Structural studies on the wall teichoic acid from Bacillus licheniformis 6346 MH-1

1983 ◽  
Vol 11 (2) ◽  
pp. 173-174
Author(s):  
DAVID BUTTON ◽  
NORMAN L. HEMMINGS
Keyword(s):  
Bacillus Licheniformis ◽  
Teichoic Acid ◽  
Structural Studies ◽  
Wall Teichoic Acid

Preparation of a fragment of the cell wall teichoic acid of Bacillus licheniformis atcc 9945 via a solid phase approach

1987 ◽  
Vol 28 (14) ◽  
pp. 1557-1560 ◽  
Author(s):  
P. Westerduin ◽  
G.H. Veeneman ◽  
Y. Pennings ◽  
G.A. van der Marel ◽  
J.H. van Boom
Keyword(s):  
Cell Wall ◽  
Bacillus Licheniformis ◽  
Solid Phase ◽  
Teichoic Acid ◽  
Wall Teichoic Acid ◽  
Phase Approach

scholarly journals Biosynthesis of the wall teichoic acid in Bacillus licheniformis

1972 ◽  
Vol 127 (1) ◽  
pp. 27-37 ◽  
Author(s):  
I. C. Hancock ◽  
J. Baddiley
Keyword(s):  
Bacillus Licheniformis ◽  
Teichoic Acid ◽  
Chain Extension ◽  
Pulse Labelling ◽  
Glycerol Phosphate ◽  
Wall Teichoic Acid ◽  
Anomeric Configuration ◽  
Glucose Phosphate ◽  
Chemical Studies ◽  
Two Stages

1. The biosynthesis of the wall teichoic acid, poly(glycerol phosphate glucose), has been studied with a particulate membrane preparation from Bacillus licheniformis A.T.C.C. 9945. The precursor CDP-glycerol supplies glycerol phosphate residues, whereas UDP-glucose supplies only glucose to the repeating structure of the polymer. 2. Synthesis proceeds through polyprenol phosphate derivatives, and chemical studies and pulse-labelling techniques show that the first intermediate is the phosphodiester, glucose polyprenol monophosphate. CDP-glycerol donates a glycerol phosphate residue to this to give a second intermediate, (glycerol phosphate glucose phosphate) polyprenol. 3. The glucose residue in the lipid intermediates has the β configuration, and chain extension in the synthesis of polymer occurs by transglycosylation with inversion of anomeric configuration at two stages.

ChemInform Abstract: Preparation of a Fragment of the Cell Wall Teichoic Acid of Bacillus licheniformis ATCC 9945 via a Solid Phase Approach.

ChemInform ◽  
1987 ◽  
Vol 18 (38) ◽  
Author(s):  
P. WESTERDUIN ◽  
G. H. VEENEMAN ◽  
Y. PENNINGS ◽  
G. A. VAN DER MAREL ◽  
J. H. VAN BOOM
Keyword(s):  
Cell Wall ◽  
Bacillus Licheniformis ◽  
Solid Phase ◽  
Teichoic Acid ◽  
Wall Teichoic Acid ◽  
Phase Approach

scholarly journals Depletion of Undecaprenyl Pyrophosphate Phosphatases Disrupts Cell Envelope Biogenesis in Bacillus subtilis

2016 ◽  
Vol 198 (21) ◽  
pp. 2925-2935 ◽  
Author(s):  
Heng Zhao ◽  
Yingjie Sun ◽  
Jason M. Peters ◽  
Carol A. Gross ◽  
Ethan C. Garner ◽  
...  
Keyword(s):  
Bacillus Subtilis ◽  
Transcriptional Repression ◽  
Cell Envelope ◽  
Turgor Pressure ◽  
Teichoic Acid ◽  
Lethal Gene ◽  
Genetic Redundancy ◽  
Wall Teichoic Acid ◽  
Content Type ◽  
Lipid Ii

ABSTRACTThe integrity of the bacterial cell envelope is essential to sustain life by countering the high turgor pressure of the cell and providing a barrier against chemical insults. InBacillus subtilis, synthesis of both peptidoglycan and wall teichoic acids requires a common C55lipid carrier, undecaprenyl-pyrophosphate (UPP), to ferry precursors across the cytoplasmic membrane. The synthesis and recycling of UPP requires a phosphatase to generate the monophosphate form Und-P, which is the substrate for peptidoglycan and wall teichoic acid synthases. Using an optimizedclusteredregularlyinterspacedshortpalindromicrepeat (CRISPR) system with catalytically inactive (“dead”)CRISPR-associated protein9(dCas9)-based transcriptional repression system (CRISPR interference [CRISPRi]), we demonstrate thatB. subtilisrequires either of two UPP phosphatases, UppP or BcrC, for viability. We show that a third predicted lipid phosphatase (YodM), with homology to diacylglycerol pyrophosphatases, can also support growth when overexpressed. Depletion of UPP phosphatase activity leads to morphological defects consistent with a failure of cell envelope synthesis and strongly activates the σM-dependent cell envelope stress response, includingbcrC, which encodes one of the two UPP phosphatases. These results highlight the utility of an optimized CRISPRi system for the investigation of synthetic lethal gene pairs, clarify the nature of theB. subtilisUPP-Pase enzymes, and provide further evidence linking the σMregulon to cell envelope homeostasis pathways.IMPORTANCEThe emergence of antibiotic resistance among bacterial pathogens is of critical concern and motivates efforts to develop new therapeutics and increase the utility of those already in use. The lipid II cycle is one of the most frequently targeted processes for antibiotics and has been intensively studied. Despite these efforts, some steps have remained poorly defined, partly due to genetic redundancy. CRISPRi provides a powerful tool to investigate the functions of essential genes and sets of genes. Here, we used an optimized CRISPRi system to demonstrate functional redundancy of two UPP phosphatases that are required for the conversion of the initially synthesized UPP lipid carrier to Und-P, the substrate for the synthesis of the initial lipid-linked precursors in peptidoglycan and wall teichoic acid synthesis.

