugal.ORCID 0000-0002-3003-1516
Ana Rute NevesMicrobe & Culture Research, Novonesis A/S, Hørsholm, Denmark.ORCID 0000-0003-4896-9585
Ahmad A ZeidanMicrobe & Culture Research, Novonesis A/S, Hørsholm, Denmark.ORCID 0000-0001-9984-5625

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Lactic acid bacteria produce exocellular polysaccharides (EPSs) that are important in food and health applications, and their functional properties often depend on their chemical structure. These polysaccharides consist of chained repeat units that are assembled stepwise by multiple glycosyltransferases. However, experimental elucidation of EPS structure is time-consuming and labor-intensive, and sequence-based prediction remains limited because the donor and acceptor specificities of glycosyltransferases are difficult to infer from sequence alone. Here, we present a constrained combinatorial optimization framework that integrates data across multiple strains to associate glycosyltransferases in EPS biosynthetic gene clusters with individual sugar residues in EPS repeat units. The framework is constrained by predicted catalytic mechanisms, published experimental evidence, and shared features of glycosyltransferase repertoires and EPS structures across strains. We applied the approach to 10 EPS repeat unit structures elucidated here by nuclear magnetic resonance (NMR) spectroscopy, including four novel structures, together with 15 previously published structures. Using the currently available data set, we could putatively and uniquely assign 42 of 144 glycosyltransferases (29%) to a single repeat-unit residue and determine donor specificity for 60 of 144 glycosyltransferases (41%). This work improves the mapping of EPS genotype-phenotype relationships in lactic acid bacteria and contributes to advancing genome-based prediction of EPS structure.IMPORTANCEThe structure of exocellular polysaccharides produced by lactic acid bacteria is important for their functional roles in food and health applications but remains difficult to predict from genome sequence because glycosyltransferase specificity is hard to infer and structural characterization is slow. By combining new exocellular polysaccharide (EPS) repeat unit structures with a constrained multi-strain computational framework, we obtain a partial mapping between

Indexed as

Bacterial ProteinsGlycosyltransferasesLactobacillalesPolysaccharides, BacterialMagnetic Resonance SpectroscopyMultigene FamilyBacterial ProteinsGlycosyltransferasesPolysaccharides, Bacterialexocellular polysaccharidesglycosyltransferaselactic acid bacteriaNMR

Identifiers

PMID42474192
PMCPMC13488360

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.