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Biomedical subjects

J Finne

Publications and source records attributed to J Finne.

At least 37 records · Page 2Linked to original sources
PubMed1993

Probing of the receptor-binding sites of the H1 and H3 influenza A and influenza B virus hemagglutinins by synthetic and natural sialosides.

To compare features of the receptor-binding sites (RBSs) of different influenza virus hemagglutinins (HA), binding of a number of synthetic sialic acid (SA) analogs and natural sialosides by a panel of about 30 human influenza A and B virus strains was studied in a competitive ligand binding assay. For all the viruses tested, the N-acetyl group of Neu5Ac, as well as the natural orientation of the carboxylic group at C2 and the hydroxylic group at C4, was essential for binding. Significant type- and subtype-specific differences were observed in virus recognition of asialic parts of sialosides. H1 strains, unlike H3 and type B viruses, were found to bind alpha 2-6-sialyl-N-acetyllactosamine with about an order of magnitude higher affinity than alpha 2-6-sialyllactose (6'SL). The H1 viruses and the H3 strains with Gln in position 226 of HA, but not the H3 strains with Leu-226, bound 6'SL with a lower affinity than alpha 2-3-sialyllactose; this effect correlated clearly with the preferential binding by the former viruses of unsubstituted alpha Neu5Ac compared to methyl alpha-glycoside of Neu5Ac. Thus, differentiation between the types of the SA-Gal linkage by the A viruses appeared to depend, at least partially, upon the recognition by the HA of the first hydrocarbon group of the aglycon. Type B virus strains were distinct in having a lower affinity for the Neu5Ac moiety and in providing a higher contribution of the asialic portions of sialosides to the HA-ligand interactions. The last effects are presumably due to the amino acid insertions in the type B HA surrounding the RBS, which makes the receptor-binding pocket deeper. The results obtained in the present investigation indicate that while the functional groups of Neu5Ac studied are recognized by the RBSs of all influenza viruses, the magnitude of their contribution to the binding energy, as well as the contribution of the asialic portion of the receptor, may vary in dependence upon the virus type, subtype, and strain.

Amino Acid Sequence↗
PubMed1992

Identification of N-acetylneuraminyl alpha 2-->3 poly-N-acetyllactosamine glycans as the receptors of sialic acid-binding Streptococcus suis strains.

Streptococcus suis is a common cause of sepsis, meningitis, and other serious infections in young piglets and also causes meningitis in humans. The cell-binding specificity of sialic acid-recognizing strains of Streptococcus suis was investigated. Treatment of human erythrocytes with sialidase or mild periodate abolished hemagglutination. Hemagglutination inhibition experiments with sialyl oligosaccharides indicated that the adhesin preferred the sequence NeuNAc alpha 2-3Gal beta 1-4Glc(NAc). Resialylation of desialylated erythrocytes with Gal beta 1-3(4)GlcNAc alpha 2-3-sialyltransferase induced a strong hemagglutination, whereas no or only weak hemagglutination was obtained with cells resialylated with two other sialyltransferases. Binding of radiolabeled bacteria to blots of erythrocyte membrane proteins revealed binding to the poly-N-acetyllactosamine-containing components Band 3, Band 4.5, and polyglycosyl ceramides and to glycophorin A. The involvement of glycophorin A as a major ligand was excluded by the strong hemagglutination of trypsin-treated erythrocytes and En(a-) erythrocytes defective in glycophorin A. Sensitivity of the hemagglutination toward endo-beta-galactosidase treatment of erythrocytes and inhibition by purified poly-N-acetyllactosaminyl glycopeptides indicated that the adhesin bound to glycans containing the following structure: NeuNAc alpha 2-3Gal beta 1-4GlcNAc beta 1-3Gal beta 1-.

Adhesins, Bacterial↗
PubMed1992

ABO blood groups and musculoskeletal injuries.

The distribution of the ABO blood groups was studied in 917 patients with specific musculoskeletal diagnoses. The ABO blood group distribution of patients with rupture of the Achilles tendon (P = 0.030) and of patients with chronic Achilles peritendinitis (P = 0.10) differed from the controls. The ABO blood group distribution was not associated with other musculoskeletal injuries studied. The blood group A/O ratio was 1.42 in the control population. In the group with rupture of the Achilles tendon this ratio was 1.0, and in the group with Achilles peritendinitis it was 0.70. The association between injuries of the Achilles tendon and the ABO blood group distribution was in accordance with an earlier report. There may be a genetic linkage between the ABO blood groups and the molecular structure of the tissue of Achilles tendons.