scholarly journals Hidden Mode of Action of Glycopeptide Antibiotics: Inhibition of Wall Teichoic Acid Biosynthesis

2017 ◽  
Vol 121 (16) ◽  
pp. 3925-3932 ◽  
Author(s):  
Manmilan Singh ◽  
James Chang ◽  
Lauryn Coffman ◽  
Sung Joon Kim
Keyword(s):  
Mode Of Action ◽  
Teichoic Acid ◽  
Glycopeptide Antibiotics ◽  
Acid Biosynthesis ◽  
Wall Teichoic Acid

scholarly journals Localization and Interactions of Teichoic Acid Synthetic Enzymes in Bacillus subtilis

2007 ◽  
Vol 190 (5) ◽  
pp. 1812-1821 ◽  
Author(s):  
Alex Formstone ◽  
Rut Carballido-López ◽  
Philippe Noirot ◽  
Jeffery Errington ◽  
Dirk-Jan Scheffers
Keyword(s):  
Bacillus Subtilis ◽  
Cell Shape ◽  
Spatial Organization ◽  
Structural Integrity ◽  
Fluorescent Protein ◽  
Teichoic Acid ◽  
Cytoskeletal Proteins ◽  
Thick Wall ◽  
Wall Teichoic Acid ◽  
Critical Function

ABSTRACT The thick wall of gram-positive bacteria is a polymer meshwork composed predominantly of peptidoglycan (PG) and teichoic acids, both of which have a critical function in maintenance of the structural integrity and the shape of the cell. In Bacillus subtilis 168 the major teichoic acid is covalently coupled to PG and is known as wall teichoic acid (WTA). Recently, PG insertion/degradation over the lateral wall has been shown to occur in a helical pattern. However, the spatial organization of WTA assembly and its relationship with cell shape and PG assembly are largely unknown. We have characterized the localization of green fluorescent protein fusions to proteins involved in several steps of WTA synthesis in B. subtilis: TagB, -F, -G, -H, and -O. All of these localized similarly to the inner side of the cytoplasmic membrane, in a pattern strikingly similar to that displayed by probes of nascent PG. Helix-like localization patterns are often attributable to the morphogenic cytoskeletal proteins of the MreB family. However, localization of the Tag proteins did not appear to be substantially affected by single disruption of any of the three MreB homologues of B. subtilis. Bacterial and yeast two-hybrid experiments revealed a complex network of interactions involving TagA, -B, -E, -F, -G, -H, and -O and the cell shape determinants MreC and MreD (encoded by the mreBCD operon and presumably involved in the spatial organization of PG synthesis). Taken together, our results suggest that, in B. subtilis at least, the synthesis and export of WTA precursors are mediated by a large multienzyme complex that may be associated with the PG-synthesizing machinery.

scholarly journals Analysis of phage-resistant mechanisms inStaphylococcus aureusSA003 reveals a different binding mechanism for the closely related Twort-like phages ϕSA012 and ϕSA039

2018 ◽  
Author(s):  
Aa Haeruman Azam ◽  
Fumiya Hoshiga ◽  
Ippei Takeuchi ◽  
Kazuhiko Miyanaga ◽  
Yasunori Tanji
Keyword(s):  
Teichoic Acid ◽  
Point Mutations ◽  
In Silico Analysis ◽  
Close Relative ◽  
Phenotypic Change ◽  
Missense Mutations ◽  
Wild Type ◽  
Wall Teichoic Acid ◽  
Whole Genome Analysis ◽  
Specific Phage

ABSTRACTWe have previously generated strains ofStaphylococcus aureusSA003 resistant to its specific phage ϕSA012 through long-term coevolution experiment. However, the DNA mutations responsible for the phenotypic change of phage resistance are unknown. Whole-genome analysis revealed six genes that acquired unique point mutations: five missense mutations and one nonsense mutation. Moreover, one deletion, 1.779-bp, resulted in the deletion of the genes encoding glycosyltransferase, TarS, and iron-sulfure repair protein, ScdA. The deletion occurred from the second round of coculture (SA003R2) and remained through the last round. The ϕSA012 infection toward SA003R2 had decreased to 79.77±7.50% according to plating efficiency. Complementation of the phage-resistant strain by the wild-type allele showed two mutated host genes were linked to the inhibition of post-adsorption, and five genes were linked to phage adsorption of ϕSA012. Unlike ϕSA012, infection by ϕSA039, a close relative of ϕSA012, onto SA003R2 was impaired drastically. Complementation of SA003R2 by wild-typetarSrestores the infectivity of ϕSA039. Thus, we concluded that ϕSA039 requires β-GlcNAc in Wall Teichoic Acid (WTA) for its binding. In silico analysis of the ϕSA039 genome revealed that several proteins in the tail and baseplate region were different from ϕSA012; notably the partial deletion oforf96of ϕSA039, a homolog oforf99of ϕSA012.Orf100of ϕSA039, a homolog ofOrf103of ϕSA012, a previously reported receptor binding protein (RBP), had low similarity (86%) to that of ϕSA012. The difference in tail and baseplate proteins might be the factor for specificity difference between ϕSA012 and ϕSA039.

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