scholarly journals Cell Wall Teichoic Acid Glycosylation inListeria monocytogenes Serotype 4b Requires gtcA, a Novel, Serogroup-Specific Gene

1999 ◽  
Vol 181 (2) ◽  
pp. 418-425 ◽  
Author(s):  
N. Promadej ◽  
F. Fiedler ◽  
P. Cossart ◽  
S. Dramsi ◽  
S. Kathariou
Keyword(s):  
Cell Wall ◽  
Marked Reduction ◽  
Teichoic Acid ◽  
Lipoteichoic Acid ◽  
Specific Gene ◽  
Specific Monoclonal Antibody ◽  
Wild Type ◽  
Wall Teichoic Acid ◽  
Insertional Inactivation ◽  
Serotype 4B

ABSTRACT We have identified a novel gene, gtcA, involved in the decoration of cell wall teichoic acid of Listeria monocytogenes serotype 4b with galactose and glucose. Insertional inactivation of gtcA brought about loss of reactivity with the serotype 4b-specific monoclonal antibody c74.22 and was accompanied by a complete lack of galactose and a marked reduction in the amounts of glucose on teichoic acid. Interestingly, the composition of membrane-associated lipoteichoic acid was not affected. Complementation of the mutants with the clonedgtcA in trans restored galactose and glucose on teichoic acid to wild-type levels. The complemented strains also recovered reactivity with c74.22. Within L. monocytogenes, sequences homologous to gtcA were found in all serogroup 4 isolates but not in strains of any other serotypes. In serotype 4b, gtcA appears to be the first member of a bicistronic operon which includes a gene with homology toBacillus subtilis rpmE, encoding ribosomal protein L31. In contrast to gtcA, the latter gene appears conserved among all screened serotypes of L. monocytogenes.

scholarly journals A Novel Serotype-Specific Gene Cassette (gltA-gltB) Is Required for Expression of Teichoic Acid-Associated Surface Antigens in Listeria monocytogenes of Serotype 4b

2001 ◽  
Vol 183 (4) ◽  
pp. 1133-1139 ◽  
Author(s):  
Xiang-He Lei ◽  
Franz Fiedler ◽  
Zheng Lan ◽  
Sophia Kathariou
Keyword(s):  
Listeria Monocytogenes ◽  
Teichoic Acid ◽  
Genomic Analysis ◽  
Gene Cassette ◽  
Surface Antigens ◽  
Comparative Genomic ◽  
Specific Gene ◽  
Chromosomal Locus ◽  
Insertional Inactivation ◽  
Serotype 4B

ABSTRACT Listeria monocytogenes serotype 4b strains account for about 40% of sporadic cases and many epidemics of listeriosis. Mutations in a chromosomal locus resulted in loss of reactivity with all three monoclonal antibodies (MAbs) which were specific to serotype 4b and the closely related serotypes 4d and 4e. Here we show that this locus contains a serotype 4b-4d-4e-specific gene cassette (3,071 bp) which consists of two genes, gltA and gltB, and is flanked by palindromic sequences (51 and 44 nucleotides). Complete loss of reactivity with the three serotype-specific MAbs resulted from insertional inactivation of either gltA orgltB. The gltA and gltB mutants were characterized by loss and severe reduction, respectively, of glucose in the teichoic acid, whereas galactose, the other serotype-specific sugar substituent in the teichoic acid, was not affected. Within L. monocytogenes, only strains of serotypes 4b, 4d, and 4e harbored the gltA-gltB cassette, whereas coding sequences on either side of the cassette were conserved among all serotypes. Comparative genomic analysis of a serotype 1/2b strain showed that the 3,071-bp gltA-gltB cassette was replaced by a much shorter (528-bp) and unrelated region, flanked by inverted repeats similar to their counterparts in serotype 4b. These findings indicate that in the evolution of different serotypes ofL. monocytogenes, this site in the genome has become occupied by serotype-specific sequences which, in the case of serotype 4b, are essential for expression of serotype-specific surface antigens and presence of glucose substituents in the teichoic acids in the cell wall.

scholarly journals Teichoic Acid Glycosylation Mediated by gtcA Is Required for Phage Adsorption and Susceptibility of Listeria monocytogenes Serotype 4b