Achilles Tendon↗
PubMed1992

Differential activities of bacteriophage depolymerase on bacterial polysaccharide: binding is essential but degradation is inhibitory in phage infection of K1-defective Escherichia coli.

Host range mutants were derived from bacteriophages PK1A and PK1E specific for the K1 polysialic acid capsule of Escherichia coli. The mutants were selected for their ability to infect E. coli bacteria with a low level of the K1 capsule. A specific loss of the cleaving activity of the phage endosialidase was observed in all the mutants, while the ability to bind specifically to the polysialic acid capsule was retained. The results indicate that the polysaccharide-binding activity of the bacteriophage enzyme is essential for the infection process. The cleaving activity, in contrast, is required for the penetration of the dense polysaccharide of wild-type bacteria but is inhibitory in the infection of bacteria with a sparse capsular polysaccharide.

Bacterial Capsules↗
PubMed1991

Sugar analysis of glycoproteins and glycolipids after methanolysis by high-performance liquid chromatography with pulsed amperometric detection.

A procedure for the analysis of the monosaccharide composition of glycoproteins and glycolipids by methanolysis and high-performance liquid chromatography with pulsed amperometric detection is described. The advantage over previous methods is the analysis of underivatized methyl glycosides of all glycoconjugate monosaccharides including sialic acid and uronic acid in a single chromatographic step at the subnanomolar level.

Animals↗
PubMed1989

Novel polyfucosylated N-linked glycopeptides with blood group A, H, X, and Y determinants from human small intestinal epithelial cells.

A novel type of N-linked glycopeptides representing a major part of the glycans in human small intestinal epithelial cells from blood group A and O individuals were isolated by gel filtrations and affinity chromatography on concanavalin A-Sepharose and Bandeiraea simplicifolia lectin I-Sepharose. Sugar composition, methylation analysis, 1H NMR spectroscopy of the underivatized glycopeptides and FAB-mass spectrometry and electron impact-mass spectrometry of the permethylated glycopeptides indicated a tri- and tetra-antennary structure containing an intersecting N-acetylglucosamine and an alpha (1----6)-linked fucose residue in the core unit for the majority of the glycans. In contrast to most glycopeptides of other sources, the intestinal glycopeptides were devoid of sialic acid, but contained 6-7 residues of fucose. The outer branches contained the following structures: Fuc alpha 1-2Gal beta 1-3GleNAc beta 1- (H type 1) Fuc alpha 1-2Gal beta 1-4GleNAc beta 1- (H type 2) Gal beta 1-4 (Fuc alpha 1-3)GlcNAc beta 1- (X) Fuc alpha 1-2Gal beta 1-4(Fuc alpha 1-3)GleNAc beta 1- (Y) GalNAc alpha 1-3(Fuc alpha 1-2)Gal beta 1-3GleNAc beta 1- (A type 1) GalNAc alpha 1-3(Fuc alpha 1-2)Gal beta 1-4GleNAc beta 1- (monofucosyl A type 2) GalNAc alpha 1-3(Fuc alpha 1-2)Gal beta 1-4 (Fuc alpha 1-3)GlcNAc beta 1- (trifucosyl A type 2) The blood group determinant structures were mainly of type 2, whereas glycolipids from the same cells contained mainly type 1 determinants. The polyfucosylated glycans represent a novel type of blood group active glycopeptides. The unique properties of the small intestinal glycopeptides as compared with glycopeptides of other tissue sources may be correlated with the specialized functional properties of the small intestinal epithelial cells.

ABO Blood-Group System↗
PubMed1989

Lectin-resistant variants and revertants of mouse melanoma cells: differential expression of a fucosylated cell-surface antigen and altered metastasizing capacity.

In order to evaluate the possible role of cell-surface carbohydrates in metastasis of tumour cells, 2 wheat-germ agglutinin-resistant (WGAr) variants of B16 mouse melanoma and 8 back revertants selected with other lectins were analyzed with respect to the surface expression of fucosylated carbohydrate antigens and their metastasizing capacity. The variant cells, expressing a greatly increased fucosyltransferase activity, were found to express the fucose-containing SSEA-I antigen on their cell surface. The revertant cells selected for lower fucosylation with Lotus tetragonolobus lectin and ricin had lost this particular antigen. Seven of the 8 revertant lines also reverted back to a state of increased metastasizing capacity as compared to the WGAr variants they were derived from. A single one of the revertants displayed reduced metastasizing capacity, suggesting that additional changes can also be present in some of the cell lines. These results suggest a possible linkage between expression of the developmental SSEA-I antigen and reduced metastasizing capacity in the mouse melanoma model.

Animals↗
PubMed1989

Structural and biological properties of the carbohydrate units of nervous tissue glycoproteins.

