Discovery of genes required for lipoteichoic acid glycosylation predicts two distinct mechanism for wall teichoic acid glycosylation
| Autor: | Rismondo, J, Percy, MG, Grundling, A |
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| Přispěvatelé: | Wellcome Trust, Medical Research Council (MRC), Commission of the European Communities |
| Rok vydání: | 2018 |
| Předmět: |
Biochemistry & Molecular Biology
animal structures GRAM-POSITIVE BACTERIA glycosylation wall teichoic acid Bacillus bacterial glycobiology macromolecular substances glycosyltransferase BACILLUS-SUBTILIS CELL-WALL BIOSYNTHESIS LISTERIA-MONOCYTOGENES STAPHYLOCOCCUS-AUREUS Science & Technology IDENTIFICATION 11 Medical And Health Sciences 06 Biological Sciences teichoic acid carbohydrates (lipids) stomatognathic diseases Staphylococcus aureus (S. aureus) lipoteichoic acid CORYNEBACTERIUM-GLUTAMICUM ESCHERICHIA-COLI cell wall lipids (amino acids peptides and proteins) MYCOBACTERIUM-TUBERCULOSIS 03 Chemical Sciences Life Sciences & Biomedicine |
| Popis: | The bacterial cell wall is an important and highly complex structure that is essential for bacterial growth because it protects bacteria from cell lysis and environmental insults. A typical Gram-positive bacterial cell wall is composed of peptidoglycan and the secondary cell wall polymers, wall teichoic acid (WTA) and lipoteichoic acid (LTA). In many Gram-positive bacteria, LTA is a polyglycerol-phosphate chain that is decorated with D-alanine and sugar residues. However, the function of and proteins responsible for the glycosylation of LTA are either unknown or not well-characterized. Here, using bioinformatics, genetic, and NMR spectroscopy approaches, we found that the Bacillus subtilis csbB and yfhO genes are essential for LTA glycosylation. Interestingly, the Listeria monocytogenes gene lmo1079, which encodes a YfhO ortholog, was not required for LTA glycosylation, but instead was essential for WTA glycosylation. LTA is polymerized on the outside of the cell and hence can only be glycosylated extracellularly. Based on the similarity of the genes coding for YfhO orthologs that are required in B. subtilis for LTA glycosylation or in L. monocytogenes for WTA glycosylation, we hypothesize that WTA glycosylation might also occur extracellularly in Listeria species. Finally, we discovered that in L. monocytogenes lmo0626 (gtlB) was required for LTA glycosylation, indicating that the encoded protein has a similar function to YfhO, even though the proteins are not homologous. Together, our results enable us to propose an updated model for LTA glycosylation and also indicate that glycosylation of WTA might occur through two different mechanisms in Gram-positive bacteria. |
| Databáze: | OpenAIRE |
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