2008 ◽  
Vol 74 (5) ◽  
pp. 1653-1655 ◽  
Author(s):  
Ying Cheng ◽  
Nattawan Promadej ◽  
Jae-Won Kim ◽  
S. Kathariou
Keyword(s):  
Cell Wall ◽  
Listeria Monocytogenes ◽  
Teichoic Acid ◽  
Insertion Mutant ◽  
Wall Teichoic Acid ◽  
Phage Adsorption ◽  
Serotype 4B

ABSTRACT An insertion mutant of gtcA, responsible for serotype-specific glycosylation of the cell wall teichoic acid in serotype 4b strains of Listeria monocytogenes, was also resistant to both Listeria genus- and serotype 4b-specific phages. The sugar substituents on teichoic acid appeared essential for the adsorption of phages A500 (serotype 4b specific) and A511 (Listeria genus specific) to serotype 4b L. monocytogenes.

scholarly journals Inactivation of the monofunctional peptidoglycan glycosyltransferase SgtB allowsStaphylococcus aureusto survive in the absence of lipoteichoic acid

2018 ◽  
Author(s):  
Eleni Karinou ◽  
Christopher F. Schuster ◽  
Manuel Pazos ◽  
Waldemar Vollmer ◽  
Angelika Gründling
Keyword(s):  
Staphylococcus Aureus ◽  
Cell Wall ◽  
Teichoic Acid ◽  
Fold Increase ◽  
Lipoteichoic Acid ◽  
Wall Teichoic Acid ◽  
Anionic Polymers ◽  
Peptidoglycan Structure ◽  
Intimate Link ◽  
Inactivating Mutations

AbstractThe cell wall ofStaphylococcus aureusis composed of peptidoglycan and the anionic polymers lipoteichoic acid (LTA) and wall teichoic acid. LTA is required for growth and normal cell morphology inS. aureus.Strains lacking LTA are usually only viable when grown under osmotically stabilizing conditions or after the acquisition of compensatory mutations. LTA negative suppressor strains with inactivating mutations ingdpP, resulting in an increase in intracellular c-di-AMP levels, have been described previously. Here, we sought to identify factors other than c-di-AMP that allowS. aureusto survive without LTA. LTA-negative strains able to grow in un-supplemented medium were obtained and found to contain mutations insgtB, mazE, clpXorvraT. The growth improvement through mutations inmazEandsgtBwas confirmed by complementation analysis. We also show that anS. aureus sgtBtransposon mutant, inactivated for the monofunctional peptidoglycan glycosyltransferase SgtB, displays a 4-fold increase in the MIC towards a number of cell wall-targeting antibiotics, suggesting that alteration in the peptidoglycan structure could help bacteria compensate for the lack of LTA. Muropeptide analysis of peptidoglycan isolated from a WT andsgtBmutant strains did not reveal any sizable alternations in the peptidoglycan structure. In contrast, the peptidoglycan isolated from an LTA-negativeltaSmutant strain showed a significant reduction in the fraction of highly crosslinked peptidoglycan, which was partially rescued in thesgtB/ltaSdouble mutant suppressor strain. Taken together, these data point towards an important function of LTA in cell wall integrity through its requirement for proper peptidoglycan assembly.ImportanceThe bacterial cell wall acts as primary defence against environmental insults such as changes in osmolarity. It is also a vulnerable structure as defects in its synthesis can lead to growth arrest or cell death. The important human pathogenStaphylococcus aureushas a typical Gram-positive cell wall, which consists of peptidoglycan and the anionic polymers lipoteichoic acid (LTA) and wall teichoic acid. Several clinically relevant antibiotics inhibit the synthesis of peptidoglycan; hence it and teichoic acids are considered attractive targets for the development of new antimicrobials. We show that LTA is required for efficient peptidoglycan crosslinking inS. aureusand inactivation of a peptidoglycan glycosyltransferase can partially rescue this defect, altogether revealing an intimate link between peptidoglycan and LTA synthesis.

scholarly journals Cross-Linked Peptidoglycan Mediates Lysostaphin Binding to the Cell Wall Envelope of Staphylococcus aureus

2006 ◽  
Vol 188 (7) ◽  
pp. 2463-2472 ◽  
Author(s):  
Angelika Gründling ◽  
Olaf Schneewind
Keyword(s):  
Staphylococcus Aureus ◽  
Cell Wall ◽  
Fluorescent Protein ◽  
Teichoic Acid ◽  
Lipoteichoic Acid ◽  
Wall Teichoic Acid ◽  
Cross Bridges ◽  
Specific Association ◽  
Species Specific ◽  
Green Fluorescent