We have identified structures in nervous tissue glycoproteins that are novel for glycoproteins in general or enriched in nervous tissue or cells of neural origin. These include: (alpha 2-8)-linked polysialic acid units, the linear form of poly-N-acetyllactosamine glycans, the sialylated X antigen determinant NeuAc(alpha 2-3)-Gal(beta 1-4) [Fuc(alpha 1-3)]GlcNAc, a series of Man-O-Ser(Thr)-linked glycans, and the O-glycosidically linked disaccharide unit Gal(alpha 1-3)GalNAc. The polysialic and poly-N-acetyllactosamine glycans are also developmentally regulated. The polysialic acid units in the cell adhesion molecule N-CAM. The poly-N-acetyllactosamine units occur in the adhesion molecule NILE (which is immunologically similar to Ng-CAM and L1) and in some other components revealed by a cell surface-labelling method specific for these glycans. The mannose-linked glycans occur in a chondroitin sulphate proteoglycan involved in neuron-glia interactions. Other biological interactions of the carbohydrates include their serving as bacterial receptors in meningitis, their serving as models for molecular mimicry by the capsules of meningitis-causing bacteria, and the role of some structures as antigens in autoimmune conditions. At the molecular level, two types of mechanisms are suggested for the glycans in molecular interactions: they may function either as mediators of interactions by serving as specific recognition ligands, or as modulators of the interactions determined by polypeptides or other molecules.

Animals↗
PubMed1989

Purification of the N-acetylglucosaminide alpha(1-3/4)fucosyltransferase of human milk.

The N-acetylglucosaminide alpha(1-3/4)fucosyltransferase has been purified 1.8 x 10(6)-fold from human milk by ion-exchange chromatography, affinity chromatography on GDP-agarose and HPLC. The alpha(1-3/4)fucosyltransferase behaves in gel filtration-HPLC as a molecule of M(r) 98,000, and differs from the alpha(1-3)fucosyltransferase which behaves like a molecule of about M(r) 47,000. The enzyme is a glycoprotein, and the purified preparation appears in SDS polyacrylamide gel electrophoresis as a band of M(r) 44,000. The results present the first purification of human milk alpha(1-3/4)fucosyltransferase to apparent homogeneity, and suggest that the alpha(1-3/4)- and alpha(1-3)fucosyltransferase of human milk differ in their native molecular sizes, the former being a dimer of two subunits.

Carbohydrate Conformation↗
PubMed1989

Interaction of meningococcal group B monoclonal antibody and its Fab fragment with alpha 2-8-linked sialic acid polymers: requirement of a long oligosaccharide segment for binding.

Mouse monoclonal IgG2a antibody (735D4) and other antibodies to the capsular polysaccharide of group B meningococci have been shown to require an unusually long segment of the alpha 2-8-linked N-acetylneuraminic acid polymer for binding. This property may be due to a conformational nature of the polysaccharide epitope recognized, or alternatively due to the requirement of bivalent binding of the antibody to the polysaccharide. In order to study the binding requirements, Fab fragments were prepared from the monoclonal antibody and their binding to alpha 2-8-linked sialic acid polymers of different lengths was studied. Both the intact antibody and its Fab fragment bound to sialic acid poly- and oligomers to similar extents, the critical chain length being about 10 sialyl units for both molecules. This excluded bivalency as the explanation for the requirement of a long oligosaccharide segment for binding. Although the binding was enhanced with increasing chain length, the first 10 monosaccharides were calculated to contribute to more than 90% of the total binding energy. This is in agreement with an oligosaccharide segment with defined conformational epitope binding to the antibody combining site. The antibody preparations also bound polysialic acid containing glycopeptides isolated from developing human and rat brain, suggesting, in quantitative binding assay, an average chain length of 10 or more sialic acid residues. The interaction of the antibody with both the bacterial and the tissue derived polysialic acids suggests that the conformational epitope critical for the interaction is formed by both classes of compounds.

Animals↗
PubMed1989

Structural similarity of the type-specific group B streptococcal polysaccharides and the carbohydrate units of tissue glycoproteins: evaluation of possible cross-reactivity.

