N-acetylglucosamine 1-phosphate Research Articles

Demonstration of the enzymatic mechanisms of α- N-acetyl- d-glucosamine-1-phosphodiester N-acetylglucosaminidase (formerly called α- N-acetylglucosaminylphosphodiesterase) and lysosomal α- N-acetylglucosaminidase

An enzyme that is capable of removing the outer N-acetylglucosamine residues from phosphodiesters present on the high-mannose-type oligosaccharides of newly synthesized lysosomal enzymes has been described. This enzyme has been called an α- Nacetylglucosaminylphosphodiesterase, based upon its substrate specificity and on inhibitor studies. In this study it is demonstrated by the 18O enrichment method that the enzyme cleaves the CO bond rather than the OP bond, and therefore acts by a glycosidase type of mechanism. In addition, the enzyme has no significant activity toward α- N-acetylglucosamine 1-phosphate, and therefore requires an underlying phosphodiester for activity. In accordance with the IUB recommendations for enzyme nomenclature, it is therefore suggested that the enzyme be renamed α- N-acetyl- dglucosamine-1-phosphodiester N-acetylglucosaminidase (systematic name, 2-acetamido-2-deoxy-α- d-glucose 1-phosphodiester acetamidodeoxyglucohydrolase). For convenience, the trivial name phosphodiester glycosidase is proposed. Lysosomal α- Nacetylglucosaminidase also has a glycosidase type of mechanism but it is active toward α- N-acetylglucosamine 1-phosphate as well as phosphodiesters with outer N-acetylglucosamine residues.

The dolichol pathway of protein glycosylation in rat liver. Evidence that GTP promotes transformation of endogenous dolichyl phosphate into dolichylpyrophosphoryl-N-acetylglucosamine in stripped rough microsomes.

Tunicamycin, an antibiotic which inhibits the transfer of N-acetylglucosamine 1-phosphate to dolichyl phosphate, has been used to decide whether or not, in stripped rough microsomes incubated with UDP-N-acetylglucosamine and GDP-mannose in the absence of detergent, the earliest effect of GTP in core glycosylation of proteins is to enhance synthesis of dolichylpyrophosphoryl-N-acetylglucosamine from endogenous dolichyl phosphate, or to transform this monoglycoside derivative into dolichylpyrophosphorylchitobiose. It has been found that the presence of tunicamycin in the reaction medium annihilates incorporation of N-acetylglucosamine and mannose into all kinds of glycoside derivative of dolichyl pyrophosphate, whereas dolichylphosphorylmannose is then formed in greater amount. Incorporation of N-acetylglucosamine into protein was also abolished; that of mannose was considerably reduced. Other experiments showed that transfer of N-acetylglucosamine 1-phosphate is the only reaction of the lipid intermediates pathway that becomes limiting after addition of tunicamycin in our GTP-stimulated system. Taking these and previous results from this laboratory [Godelaine et al. (1979) Eur. J. Biochem. 96, 17-26 and 27-34] into account, we conclude that GTP enhances the transformation of endogenous dolichyl phosphate into dolichylpyrophosphoryl-N-acetylglucosamine and leads to the complete assembly of dolichol-linked oligosaccharides which become ultimately transferred to protein. Triton X-100 increased the amount of dolichol glycosylated and markedly raised the ratio of labelled dolichylpyrophosphorylchitobiose to dolichylpyrophosphoryl-N-acetylglucosamine. Such changes being induced by GTP, we suggest that this nucleotide makes it possible to overcome a structural barrier of rough microsomes.

Inhibition of protein glycosylation and selective cytotoxicity toward virally transformed fibroblasts caused by B3-tunicamycin.