ABSTRACT Staphylococcus simulans bv. staphylolyticus secretes lysostaphin, a bacteriocin that cleaves pentaglycine cross bridges in the cell wall of Staphylococcus aureus. The C-terminal cell wall-targeting domain (CWT) of lysostaphin is required for selective binding of this bacteriocin to S. aureus cells; however, the molecular target for this was unknown. We used purified green fluorescent protein fused to CWT (GFP-CWT) to reveal species-specific association of the reporter with staphylococci. GFP-CWT bound S. aureus cells as well as purified peptidoglycan sacculi. The addition of cross-linked murein, disaccharides linked to interconnected wall peptides, blocked GFP-CWT binding to staphylococci, whereas murein monomers or lysostaphin-solubilized cell wall fragments did not. S. aureus strain Newman variants lacking the capacity for synthesizing polysaccharide capsule (capFO), poly-N-acetylglucosamine (icaAC), lipoprotein (lgt), cell wall-anchored proteins (srtA), or the glycolipid anchor of lipoteichoic acid (ypfP) bound GFP-CWT similar to wild-type staphylococci. A tagO mutant strain, defective in the synthesis of polyribitol wall teichoic acid attached to the cell wall envelope, displayed increased GFP-CWT binding. In contrast, a femAB mutation, reducing both the amount and the length of peptidoglycan cross-linking (monoglycine cross bridges), showed a dramatic reduction in GFP-CWT binding. Thus, the CWT domain of lysostaphin directs the bacteriocin to cross-linked peptidoglycan, which also serves as the substrate for its glycyl-glycine endopeptidase domain.

scholarly journals GtcA is required for LTA glycosylation in Listeria monocytogenes serovar 1/2a and Bacillus subtilis

2019 ◽  
Author(s):  
Jeanine Rismondo ◽  
Talal F. M. Haddad ◽  
Yang Shen ◽  
Martin J. Loessner ◽  
Angelika Gründling
Keyword(s):  
Cell Wall ◽  
Bacillus Subtilis ◽  
Listeria Monocytogenes ◽  
Teichoic Acid ◽  
Lipoteichoic Acid ◽  
Wall Teichoic Acid ◽  
Gram Positive Bacteria ◽  
Cell Wall Polymers ◽  
Galactose Residue

ABSTRACTThe cell wall polymers wall teichoic acid (WTA) and lipoteichoic acid (LTA) are often modified with glycosyl and D-alanine residues. Recent studies have shown that a three-component glycosylation system is used for the modification of LTA in several Gram-positive bacteria including Bacillus subtilis and Listeria monocytogenes. In the L. monocytogenes 1/2a strain 10403S, the cytoplasmic glycosyltransferase GtlA is thought to use UDP-galactose to produce the C55-P-galactose lipid intermediate, which is transported across the membrane by an unknown flippase. Next, the galactose residue is transferred onto the LTA backbone on the outside of the cell by the glycosyltransferase GtlB. Here we show that GtcA is necessary for the glycosylation of LTA in L. monocytogenes 10403S and B. subtilis 168 and we hypothesize that these proteins act as C55-P-sugar flippases. With this we revealed that GtcA is involved in the glycosylation of both teichoic acid polymers in L. monocytogenes 10403S, namely WTA with N-acetylglucosamine and LTA with galactose residues. These findings indicate that the L. monocytogenes GtcA protein can act on different C55-P-sugar intermediates. Further characterization of GtcA in L. monocytogenes led to the identification of residues essential for its overall function as well as residues, which predominately impact WTA or LTA glycosylation.GRAPHICAL ABSTRACT

scholarly journals Teichoic Acid Polymers Affect Expression and Localization of dl-Endopeptidase LytE Required for Lateral Cell Wall Hydrolysis in Bacillus subtilis

