scholarly journals Poly(glucosyl-N-acetylgalactosamine 1-phosphate), a wall teichoic acid of Bacillus subtilis 168: its biosynthetic pathway and mode of attachment to peptidoglycan

Microbiology ◽  
2006 ◽  
Vol 152 (6) ◽  
pp. 1709-1718 ◽  
Author(s):  
Pierre-Philippe Freymond ◽  
Vladimir Lazarevic ◽  
Blazenka Soldo ◽  
Dimitri Karamata
Keyword(s):  
Bacillus Subtilis ◽  
Nucleotide Sequence ◽  
Outer Surface ◽  
Biosynthetic Pathway ◽  
Teichoic Acid ◽  
Glycerol Phosphate ◽  
Wall Teichoic Acid ◽  
Gram Positive Bacteria ◽  
Bacillus Subtilis 168 ◽  
Mode Of Attachment

The ggaAB operon of Bacillus subtilis 168 encodes enzymes responsible for the synthesis of poly(glucosyl N-acetylgalactosamine 1-phosphate) [poly(GlcGalNAc 1-P)], a wall teichoic acid (WTA). Analysis of the nucleotide sequence revealed that both GgaA and GgaB contained the motif characteristic of sugar transferases, while GgaB was most likely to be bifunctional, being endowed with an additional motif present in glucosyl/glycerophosphate transferases. Transcription of the operon was thermosensitive, and took place from an unusually distant σ A-controlled promoter. The incorporation of the poly(GlcGalNAc 1-P) precursors by various mutants deficient in the synthesis of poly(glycerol phosphate), which is the most abundant WTA of strain 168, revealed that both WTAs were most likely to be attached to peptidoglycan (PG) through the same linkage unit (LU). The incorporation of poly(GlcGalNAc 1-P) precursors by protoplasts confirmed the existence of this LU, and provided further evidence that incorporation takes place at the outer surface of the protoplast membrane. The data presented here strengthen the view that biosynthesis of the LU, and the hooking of the LU-endowed polymer to PG, offer distinct widespread targets for antibiotics specific to Gram-positive bacteria.

scholarly journals Teichoic Acid Is an Essential Polymer in Bacillus subtilis That Is Functionally Distinct from Teichuronic Acid

2004 ◽  
Vol 186 (23) ◽  
pp. 7865-7873 ◽  
Author(s):  
Amit P. Bhavsar ◽  
Laura K. Erdman ◽  
Jeffrey W. Schertzer ◽  
Eric D. Brown
Keyword(s):  
Cell Wall ◽  
Bacillus Subtilis ◽  
Teichoic Acid ◽  
Wall Thickening ◽  
Glycerol Phosphate ◽  
Wall Teichoic Acid ◽  
Teichoic Acids ◽  
Gram Positive Bacteria ◽  
Teichuronic Acid ◽  
Wall Teichoic Acids

ABSTRACT Wall teichoic acids are anionic, phosphate-rich polymers linked to the peptidoglycan of gram-positive bacteria. In Bacillus subtilis, the predominant wall teichoic acid types are poly(glycerol phosphate) in strain 168 and poly(ribitol phosphate) in strain W23, and they are synthesized by the tag and tar gene products, respectively. Growing evidence suggests that wall teichoic acids are essential in B. subtilis; however, it is widely believed that teichoic acids are dispensable under phosphate-limiting conditions. In the work reported here, we carefully studied the dispensability of teichoic acid under phosphate-limiting conditions by constructing three new mutants. These strains, having precise deletions in tagB, tagF, and tarD, were dependent on xylose-inducible complementation from a distal locus (amyE) for growth. The tarD deletion interrupted poly(ribitol phosphate) synthesis in B. subtilis and represents a unique deletion of a tar gene. When teichoic acid biosynthetic proteins were depleted, the mutants showed a coccoid morphology and cell wall thickening. The new wall teichoic acid biogenesis mutants generated in this work and a previously reported tagD mutant were not viable under phosphate-limiting conditions in the absence of complementation. Cell wall analysis of B. subtilis grown under phosphate-limited conditions showed that teichoic acid contributed approximately one-third of the wall anionic content. These data suggest that wall teichoic acid has an essential function in B. subtilis that cannot be replaced by teichuronic acid.

scholarly journals Surface Glycopolymers Are Crucial forIn VitroAnti-Wall Teichoic Acid IgG-Mediated Complement Activation and Opsonophagocytosis of Staphylococcus aureus