The biological effect of B3-tunicamycin, the only known homologue of tunicamycin which contains a saturated fatty-acid side chain, was examined using chick embryo fibroblasts, a mouse fibroblastic line (3T3) and a virally transformed mouse fibroblastic line (SV40-3T3). This homologue inhibited the transfer of N-acetylglucosamine 1-phosphate from UDP-N-acetylglucosamine to dolichyl phosphate, catalyzed by microsomes from chick liver or from cultured mouse fibroblasts. B3-tunicamycin also inhibited the incorporation of mannose into glycoproteins synthesized by chick or mouse fibroblasts. Incorporation of the amino acids proline and tyrosine was inhibited by B3-tunicamycin to a lesser extent than the incorporation of mannose. The mannose incorporation into glycoproteins synthesized by virally transformed cells was inhibited by B3-tunicamycin to a higher degree than what was achieved in the nontransformed lines or in the chick primary fibroblasts. When the activity of B3-tunicamycin as an inhibitor of protein glycosylation was compared to other homologues of tunicamycin, it was found to be the most active. This homologue caused complete (more than 95%) inhibition of protein glycosylation at a concentration of 50 ng/ml in chick and in mouse fibroblasts and at a concentration of 10 ng/ml in transformed mouse fibroblasts. When the cytotoxic activities of tunicamycin homologues were examined on nontransformed and virally transformed 3T3 cells, it was found that B3-tunicamycin displayed the highest selective cytotoxicity toward the transformed cells. When transformed fibroblasts (10(5) cells/plate) were treated with B3-tunicamycin (100 ng/ml) for 48 h, complete cell death was observed. The viability and the proliferative activity of the nontransformed fibroblast were normal even when treated with concentrations up to 500 ng/ml of B3-tunicamycin. This suggests that B3-tunicamycin may be a suitable candidate for studies of tumor growth in animals.

Lysosomal enzyme oligosaccharide phosphorylation in mouse lymphoma cells: specificity and kinetics of binding to the mannose 6-phosphate receptor in vivo

Phosphomannosyl residues on lysosomal enzymes serve as an essential component of the recognition marker necessary for binding to the mannose 6-phosphate (Man 6-P) receptor and translocation to lysosomes. The high mannose-type oligosaccharide units of lysosomal enzymes are phosphorylated by the following mechanism: N-acetylglucosamine 1-phosphate is transferred to the 6 position of a mannose residue to form a phosphodiester; then N- acetylglucosamine is removed to expose a phosphomonoester. We examined the kinetics of this phosphorylation pathway in the murine lymphoma BW5147.3 cell line to determine the state of oligosaccharide phosphorylation at the time the newly synthesized lysosomal enzymes bind to the receptor. Cells were labeled with [2-(3)H]mannose for 20 min and then chased for various times up to 4 h. The binding of newly synthesized glycoproteins to the Man 6-P receptor was followed by eluting the bound ligand with Man 6-P. Receptor-bound material was first detected at 30 min of chase and reached a maximum at 60 min of chase, at which time approximately 10 percent of the total phosphorylated oligosaccharides were associated with the receptor. During longer chase times, the total quantity of cellular phosphorylated oligosaccharides decreased with a half-time of 1.4 h, suggesting that the lysosomal enzymes had reached their destination and had been dephosphorylated. The structures of the phosphorylated aligosaccharides of the eluted ligand were then determined and compared with the phosphorylated oligosaccharides of molecules which were not bond to the receptor. The major phosphorylated oligosaccharide species present in the nonreceptor-bound material contained a single phosphosphodiester at all time examined. In contrast, receptor-bound oligosaccharides were greatly enriched in species possessing one and two phosphomonoesters. These results indicate that binding of newly synthesized lysosomal enzymes to the Man 6-P receptor occurs only after removal of the covering N- acetylglucosamine residues.

A microassay for UDP-N-acetylglucosamine pyrophosphorylase.

A rapid and sensitive radiochemical microassay for UDP-N-acetylglucosamine pyrophosphorylase (EC 2.7.7.23) activity was developed in which the rate of production of UDP-N-acetylglucosamine was monitored. In this direction the assay was suitable for measuring the amount of pyrophosphorylase activity in cellular extracts in the presence of pyrophosphatase. The Km values for UTP and N-acetylglucosamine 1-phosphate in extracts prepared from Candida albicans are 0.8 and 2.1 mM, respectively.

UDP-N-acetylglucosamine:glycoprotein N-acetylglucosamine-1-phosphotransferase. Proposed enzyme for the phosphorylation of the high mannose oligosaccharide units of lysosomal enzymes.

