Isolation and characterization by electrospray-ionization mass spectrometry and high-performance anion-exchange chromatography of oligosaccharides derived from hyaluronic acid by hyaluronate lyase digestion: Observation of some heretofore unobserved oligosaccharides that contain an odd number of units

Price, Kenneth N.; Tuinman, Al; Baker, David C.; Chisena, Christina; Cysyk, Richard L.

doi:10.1016/s0008-6215(97)00171-7

Cited by 56 publications

(49 citation statements)

References 27 publications

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“…In addition to the overlapping components tetradeca-and decasaccharide, two other unusual minor components, HA trideca-and undecasaccharide, were also observed (21). The minor components in B12 (Fig.…”

Section: Resultsmentioning

confidence: 92%

Inhibition of Adhesion of Plasmodium falciparum -Infected Erythrocytes by Structurally Defined Hyaluronic Acid Dodecasaccharides

et al. 2001

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We recently reported that Plasmodium falciparum-infected erythrocytes (IRBCs) can adhere to hyaluronic acid (HA), which appears to be a receptor, in addition to chondroitin sulfate A (CSA), for parasite sequestration in the placenta. Further investigations of the nature and specificity of this interaction indicate that HA oligosaccharide fragments competitively inhibit parasite adhesion to immobilized purified HA in a sizedependent manner, with dodecasaccharides being the minimum size for maximum inhibition. Rigorously purified and structurally defined HA dodecasaccharides, free of contamination by CSA or other glycosaminoglycans, effectively inhibited IRBC adhesion to HA but not CSA, providing compelling evidence of a specific interaction between IRBCs and HA.A characteristic of infection with the malaria parasite Plasmodium falciparum is the ability of parasite-infected erythrocytes (IRBCs) to adhere to host endothelial cells and accumulate in various organs. During pregnancy, the accumulation of IRBCs in the placenta is a key feature of infection and is associated with adverse outcomes and excess perinatal and maternal mortality (6,18). Studies in Africa suggest that sequestration of IRBCs in the placenta is mediated in part by adhesion of parasites to the glycosaminoglycan (GAG) chondroitin sulfate A (CSA) present on syncytiotrophoblasts lining the placental blood spaces (2, 11).We have recently reported that hyaluronic acid (HA) can also support the adhesion of IRBCs in vitro and appears to be an additional receptor for parasite sequestration in the placenta (4). HA is nonsulfated and is the simplest member of the GAG family composed of repeating disaccharide units, -4GlcA␤1-3GlcNAc␤1-, in a linear chain that varies in size from 2,000 to 25,000 disaccharide units. It has been identified on syncytiotrophoblasts (17, 28), and we found that most parasite isolates from infected placentas bound to immobilized HA, whereas isolates from the peripheral blood bound to a lesser extent (4). HA is also present on the surfaces of microvascular endothelial cells (19), raising the possibility that it acts as a receptor for parasite sequestration in other organs.To further investigate the nature and specificity of the interaction of HA with IRBCs, we generated oligosaccharide fragments, including high-performance liquid chromatography (HPLC)-purified and structurally defined dodecasaccharides, and examined their abilities to competitively inhibit parasite adhesion to immobilized HA. Some HA preparations can be contaminated with other GAGs, such as CSs, and it was therefore important to exclude the possibility that the adhesion observed could be explained by such contaminants. MATERIALS AND METHODSPartial depolymerization of HA. HA (from bovine vitreous humor; Sigma) (HA-BVH) was partially depolymerized by controlled digestion with either testicular hyaluronidase (EC 3.2.1.35; from bovine testes; Sigma) or hyaluronate lyase (EC 4.2.2.1; from Streptomyces hyalurolyticus; Sigma). Testicular hyaluronidase digestion was carried...

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Section: Resultsmentioning

confidence: 92%

Inhibition of Adhesion of Plasmodium falciparum -Infected Erythrocytes by Structurally Defined Hyaluronic Acid Dodecasaccharides

et al. 2001

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“…† Rcryst ϭ ͚ʈFobs͉ Ϫ ͉Fcalcʈ͚͉͞Fobs͉. Identification of hyaluronan oligosaccharides, over a range of time points from 0 min to 24 h, was achieved by using electrospray mass spectrometry (42) with the degree of polymerization of product shown. ‫,ء‬ artifact.…”

Section: Resultsmentioning

confidence: 99%

Structure of a group A streptococcal phage-encoded virulence factor reveals a catalytically active triple-stranded β-helix

Smith

Taylor

Lindsay

et al. 2005

Proc. Natl. Acad. Sci. U.S.A.