2016 ◽  
Vol 198 (11) ◽  
pp. 1585-1594 ◽  
Author(s):  
Jun Kasahara ◽  
Yuuka Kiriyama ◽  
Mari Miyashita ◽  
Takuma Kondo ◽  
Takeshi Yamada ◽  
...  
Keyword(s):  
Cell Wall ◽  
Cell Surface ◽  
High Temperatures ◽  
Teichoic Acid ◽  
Lipoteichoic Acid ◽  
Peptidoglycan Hydrolase ◽  
Wall Teichoic Acid ◽  
Anionic Polymers ◽  
Peptidoglycan Hydrolysis ◽  
Lateral Cell

ABSTRACTInBacillus subtilis, thedl-endopeptidase LytE is responsible for lateral peptidoglycan hydrolysis during cell elongation. We found that σI-dependent transcription oflytEis considerably enhanced in a strain with a mutation inltaS, which encodes a major lipoteichoic acid (LTA) synthase. Similar enhancements were observed in mutants that affect the glycolipid anchor and wall teichoic acid (WTA) synthetic pathways. Immunofluorescence microscopy revealed that the LytE foci were considerably increased in these mutants. The localization patterns of LytE on the sidewalls appeared to be helix-like in LTA-defective or WTA-reduced cells and evenly distributed on WTA-depleted or -defective cell surfaces. These results strongly suggested that LTA and WTA affect both σI-dependent expression and localization of LytE. Interestingly, increased LytE localization along the sidewall in theltaSmutant largely occurred in an MreBH-independent manner. Moreover, we found that cell surface decorations with LTA and WTA are gradually reduced at increased culture temperatures and that LTA rather than WTA on the cell surface is reduced at high temperatures. In contrast, the amount of LytE on the cell surface gradually increased under heat stress conditions. Taken together, these results indicated that reductions in these anionic polymers at high temperatures might give rise to increases in SigI-dependent expression and cell surface localization of LytE at high temperatures.IMPORTANCEThe bacterial cell wall is required for maintaining cell shape and bearing environmental stresses. The Gram-positive cell wall consists of mesh-like peptidoglycan and covalently linked wall teichoic acid and lipoteichoic acid polymers. It is important to determine if these anionic polymers are required for proliferation and environmental adaptation. Here, we demonstrated that these polymers affect the expression and localization of a peptidoglycan hydrolase LytE required for lateral cell wall elongation. Moreover, we found that cell surface decorations with teichoic acid polymers are substantially decreased at high temperatures and that the peptidoglycan hydrolase is consequently increased. These findings suggest that teichoic acid polymers control lateral peptidoglycan hydrolysis by LytE, and bacteria drastically change their cell wall content to adapt to their environment.

scholarly journals Inactivation of the Monofunctional Peptidoglycan Glycosyltransferase SgtB AllowsStaphylococcus aureusTo Survive in the Absence of Lipoteichoic Acid

2018 ◽  
Vol 201 (1) ◽  
Author(s):  
Eleni Karinou ◽  
Christopher F. Schuster ◽  
Manuel Pazos ◽  
Waldemar Vollmer ◽  
Angelika Gründling
Keyword(s):  
Staphylococcus Aureus ◽  
Cell Wall ◽  
Mutant Strain ◽  
Teichoic Acid ◽  
Fold Increase ◽  
Lipoteichoic Acid ◽  
Wall Teichoic Acid ◽  
Content Type ◽  
Anionic Polymers ◽  
Peptidoglycan Structure

ABSTRACTThe cell wall ofStaphylococcus aureusis composed of peptidoglycan and the anionic polymers lipoteichoic acid (LTA) and wall teichoic acid. LTA is required for growth and normal cell morphology inS. aureus. Strains lacking LTA are usually viable only when grown under osmotically stabilizing conditions or after the acquisition of compensatory mutations. LTA-negative suppressor strains with inactivating mutations ingdpP, which resulted in increased intracellular c-di-AMP levels, were described previously. Here, we sought to identify factors other than c-di-AMP that allowS. aureusto survive without LTA. LTA-negative strains able to grow in unsupplemented medium were obtained and found to contain mutations insgtB,mazE,clpX, orvraT. The growth improvement through mutations inmazEandsgtBwas confirmed by complementation analysis. We also showed that anS. aureussgtBtransposon mutant, with the monofunctional peptidoglycan glycosyltransferase SgtB inactivated, displayed a 4-fold increase in the MIC of oxacillin, suggesting that alterations in the peptidoglycan structure could help bacteria compensate for the lack of LTA. Muropeptide analysis of peptidoglycans isolated from a wild-type strain andsgtBmutant strain did not reveal any sizable alterations in the peptidoglycan structure. In contrast, the peptidoglycan isolated from an LTA-negativeltaSmutant strain showed a significant reduction in the fraction of highly cross-linked peptidoglycan, which was partially rescued in thesgtB ltaSdouble mutant suppressor strain. Taken together, these data point toward an important function of LTA in cell wall integrity through its necessity for proper peptidoglycan assembly.IMPORTANCEThe bacterial cell wall acts as a primary defense against environmental insults such as changes in osmolarity. It is also a vulnerable structure, as defects in its synthesis can lead to growth arrest or cell death. The important human pathogenStaphylococcus aureushas a typical Gram-positive cell wall, which consists of peptidoglycan and the anionic polymers LTA and wall teichoic acid. Several clinically relevant antibiotics inhibit the synthesis of peptidoglycan; therefore, it and teichoic acids are considered attractive targets for the development of new antimicrobials. We show that LTA is required for efficient peptidoglycan cross-linking inS. aureusand inactivation of a peptidoglycan glycosyltransferase can partially rescue this defect, together revealing an intimate link between peptidoglycan and LTA synthesis.