The recognition marker for the targeting of lysosomal enzymes contains mannose 6-phosphate. The recent discovery of phosphate in diester linkage between N-acetylglucosamine (GlcNAc) and mannose in newly synthesized beta-glucuronidase led to the proposal that the phosphate might be acquired via N-acetylglucosamine-phosphate transfer from UDP-GlcNAc (Tabas, I., and Kornfeld, S. (1980) J. Biol. Chem. 255, 6633-6639). We describe the synthesis of [beta-32P]UDP-[3H]GlcNAc and the use of this compound to demonstrate a UDP-GlcNAc:glycoprotein N-acetylglucosamine-1-phosphotransferase. The basis of the enzyme assay is the incorporation of 32P and 3H into glycopeptides with a high affinity for Concanavalin A-Sepharose. This membrane-associated transferase is neither inhibited by tunicamycin nor stimulated by dolichol-phosphate, indicating that the reaction does not proceed via a dolichylpyrophosphoryl-N-acetylglucosamine intermediate. Characterization of the enzyme reaction products (derived from either endogenous or exogenous acceptors) demonstrated that alpha-linked N-acetylglucosamine 1-phosphate is transferred en bloc to the 6-hydroxyl of mannose in high mannose oligosaccharides of glycoproteins. We propose that the function of this enzyme is to donate N-acetylglucosamine 1-phosphate to mannose residues of newly synthesized lysosomal enzymes.

Fibroblasts from patients with I-cell disease and pseudo-Hurler polydystrophy are deficient in uridine 5'-diphosphate-N-acetylglucosamine: glycoprotein N-acetylglucosaminylphosphotransferase activity.

Newly synthesized acid hydrolases, destined for transport to lysosomes, acquire a phosphomannosyl targeting signal by the transfer of N-acetylglucosamine 1-phosphate from uridine 5'-diphosphate (UDP)-N-acetylglucosamine to a mannose residue of the acid hydrolase followed by removal of the outer, phosphodiester-linked N-acetylglucosamine to expose 6-phosphomannose. This study demonstrates that fibroblasts from patients with the lysosomal enzyme storage diseases, I-cell disease (mucolipidosis II) and pseudo-Hurler polydystrophy (mucolipidosis III), are severely deficient in UDP-N-acetylglucosamine:glycoprotein N-acetylglucosaminylphosphotransferase, the first enzyme of the sequence. The N-acetylglucosaminylphosphotransferase activity (assayed using endogenous acceptors) in cultures from six normal subjects ranged from 0.67 to 1.46 pmol N-acetylglucosamine-1-phosphate transferred/mg protein per h, whereas five pseudo-Hurler polydystrophy and five I-cell disease cultures transferred less than 0.02 pmol/mg protein per h. The activity in five other pseudo-Hurler cultures ranged from 0.02 to 0.27 pmol transferred/mg protein per h. The activity of alpha-N-acetylglucosaminyl phosphodiesterase, the enzyme responsible for phosphomonoester exposure, is normal or elevated in cultured fibroblasts from both I-cell disease and pseudo-Hurler polydystrophy patients. The deficiency of UDP-N-acetylglucosamine:glycoprotein N-acetylglucosaminylphosphotransferase explains the biochemical abnormalities previously observed in I-cell disease and pseudo-Hurler polydystrophy.

The diagnosis of the Sanfilippo C syndrome, using monosaccharide and oligosaccharide substrates to assay acetyl-CoA: 2-amino-2-deoxy-α-glucoside N-acetyltransferase activity

Glucosamine, galactosamine, mannosamine, several disaccharides and a tetrasaccharide were evaluated as substrates for the N-acetyltransferase involved in the pathogenesis of the Sanfilippo C syndrome. Glucosamine and α- d-glucosaminide disaccharides and a tetrasaccharide derived from heparin were exo-N-acetylated by homogenates of cultured skin fibroblast from normal individuals at pH 6.0 in the presence of acetyl-CoA, whereas fibroblast homogenates prepared from a Sanfilippo C patient failed to catalyse the N-acetyltransferase from acetyl-CoA to these substrates. The apparent K m values of the glucosamine and α-glucosaminide disaccharide N-acetyltransferase were 98 and 200 μmol/l respectively; the corresponding V values were 200 and 180 nmolomin −1og −1 fibroblast whole cell homogenate protein respectively. Incubation of homogenates from normal individuals or the Sanfilippo C patient with glucosamine 6-phosphate and acetyl-CoA at pH 6.0 produced N-acetylglucosamine 6-phosphate. Acetyltransfer to glucosamine or glucosamine 6-phosphate in homogenates of normal fibroblasts was not inhibited by the addition of arylamines. It is proposed that N-acetyltransferase to glucosamine, glucosamine 6-phosphate and arylamines is carried out by separate enzymes. Glucosamine is a suitable substrate for the diagnostic assay of the enzyme involved in the exo-N-acetylation of α-glucosaminide residues at the non-reducing end of the heparan sulfate stored and excreted by Sanfilippo C patients.

