Antigenic and structural relationships within group 19 Streptococcuspneumoniae: chemical characterization of the specific capsular polysaccharides of types 19B and 19C

1992 ◽  
Vol 70 (1) ◽  
pp. 218-232 ◽  
Author(s):  
Linda M. Beynon ◽  
James C. Richards ◽  
Malcolm B. Perry ◽  
Peter J. Kniskern
Keyword(s):  
Capsular Polysaccharide ◽  
Chemical Characterization ◽  
Structural Similarity ◽  
Cross Reactivity ◽  
Resonance Spectroscopy ◽  
Capsular Polysaccharides ◽  
Phosphate Diester ◽  
Structural Relationships ◽  
Nuclear Overhauser

The specific capsular polysaccharides of Streptococcuspneumoniae types 19B and 19C (American types 58 and 59) were investigated by a combination of 1H, 13C, and 31P nuclear magnetic resonance spectroscopy and analytical methods based on mass spectrometry. The two polysaccharides were found to be high molecular weight polymers composed of L-rhamnose, 2-amino-2-deoxy-D-mannose, D-ribose, D-glucose, and phosphate. Homo- and heteronuclear chemical shift correlation techniques and nuclear Overhauser enhancement experiments led to the unambiguous assignment of the 1H and 13C resonances from the glycose residues and established their sequence within repeating oligosaccharide units. The oligosaccharide units are polymerized through phosphate diester linkages.[Formula: see text]Both polysaccharides share a common hexasaccharide structural unit and they differ only in the degree of substitution at the branched 2-acetamido-2-deoxy-β-D-mannopyranosyl residue: the 19C polysaccharide is O-6 linked by β-D-glucopyranosyl end groups to form a heptasaccharide repeating unit, while the 19B polysaccharide is unsubstituted at that position. The serologic cross-reactivity between S. pneumoniae serotypes 19B and 19C can now be related to the structural similarity of the antigenic capsular polysaccharides. Keywords: Streptococcuspneumoniae, capsular polysaccharide, immuno chemistry.

scholarly journals Characterization of the structure and redox behaviour of cytochrome c3 from Desulfovibrio baculatus by 1H-nuclear-magnetic-resonance spectroscopy

1993 ◽  
Vol 294 (3) ◽  
pp. 899-908 ◽  
Author(s):  
I B Coutinho ◽  
D L Turner ◽  
J LeGall ◽  
A V Xavier
Keyword(s):  
Chemical Shifts ◽  
Three Dimensional ◽  
Dimensional Structure ◽  
Resonance Spectroscopy ◽  
Cytochrome C3 ◽  
X Ray ◽  
1H Nuclear Magnetic Resonance ◽  
Proton Resonances ◽  
Nuclear Overhauser

Complete assignment of the aromatic and haem proton resonances in the cytochromes c3 isolated from Desulfovibrio baculatus strains (Norway 4, DSM 1741) and (DSM 1743) was achieved using one- and two-dimensional 1H n.m.r. Nuclear Overhauser enhancements observed between haem and aromatic resonances and between resonances due to different haems, together with the ring-current contributions to the chemical shifts of haem resonances, support the argument that the haem core architecture is conserved in the various cytochromes c3, and that the X-ray structure of the D. baculatus cytochrome c3 is erroneous. The relative orientation of the haems for both cytochromes was determined directly from n.m.r. data. The n.m.r. structures have a resolution of approximately 0.25 nm and are found to be in close agreement with the X-ray structure from D. vulgaris cytochrome c3. The proton assignments were used to relate the highest potential to a specific haem in the three-dimensional structure by monitoring the chemical-shift variation of several haem resonances throughout redox titrations followed by 1H n.m.r. The haem with highest redox potential is not the same as that in other cytochromes c3.

Chemical Characterization of Capsular Polysaccharide fromCryptococcus neoformansSerotype A-D

1985 ◽  
Vol 29 (10) ◽  
pp. 981-991 ◽  
Author(s):  
Reiko Ikeda ◽  
Akemi Nishikawa ◽  
Takako Shinoda ◽  
Yoshimura Fukazawa
Keyword(s):  
Capsular Polysaccharide ◽  
Chemical Characterization

scholarly journals Development and Evaluation of a Tetraplex Flow Cytometric Assay for Quantitation of Serum Antibodies to Neisseria meningitidis Serogroups A, C, Y, and W-135

2004 ◽  
Vol 11 (2) ◽  
pp. 272-279 ◽  
Author(s):  
Gouri Lal ◽  
Paul Balmer ◽  
Helen Joseph ◽  
Maureen Dawson ◽  
Ray Borrow
Keyword(s):  
Neisseria Meningitidis ◽  
Capsular Polysaccharide ◽  
Cross Reactivity ◽  
Enzyme Linked Immunosorbent Assay ◽  
Capsular Polysaccharides ◽  
Simple Method ◽  
Serum Dilution ◽  
Flow Cytometric ◽  
Important Addition ◽  
Inhibition Studies