Type-specific capsular polysaccharides of group B streptococci show striking structural similarity with the terminal sugar sequences of tissue glycoconjugates. The polysaccharides have been put forward as vaccines against neonatal meningitis. A potential source of hazard in immunization of pregnant mothers may be the presence of the cross-reactive components in adult or fetal tissues. A radioactive ligand binding assay was used to test human immune sera to type Ia, II and III group B streptococcal polysaccharides for binding to tissue-derived glycopeptides showing structural similarities with the streptococcal polysaccharides. Of the 13 glycopeptides of human and rat tissues studied, representing a wide selection of structures known to occur in glycoproteins, only two showed some reactivity with the antisera. The reactivity with human small intestinal glycopeptides could be explained by the presence of natural blood group A antibodies, and was not related to the streptococcal group B antibodies. The basis of the reactivity of a high-molecular-weight glycopeptide from rat kidney with some of the sera was unknown, but was unrelated to the vaccination and clearly could not be inhibited with the streptococcal polysaccharides. Thus, no immunological cross-reactions of the tissue glycopeptides studied could be demonstrated with the group B streptococcal antisera.

ABO Blood-Group System↗
PubMed1989

Hemagglutination activities of group B, C, D, and G streptococci: demonstration of novel sugar-specific cell-binding activities in Streptococcus suis.

A total of 378 streptococcal isolates of Lancefield groups B, C, D and G were tested for their ability to hemagglutinate untreated, sialidase-treated, and endo-beta-galactosidase-treated human erythrocytes. Of the 43 strains showing positive hemagglutination, 9 were inhibitable with neutral monosaccharides. Four strains were inhibited with galactose and N-acetylgalactosamine, whereas five were inhibited with galactose only. A third, sialic acid-specific adhesion activity was suggested for two additional strains on the basis of their agglutination of native and endo-beta-galactosidase-treated but not sialidase-treated erythrocytes. All the sugar-specific agglutination activities detected were confined to Streptococcus suis strains of group D streptococci, whereas streptococci of other groups did not exhibit these types of hemagglutination activities. The adhesins were sensitive to proteases and heat treatment, which indicates that they were proteins. The hemagglutinating isolates of S. suis originated from pig brain and lung, human brain, and the tonsils of healthy pigs. No clear correlation with a particular serotype was observed. These results demonstrate the occurrence of unique sugar-specific adherence activities in S. suis, an important pig pathogen with occasional human pathogenicity.

Adult↗
PubMed1989

Common cleavage pattern of polysialic acid by bacteriophage endosialidases of different properties and origins.

The cleavage specificities of seven bacteriophage endosialidases degrading the alpha 2-8-linked polysialic acid common to bacterial polysaccharides and to the cell adhesion molecule N-CAM were investigated. The bacteriophages studied represented five different phenotypic groups by protein and DNA fragment analysis and two different morphology groups by electron microscopy. Characterization of the fragments arising from the native or chemically modified substrates of different sizes showed that cleavage specificity was influenced by enzyme concentration. At the initial phase of degradation, at concentrations ranging from 20- to 100-fold, the minimum substrate size was an oligomer of eight (in one case, nine) sialic acid units that was preferably cleaved at the same position. Under exhaustive conditions, the oligomers were degraded further, and each enzyme type had its own specificity. The similar initial cleavage of polysialic acid by endosialidases associated with phages of different properties and morphology suggests a conserved mechanism of enzyme-substrate interaction. This mechanism may be conformationally determined and related to the specific properties of polysialic acid in other molecular interactions.

Bacteriophages↗
PubMed1988

Polyacrylamide gel electrophoresis of the capsular polysaccharides of Escherichia coli K1 and other bacteria.

Methods were developed for the polyacrylamide gel electrophoretic analysis of capsular polysaccharides of bacteria with Escherichia coli K1 as a model. Conditions were determined for the rapid and gentle extraction of the K1 polysaccharide by incubation of the bacteria in a volatile buffer and for the subsequent removal of the putative phospholipid moiety attached to the reducing end of the polysaccharide. Detection of the polysaccharides after gel electrophoresis was carried out by fluorography of samples labeled by sodium borotritiide reduction or by combined alcian blue and silver staining. The smallest components could be detected only by fluorography, owing to diffusion during staining. Components of the E. coli K1 polysialic acid capsule ranging from monomers to 80 sialic-acid-unit-containing polymers could be separated as distinct bands in a ladderlike pattern. A maximum chain length of 160 to 230 sialyl residues was estimated for the bulk of the K1 polysaccharide from the nearly linear reciprocal relationship between the logarithm of the molecular size and the distance of migration. Gel electrophoresis of capsular polysaccharides of other bacterial species revealed different electrophoretic mobilities for each polysaccharide, with a ladderlike pattern displayed by the fastest-moving components. There are many potential applications of this facile method for the determination of the sizes of molecules present in a polydisperse polysaccharide sample. When combined with the simple method for the isolation of the capsule, as in the case of the K1 capsule, it provides an efficient tool for the characterization and comparison of the capsular polysaccharides of bacteria.

Electrophoresis, Polyacrylamide Gel↗