Enzymatic phosphorylation of lysosomal enzymes in the presence of UDP-N-acetylglucosamine. Absence of the activity in l-cell fibroblasts

Recent finding of α-N-acetylglucosamine(1)phospho(6)mannose diesters in lysosomal enzymes suggested that formation of mannose 6-phosphate residues involves transfer of N-acetylglucosamine 1-phosphate to mannose. Using dephosphorylated β-hexosaminidase as acceptor and [β-32P]UDP-N-acetylglucosamine as donor for the phosphate group, phosphorylation of β-hexosaminidase by microsomes from rat liver, human placenta and human skin fibroblasts was achieved. The reaction was not affected by tunicamycin. Acid hydrolysis released mannose 6-[32P]phosphate from the phosphorylated β-hexosaminidase. Our results suggest that lysosomal enzymes are phosphorylated by transfer of N-acetylglucosamine 1-phosphate from UDP-N-acetylglucosamine. The transferase activity was deficient in fibroblasts from patients affected with l-cell disease. This deficiency is proposed to be the primary enzyme defect in l-cell disease.

N-Acetyl- d-glucosamine kinase and germ-tube formation in Candida albicans

N-Acetyl- d-glucosamine kinase (GlcNAc kinase, EC 2.7.1.59), the specific enzyme required for the phosphorylation of N-acetyl- d-glucosamine (GlcNAc) to N-acetylglucosamine 6-phosphate, was found to be an inducible enzyme in Candida albicans. The pattern of GlcNAc kinase induction was examined under conditions where germ-tube formation was elicited and where blastospores metabolized GlcNAc with no change in morphology. There was no change in either the time course or the extent of GlcNAc kinase induction, indicating that this enzyme is not a control point for the dimorphic development in C. albicans. A low basal level of GlcNAc kinase activity was found in noninduced cells of C. albicans but this increased 20- to 30-fold after the addition of GlcNAc to the cell suspension. GlcNAc is both an inducer and a substrate for the enzyme; ATP and Mg 2+ were also required for activity. The K mvalues for GlcNAc and ATP are 1.9 and 1.3 m m, respectively. ADP was found to be a noncompetitive inhibitor with respect to GlcNAc with a K ivalue of 7.1 m m. UDP-GlcNAc and glucosamine 6-phosphate had no effect on GlcNAc kinase activity. The presence of ethidium bromide (an inhibitor of transcription) or trichodermin (an inhibitor of translation) in cell suspensions of C. albicans inhibited the increase in GlcNAc kinase specific activity. The glucose analogs, α-methylglucopyranoside and 3- O-methylglucose, enhanced the formation of germ tubes by C. albicans but the induction of GlcNAc kinase was not affected. 2-Deoxyglucose, an inhibitor of germ-tube formation, had no effect on the induction of GlcNAc kinase.

Fate of oligosaccharide-lipid intermediates synthesized by resting rat-spleen lymphocytes.

Using conditions to avoid the utilization of labelled precursors by intracellular glycosyltransferases, experiments are described demonstrating that intact rat-spleen lymphocytes are capable of utilizing exogenous GDP-mannose and UDP-N-acetylglucosamine to synthesize dolichyl monophosphate mannose and dolichyl diphosphate oligosaccharides. Kinetic and chase experiments show that dolichyl diphosphate oligosaccharides are either utilized for the transfer of their carbohydrate moieties to protein acceptors or further degraded. Since glycosylation of proteins is limited in resting lymphocytes, the degradation pathway appears as a major event in the fate of the dolichyl diphosphate oligosaccharides synthesized in vitro. These dolichyl diphosphate oligosaccharides are degraded into phospho-oligosaccharides and oligosaccharides which are released in the medium. This enzymatic cleavage of the phosphodiester bond is inhibited by bacitracin. The phospho-oligosaccharides are susceptible to alkaline phosphatase giving neutral oligosaccharides and they are cleaved by endo-N-acetyl-beta-D-glucosaminidase H leaving N-acetylglucosamine 1-phosphate and neutral oligosaccharides. These data suggest that splitting of the phosphodiester bond of colichyl diphosphate oligosaccharides, dephosphorylation and/or endo-N-acetyl-beta-D-glucosaminidase hydrolysis of the phosphorylated oligosaccharides could represent the beginning of the catabolic pathway of dolichyl diphosphate oligosaccharides.