ABSTRACT A rapid and simple method for the simultaneous quantitation of serum immunoglobulin G (IgG) antibodies specific for Neisseria meningitidis serogroups A, C, Y, and W-135 was developed and evaluated. Four bead sets were generated, each conjugated with one of the meningococcal capsular polysaccharides (A, C, Y, or W-135) and serologically assessed by the use of antimeningococcal international reference sera. Cross-reactivity studies demonstrated no inhibition between monoplex and multiplex assays, and the assay was linear over a 24-fold serum dilution range. Inhibition studies demonstrated that the assay is specific, with <25% heterologous inhibition occurring. The assay was also found to have low intra- and interassay variations and limits of detection ≤650 pg/ml. A comparison of the meningococcal bead assay with the standardized meningococcal enzyme-linked immunosorbent assay showed a good correlation between the IgG concentrations obtained by each assay. The tetraplex assay has the potential to be an important addition to the serologic evaluation of meningococcal capsular polysaccharide conjugate vaccines.

Structural characterization of the antigenic capsular polysaccharide and lipopolysaccharide O-chain produced byActinobacillus pleuropneumoniaeserotype 15

2005 ◽  
Vol 83 (1) ◽  
pp. 61-69 ◽  
Author(s):  
Malcolm B Perry ◽  
Leann L MacLean ◽  
Evgeny Vinogradov
Keyword(s):  
Molecular Mass ◽  
Key Words ◽  
Structural Characterization ◽  
Capsular Polysaccharide ◽  
Actinobacillus Pleuropneumoniae ◽  
High Molecular Mass ◽  
O Antigen ◽  
Phosphate Diester ◽  
Nmr Methods

The specific capsular polysaccharide produced by Actinobacillus pleuropneumoniae serotype 15 was determined to be a high-molecular-mass polymer having [α]D+ 69° (water) and composed of a linear backbone of phosphate diester linked disaccharide units of 2-acetamido-2-deoxy-D-glucose (D-GlcNAc) and 2-acetamido-2-deoxy-D-galactose (D-GalNAc) residues (1:1). Thirty percent of the D-GalNAc residues were substituted at O-4 by β-D-galactopyranose (β-D-Galp) residues. Through the application of chemical and NMR methods, the capsule, which defines the serotype specificity of the bacterium, was found to have the structure                        [Formula: see text]The O-polysaccharide (O-PS) component of the A. pleuro pneumoniae serotype 15 lipopolysaccharide (LPS) was characterized as a linear unbranched polymer of repeating pentasaccharide units composed of D-glucose (2 parts) and D-galactose (3 parts), shown to have the structure[Formula: see text]The O-PS was chemically identical with the O-antigen previously identified in the LPSs produced by A. pleuro pneumoniae serotypes 3 and 8. Key words: Capsule, lipopolysaccharide, Actinobacillus pleuropneumoniae serotype 15.

scholarly journals Toxic peptides and genes encoding toxin γ of the Brazilian scorpions Tityus bahiensis and Tityus stigmurus

1996 ◽  
Vol 313 (3) ◽  
pp. 753-760 ◽  
Author(s):  
Baltazar BECERRIL ◽  
Miguel CORONA ◽  
Fredy I. V. CORONAS ◽  
Fernando ZAMUDIO ◽  
Emma S. CALDERONARANDA ◽  
...  
Keyword(s):  
Chemical Characterization ◽  
Large Degree ◽  
Cross Reactivity ◽  
Terminal Sequence ◽  
Cdna Sequences ◽  
Genes Encoding ◽  
Tityus Serrulatus ◽  
Toxic Peptides ◽  
Degree Of Similarity

Seven toxic peptides from the venom of Tityus bahiensis and Tityus stigmurus were isolated and sequenced, five of them to completion. The most abundant peptide from each of these two species of scorpion was 95% identical with that of toxin γ from the venom of Tityus serrulatus. They were consequently named γ-b and γ-st respectively. The genes encoding these new γ-like peptides were cloned and sequenced by utilizing oligonucleotides synthesized according to known cDNA sequences of toxin γ, and amplified by PCR on templates of DNA purified from both T. bahiensis and T. stigmurus. They contain an intron of approx. 470 bp. Possible mechanisms of processing and expressing these peptides are discussed, in view of the fact that glycine is the first residue of the N-terminal sequence of T. stigmurus, whereas lysine is the residue at position 1 of toxin γ from T. serrulatus and T. bahiensis. In addition, chemical characterization of the less abundant toxic peptides showed the presence of at least four distinct families of peptides in all three species of the genus Tityus studied. There is a large degree of similarity among peptides from different venoms of the same family. By using specific horse and rabbit antisera, the venoms of T. bahiensis, T. serrulatus and T. stigmurus were compared. They showed an extended degree of cross-reactivity. Thus these three species of scorpion have similar toxic components, the genes of which are similarly organized, processed and expressed.