scholarly journals Absence of Serotype-Specific Surface Antigen and Altered Teichoic Acid Glycosylation among Epidemic-Associated Strains of Listeria monocytogenes

2000 ◽  
Vol 38 (10) ◽  
pp. 3856-3859 ◽  
Author(s):  
Elizabeth E. Clark ◽  
Irene Wesley ◽  
Franz Fiedler ◽  
Nattawan Promadej ◽  
Sophie Kathariou
Keyword(s):  
Monoclonal Antibody ◽  
Cell Wall ◽  
Listeria Monocytogenes ◽  
Specific Surface ◽  
Surface Antigen ◽  
Teichoic Acid ◽  
Specific Monoclonal Antibody ◽  
Specific Phage ◽  
Food Borne ◽  
Serotype 4B

Outbreaks of food-borne listeriosis have often involved strains of serotype 4b. Examination of multiple isolates from three different outbreaks revealed that ca. 11 to 29% of each epidemic population consisted of strains which were negative with the serotype-specific monoclonal antibody c74.22, lacked galactose from the teichoic acid of the cell wall, and were resistant to the serotype 4b-specific phage 2671.

scholarly journals Transcriptome and metabolome profiling provide insights into molecular mechanism of pseudostem elongation in banana

2021 ◽  
Vol 21 (1) ◽  
Author(s):  
Guiming Deng ◽  
Fangcheng Bi ◽  
Jing Liu ◽  
Weidi He ◽  
Chunyu Li ◽  
...  
Keyword(s):  
Cell Wall ◽  
Cell Elongation ◽  
Molecular Mechanisms ◽  
Specific Gene ◽  
Wild Type ◽  
Banana Plant ◽  
Cell Wall Modification ◽  
Dwarf Cultivar ◽  
Important Trait ◽  
Metabolome Profiling

AbstractBackgroundBanana plant height is an important trait for horticultural practices and semi-dwarf cultivars show better resistance to damages by wind and rain. However, the molecular mechanisms controlling the pseudostem height remain poorly understood. Herein, we studied the molecular changes in the pseudostem of a semi-dwarf banana mutant Aifen No. 1 (Musaspp. Pisang Awak sub-group ABB) as compared to its wild-type dwarf cultivar using a combined transcriptome and metabolome approach.ResultsA total of 127 differentially expressed genes and 48 differentially accumulated metabolites were detected between the mutant and its wild type. Metabolites belonging to amino acid and its derivatives, flavonoids, lignans, coumarins, organic acids, and phenolic acids were up-regulated in the mutant. The transcriptome analysis showed the differential regulation of genes related to the gibberellin pathway, auxin transport, cell elongation, and cell wall modification. Based on the regulation of gibberellin and associated pathway-related genes, we discussed the involvement of gibberellins in pseudostem elongation in the mutant banana. Genes and metabolites associated with cell wall were explored and their involvement in cell extension is discussed.ConclusionsThe results suggest that gibberellins and associated pathways are possibly developing the observed semi-dwarf pseudostem phenotype together with cell elongation and cell wall modification. The findings increase the understanding of the mechanisms underlying banana stem height and provide new clues for further dissection of specific gene functions.

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