Concomitant synthesis and attachment of cell wall polymers by a membrane preparation from Micrococcus varians ATCC 29750

Membranes from Micrococcus varians catalyse the de novo synthesis of poly( N-acetylglucosamine 1-phosphate) attached to noncrosslinked peptidoglycan through a linkage unit of N-acetylglucosamine phosphate-tri(glycerol phosphate). The absence of CDP-glycerol, one of the precursors of linkage unit, precludes the attachment of the sugar 1-phosphate polymer. This report is the first of such polymer attachment performed by membranes which are completely free of cell walls.

The effects of triton X-100 on the transfer of mannose, glucose and N-acetylglusomine phosphate to dolichol monophosphate by preparations of rough and smooth endoplasmic reticulum and of mitochondria of rat liver

Triton X-100 and exogenous dolichol monophosphate have been used to investigate the nature of enzymes responsible for the transfer of mannose, glucose and N-acetylglucosamine phosphate from nucleotide donors to dolichol monophosphate in vesicles derived from rough and smooth endoplasmic reticulum and mitochondria. Mitochondria were shown to contain the highest specific activities of these enzymes. The responses of the glycosyltransferases to increasing concentrations of Triton X-100 and the effect on these responses of exogenous dolichol monophosphate suggest that the enzymes for mannose and glucose transfer are less hydrophobic, and therefore less intrinsic, in the membrane than the enzyme for N-acetylglucosamine phosphate transfer. In smooth vesicles the results are consistent with mannosyl- and glucosyl-transferases being located at both inner and outer faces of the membrane. In rough vesicles and in mitochondria mannosyl- and glucosyl-transferases were confirmed at the outer face. There is, however, only one site of N-acetylglucosamine phosphate transfer, this being more hydrophobically located in the membrane than the other sites of glycosyl transfer. Mitochondrial enzyme activity closely resembled that of rough endoplasmic reticulum in response to Triton X-100 and exogenous dolichol monophosphate, and is probably associated with the outer membrane.

Glucosamine itself mediates reversible inhibition of protein glycosylation. A study of glucosamine metabolism at inhibitory concentrations in influenza-virus-infected cells.

The metabolism of glucosamine in chick embryo fibroblasts was studied at different concentrations of the amino sugar added to the culture medium. In glucose-containing medium the well-known metabolites, UDP-N-acetylglucosamine, N-acetylglucosamine 6-phosphate and N-acetylglucosamine, are detectable after inhibition of glycosylation resulting from glucosamine treatment. Especially when the cells were infected with influenza virus, high intracellular concentrations of non-metabolized glucosamine are demonstrable in addition. Removal of the inhibitor from the medium results in release of the block of influenza virus glycoprotein glycosylation within 10 min. The onset of glycosylation is paralleled by a rapid reduction of intracellular levels of glucosamine without significant changes in the concentration of its metabolites. Furthermore, concentrations of GDP-mannose, UDP-glucose, and UDP-galactose remain constant for at least 30 min after reversal of the block. It is concluded that glucosamine as such exerts its effect on glycosylation, rather than one of its metabolites being responsible for this effect.

Biosynthesis of the linkage unit joining peptidoglycan to poly( N-acetylglucosamine 1-phosphate) in walls of Micrococcus varians ATCC 29750

Biosynthesis of the linkage unit joining peptidoglycan to poly( N-acetylglucosamine 1-phosphate) in walls of Micrococcus varians ATCC 29750

Glucosamine metabolism in Drosophila salivary glands separation of metabolites and some characteristics of three enzymes involved