Conformational and Structural characterization of carbohydrates and their interactions studied by NMR

2021 ◽  
Vol 28 ◽  
Author(s):  
Francisco Javier Cañada ◽  
Ángeles Canales ◽  
Pablo Valverde ◽  
Beatriz Fernández de Toro ◽  
Mónica Martínez-Orts ◽  
...  
Keyword(s):  
Structural Information ◽  
Theoretical Calculations ◽  
Chemical Shifts ◽  
Structural Complexity ◽  
Coupling Constants ◽  
Resonance Spectroscopy ◽  
Additional Information ◽  
Nuclear Overhauser ◽  
Nuclear Overhauser Effects

: Carbohydrates, either free or as glycans conjugated with other biomolecules, participate in many essential biological processes. Their apparent simplicity in terms of chemical functionality hides an extraordinary diversity and structural complexity. Deeply deciphering at the atomic level their structures is essential to understand their biological function and activities, but it is still a challenging task in need of complementary approaches and no generalized procedures are available to address the study of such complex, natural glycans. The versatility of Nuclear Magnetic Resonance spectroscopy (NMR) often makes it the preferred choice to study glycans and carbohydrates in solution media. The most basic NMR parameters, namely chemical shifts, coupling constants and nuclear Overhauser effects, allow defining short or repetitive chain sequences and characterize their structures and local geometries either in the free state or when interacting with other biomolecules, rendering additional information on the molecular recognition processes. The increased accessibility to carbohydrate molecules extensively or selectively labeled with 13C boosts the resolution and detail that analyzed glycan structures can reach. In turn, structural information derived from NMR, complemented with molecular modeling and theoretical calculations can also provide dynamic information on the conformational flexibility of carbohydrate structures. Furthermore, using partially oriented media or paramagnetic perturbations, it has been possible to introduce additional long-range observables rendering structural information on longer and branched glycan chains. In this review, we provide examples of these studies and an overview of the recent and most relevant NMR applications in the glycobiology field.

Chemical and morphological characterization of sugar cane bagasse

TAPPI Journal ◽  
2014 ◽  
Vol 13 (6) ◽  
pp. 27-33 ◽  
Author(s):  
MARCELA FREITAS ANDRADE ◽  
JORGE LUIZ COLODETTE ◽  
HASAN JAMEEL
Keyword(s):  
Sugar Cane ◽  
Chemical Characterization ◽  
Fiber Material ◽  
Short Fiber ◽  
Morphological Characterization ◽  
Sugar Cane Bagasse ◽  
Resonance Spectroscopy ◽  
Lignin Composition ◽  
Physical And Chemical

The sugar cane industry in Brazil is expanding, leading to great interest in using the leftover bagasse for other uses, beyond burning it for its energy. A thorough physical and chemical characterization of bagasse, particularly regarding its lignin structure, is relevant for a more rational utilization of the bagasse in the production of printing and writing pulp grades, dissolving pulp, ethanol, and power. The main goals of this study were characterizing the chemical (pith and fibers fractions) and morphologic (fibers fraction) properties of the sugar cane bagasse and the structure of the depithed bagasse lignin by two-dimensional nuclear magnetic resonance spectroscopy. Industrial whole bagasse was separated into two fractions: pith and depithed bagasse. The pith was only characterized chemically. The depithed bagasse was chemically and morphologically characterized. The cellulose, hemicelluloses, and lignin contents of the two materials varied significantly. The lignin composition of the depithed bagasse showed very high contents of phenolic cinnamic acids (PCAs). The depithed bagasse lignin presented fractions with different structural monomer distributions. The morphological analyses of the depithed bagasse indicated a short fiber material, similar to hardwoods.

scholarly journals The capsular polysaccharides of Pasteurella multocida serotypes B and E: Structural, genetic and serological comparisons

Glycobiology ◽  
2020 ◽  
Author(s):  
Frank St Michael ◽  
Chantelle M Cairns ◽  
Perry Fleming ◽  
Evgeny V Vinogradov ◽  
John D Boyce ◽  
...  
Keyword(s):  
Nuclear Magnetic Resonance ◽  
Structural Analysis ◽  
Magnetic Resonance ◽  
Pasteurella Multocida ◽  
Repeat Unit ◽  
Resonance Spectroscopy ◽  
Capsular Polysaccharides ◽  
Serotype B

Abstract We describe the structural characterization of the capsular polysaccharides (CPSs) of Pasteurella multocida serotypes B and E. CPS was isolated following organic solvent precipitation of the supernatant from flask grown cells. Structural analysis utilizing nuclear magnetic resonance spectroscopy enabled the determination of the CPS structures and revealed significant structural similarities between the two serotypes, but also provided an explanation for the serological distinction. This observation was extended by the development of polyclonal sera to the glycoconjugate of serotype B CPS that corroborated the structural likenesses and differences. Finally, identification of these structures enabled a more comprehensive interrogation of the genetic loci and prediction of roles for some of the encoded proteins in repeat unit biosynthesis.

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