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Streptococcus pyogenes (group A Streptococcus) causes severe invasive infections including scarlet fever, pharyngitis (streptococcal sore throat), skin infections, necrotizing fasciitis (flesh-eating disease), septicemia, erysipelas, cellulitis, acute rheumatic fever, and toxic shock. The conversion from nonpathogenic to toxigenic strains of S. pyogenes is frequently mediated by bacteriophage infection. One of the key bacteriophage-encoded virulence factors is a putative ''hyaluronidase,'' HylP1, a phage tail-fiber protein responsible for the digestion of the S. pyogenes hyaluronan capsule during phage infection. Here we demonstrate that HylP1 is a hyaluronate lyase. The 3D structure, at 1.8-Å resolution, reveals an unusual triple-stranded ␤-helical structure and provides insight into the structural basis for phage tail assembly and the role of phage tail proteins in virulence. Unlike the triple-stranded ␤-helix assemblies of the bacteriophage T4 injection machinery and the tailspike endosialidase of the Escherichia coli K1 bacteriophage K1F, HylP1 possesses three copies of the active center on the triple-helical fiber itself without the need for an accessory catalytic domain. The triple-stranded ␤-helix is not simply a structural scaffold, as previously envisaged; it is harnessed to provide a 200-Å-long substrate-binding groove for the optimal reduction in hyaluronan viscosity to aid phage penetration of the capsule.crystal ͉ enzyme ͉ lyase ͉ streptococcus ͉ bacteriophage

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“…will not act upon CS and therefore oligosaccharide identity may be confirmed by enzyme specificity. Price et al (1997) previously examined HA oligosaccharides up to hexadecasaccharide by HPAEC, however a prior SEC step was required as differently sized HA oligosaccharides coelute.…”

Section: Resultsmentioning

confidence: 99%

A fingerprinting method for chondroitin/dermatan sulfate and hyaluronan oligosaccharides

Lauder¹,

Huckerby²,

Nieduszynski³

2000

Glycobiology

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A previously published method for the analysis of glycosaminoglycan disaccharides by high pH anion exchange chromatography (Midura,R.J., Salustri,A., Calabro,A., Yanagishita,M. and Hascall,V.C. (1994), Glycobiology, 4, 333-342) has been modified and calibrated for chondroitin and dermatan sulfate oligosaccharides up to hexasaccharide in size and hyaluronan oligosaccharides up to hexadecasaccharide. For hyaluronan oligosaccharides chain length controls elution position; however, for chondroitin and dermatan sulfate oligosaccharides elution times primarily depend upon the level of sulfation, although chain length and hence charge density plays a role. The sulfation position of GalNAc residues within an oligosaccharide is also important in determining its elution position. Compared to 4-sulfation a reducing terminal 6-sulfate retards elution; however, when present on an internal GalNAc residue it is the 4-sulfate containing oligosaccharide which elutes later. These effects allow discrimination between oligosaccharides differing only in the position of GalNAc sulfation. Using this simple methodology, a Dionex CarboPac PA-1 column with NaOH/NaCl eluents and detection by absorbance at 232 nm, a quantitative analytical fingerprint of a chondroitin/dermatan sulfate chain may be obtained, allowing a determination of the abundance of chondroitin sulfate, dermatan sulfate, and hyaluronan along with an analysis of structural features with a linear response to ∼0.1 nmol. The method may readily be calibrated using either commercial disaccharides or the di-and tetrasaccharide products of a limit digest of commercial chondroitin sulfate by chondroitin ABC endolyase. Commercially available and freshly prepared shark, whale, bovine, and human cartilage chondroitin sulfates have been examined by this methodology and we have confirmed that freshly isolated shark cartilage CS contains significant amounts of the biologically important GlcA2Sβ(1-3)GalNAc6S structure.

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Cited by 56 publications

References 27 publications

Inhibition of Adhesion of Plasmodium falciparum -Infected Erythrocytes by Structurally Defined Hyaluronic Acid Dodecasaccharides

Inhibition of Adhesion of Plasmodium falciparum -Infected Erythrocytes by Structurally Defined Hyaluronic Acid Dodecasaccharides

Structure of a group A streptococcal phage-encoded virulence factor reveals a catalytically active triple-stranded β-helix

A fingerprinting method for chondroitin/dermatan sulfate and hyaluronan oligosaccharides

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