The conversion of fructose 6-phosphate to mucopolysaccharide precursors was studied in extracts of Drosophila virilis salivary glands. 1.1. Methods for chromatography of sugar phosphates were adapted and modified to allow routine separation and quantification of radioactivity of the metabolites from milligram amounts of tissue. Anion exchange chromatography was performed on Dowex 1-X8 employing steps in increasing ammonium formate. Final isolation of each compound was achieved by various thin-layer chromatographic systems.2.2. Data obtained by isotope incorporation into glucosamine 6-phosphate compare well with results of the Morgan-Elson colorimetric assay for amino-sugars.3.3. Glucosaminephosphate isomerase (glutamine-forming) EC 5.3.1.19) in gland extracts has a Km of 0.35 mM for fructose 6-phosphate, and of 0.25 mM for glutamine. The enzyme is inhibited at glutamine concentrations exceeding 1 mM and by UDP-N-acetylglucosamine (50% at 0.6 mM). Feedback inhibition by UDP-N-acetylglucosamine is enhanced by AMP and by glucose 6-phosphate.4.4. Glucosaminephosphate isomerase (EC 5.3.1.10) has a twenty-fold lower affinity towards frucose 6-phosphate (Km = 6.0 mM) compared to the glutamine-forming isomerase. JKm(NH4+) is 7.4 mM. in the presence of 20 mM glucose 6-phosphate, the pH optimum is shifted from 6.6 to 7.4, and V increased by a factor of 2.5. Furthermore, the affinity is approximately doubled for both substrates.5.5. Glucosamine acetyltransferase (EC 2.3.1.3) has a Km of 2 mM for glucosamine 6-phosphate. Its activity is not rate-limiting in salivary glands. Since N-acetylglucosamine 6-phosphate and 1-phosphate were found near equilibrium concentrations, acetylglucosamine phosphomutase (EC 2.7.5.2) must also be present in the extracts.

The enzymic synthesis of β-[ 32P]UDP- N-acetylglucosamine

Cells of Micrococcus sp. 2102 incorporate inorganic [ 32P]phosphate from the medium into the sugar-phosphate polymer of the wall. Controlled acid hydrolysis of sodium dodecyl sulphate-extracted cells gives N-acetylglucosamine 6-[ 32P]phosphate which can be purified by ion-exchange chromatography and incubated with UTP in the presence of crude preparations of phosphoacetylglucosamine mutase from Neurospora crassa and UTP: N-acetylglucosamine 1-phosphate phosphotransferase from Bacillus licheniformis which act in concert to synthesise β-[ 32P]UDP- N-acetylglucosamine.

The presence of dolichol in a lipid diphosphate N-acetylglucosamine from Saccharomyces cerevisiae (baker's yeast)

The lipid moiety of a lipid diphosphate N-acetylglucosamine, an intermediate in glycosylation of proteins, was studied. Ozonolysis of the compound gave evidence for an alpha-saturated isoprene unit. Alkaline hydrolysis of the glycolipid, followed by high-pressure liquid chromatography, showed the presence of a series of polyprenol homologues identical with those isolated directly from Saccharomyces cerevisiae (baker's yeast). No particular homologue was preferred in the enzymic transfer of N-acetylglucosamine 1-phosphate to endogenous dolichol monophosphate.

The linkage of sugar phosphate polymer to peptidoglycan in walls of Micrococcus sp. 2102.

1. Protein-free walls of Micrococcus sp. 2102 contain peptidoglycan, poly-(N-acetylglucosamine 1-phosphate) and small amounts of glycerol phosphate. 2. After destruction of the poly-(N-acetylglucosamine 1-phosphate) with periodate, the glycerol phosphate remains attached to the wall, but can be removed by controlled alkaline hydrolysis. The homogeneous product comprises a chain of three glycerol phosphates and an additional phosphate residue. 3. The poly-(N-acetylglucosamine 1-phosphate) is attached through its terminal phosphate to one end of the tri(glycerol phosphate). 4. The other end of the glycerol phosphate trimer is attached through its terminal phosphate to the 3-or 4-position of an N-acetylglucosamine. It is concluded that the sequence of residues in the sugar 1-phosphate polymer-peptidoglycan complex is: (N-acetylglucosamine 1-phosphate)24-(glycerol phosphate)3-N-acetylglucosamine 1-phosphate-muramic acid (in peptidoglycan). Thus in this organism the phosphorylated wall polymer is attached to the peptidoglycan of the wall through a linkage unit comprising a chain of three glycerol phosphate residues and an N-acetylglucosamine 1-phosphate, similar to or identical with the linkage unit in Staphylococcus aureus H.

The presence of N-acetylglucosamine 1-phosphate in the linkage unit that connects teichoic acid to peptidoglycan in Staphylococcus aureus

The presence of N-acetylglucosamine 1-phosphate in the linkage unit that connects teichoic acid to peptidoglycan in Staphylococcus aureus