2015 ◽  
Vol 83 (11) ◽  
pp. 4247-4255 ◽  
Author(s):  
Jong-Ho Lee ◽  
Na-Hyang Kim ◽  
Volker Winstel ◽  
Kenji Kurokawa ◽  
Jesper Larsen ◽  
...  
Keyword(s):  
Staphylococcus Aureus ◽  
Teichoic Acid ◽  
Complement C3 ◽  
Glycerol Phosphate ◽  
Glycosylation Pattern ◽  
Wall Teichoic Acid ◽  
Content Type ◽  
Gram Positive Bacteria ◽  
Capsule Production ◽  
Cell Envelopes

ABSTRACTThe cell envelopes of many Gram-positive bacteria contain wall teichoic acids (WTAs).Staphylococcus aureusWTAs are composed of ribitol phosphate (RboP) or glycerol phosphate (GroP) backbones substituted withd-alanine andN-acetyl-d-glucosamine (GlcNAc) orN-acetyl-d-galactosamine (GalNAc). Two WTA glycosyltransferases, TarM and TarS, are responsible for modifying the RboP WTA with α-GlcNAc and β-GlcNAc, respectively. We recently reported that purified human serum anti-WTA IgG specifically recognizes β-GlcNAc of the staphylococcal RboP WTA and then facilitates complement C3 deposition and opsonophagocytosis ofS. aureuslaboratory strains. This prompted us to examine whether anti-WTA IgG can induce C3 deposition on a diverse set of clinicalS. aureusisolates. To this end, we compared anti-WTA IgG-mediated C3 deposition and opsonophagocytosis abilities using 13 different staphylococcal strains. Of note, the majority ofS. aureusstrains tested was recognized by anti-WTA IgG, resulting in C3 deposition and opsonophagocytosis. A minority of strains was not recognized by anti-WTA IgG, which correlated with either extensive capsule production or an alteration in the WTA glycosylation pattern. Our results demonstrate that the presence of WTAs with TarS-mediated glycosylation with β-GlcNAc in clinically isolatedS. aureusstrains is an important factor for induction of anti-WTA IgG-mediated C3 deposition and opsonophagocytosis.

Expression of heterologous genes for wall teichoic acid in Bacillus subtilis 168

1987 ◽  
Vol 207 (1) ◽  
pp. 73-81 ◽  
Author(s):  
Dimitri Karamata ◽  
Harold M. Pooley ◽  
Michel Monod
Keyword(s):  
Bacillus Subtilis ◽  
Teichoic Acid ◽  
Wall Teichoic Acid ◽  
Bacillus Subtilis 168

scholarly journals The Amino Terminus of Bacillus subtilis TagB Possesses Separable Localization and Functional Properties

2007 ◽  
Vol 189 (19) ◽  
pp. 6816-6823 ◽  
Author(s):  
Amit P. Bhavsar ◽  
Michael A. D'Elia ◽  
Tiffany D. Sahakian ◽  
Eric D. Brown
Keyword(s):  
Bacillus Subtilis ◽  
Protein Function ◽  
Teichoic Acid ◽  
Acid Synthesis ◽  
Amino Terminus ◽  
Membrane Localization ◽  
Membrane Targeting ◽  
Glycerol Phosphate ◽  
Wall Teichoic Acid ◽  
Necessary And Sufficient

ABSTRACT The function(s) of gram-positive wall teichoic acid is emerging with recent findings that it is an important virulence factor in the pathogen Staphylococcus aureus and that it is crucial to proper rod-shaped cell morphology of Bacillus subtilis. Despite its importance, our understanding of teichoic acid biosynthesis remains incomplete. The TagB protein has been implicated in the priming step of poly(glycerol phosphate) wall teichoic acid synthesis in B. subtilis. Work to date indicates that the TagB protein is localized to the membrane, where it adds a single glycerol phosphate residue to the nonreducing end of the undecaprenol-phosphate-linked N-acetylmannosamine-β(1,4)-N-acetylglucosamine-1-phosphate. Thus, membrane association is critical to TagB function. In this work we elucidate the mechanism of TagB membrane localization. We report the identification of a membrane targeting determinant at the amino terminus of TagB that is necessary and sufficient for membrane localization. The putative amphipathicity of this membrane targeting determinant was characterized and shown to be required for TagB function but not localization. This work shows for the first time that the amino terminus of TagB mediates membrane targeting and protein function.

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