Immunochemical characterization of polyclonal and monoclonal Streptococcus group A antibodies by chemically defined glycoconjugates and synthetic oligosaccharides

Reimer, Kerry B.; Gidney, M. A. J.; Bundle, David R.; Pinto, B. Mario

doi:10.1016/s0008-6215(00)91000-0

Cited by 32 publications

(31 citation statements)

References 16 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…It is plausible that antibody maturation upon repeated exposure in the human subjects was responsible for the narrow epitope specificities. As previously observed (8,24,27), the results also indicate that the branch point and the size of the GAS antigen are crucial elements of the epitope recognized by both polyclonal human and rabbit antibodies.…”

Section: Vol 73 2005 Epitope On Cell Wall Polysaccharide Of Gas 6387supporting

confidence: 84%

“…1) has indicated that the branch point and the size of the GAS antigen are crucial elements of the epitope recognized by both rabbit polyclonal and mouse monoclonal antibodies that bind the native polysaccharide antigen (8,24,27). Conformational analysis has shown that the branch point represented in the trisaccharide repeating motif of the polysaccharide is a well-defined conformational feature both in the free ligand form and when the compound is bound to an antibody (15,31,36).…”

mentioning

confidence: 99%

See 1 more Smart Citation

Doubly Branched Hexasaccharide Epitope on the Cell Wall Polysaccharide of Group A Streptococci Recognized by Human and Rabbit Antisera

et al. 2005

View full text Add to dashboard Cite

A number of epitope specificities associated with the cell wall polysaccharide antigen of group A streptococci were identified in a polyclonal rabbit antiserum induced in rabbits by whole group A streptococci and in polyclonal convalescent human antisera from children that had recovered from streptococcal A infections. The identification was achieved by using a series of synthetic oligosaccharides, glycoconjugates, and bacterial polysaccharide inhibitors to inhibit the binding of the group A helical polysaccharide to the polyclonal antisera. The exclusively dominant epitope expressed in the convalescent human antisera was the doubly branched extended helical hexasaccharide with the structure ␣-L-Rhap (132) (133)]␣-L-Rhap, although both these haptens bound significantly to the same rabbit antiserum, albeit with less immunoreactivity than the hexasaccharide. Inhibition studies using streptococcal group A and B rabbit antisera and the inhibitors indicated above also suggested that the group A carbohydrate, unlike the group B streptococcal polysaccharide, does not contain the disaccharide ␣-L-Rhap(132)␣-L-Rhap motif at its nonreducing chain terminus, stressing the importance of mapping the determinant specificities of these two important streptococcal subcapsular group polysaccharides to fully understand the serological relationships between group A and group B streptococci.

show abstract

Section: Vol 73 2005 Epitope On Cell Wall Polysaccharide Of Gas 6387supporting

confidence: 84%

mentioning

confidence: 99%

Doubly Branched Hexasaccharide Epitope on the Cell Wall Polysaccharide of Group A Streptococci Recognized by Human and Rabbit Antisera

et al. 2005

View full text Add to dashboard Cite

show abstract

“…glycosyl residues (Kabat, 1966;Reimer et al, 1992;Puhlmann et al, 1994;Steffan et al, 1995;Clausen et al, 2003). Different polysaccharide preparations will vary in both the types of epitopes (structural features) present and the amounts of each epitope.…”

Section: Discussionmentioning

confidence: 99%

A Comprehensive Toolkit of Plant Cell Wall Glycan-Directed Monoclonal Antibodies

et al. 2010

View full text Add to dashboard Cite

A collection of 130 new plant cell wall glycan-directed monoclonal antibodies (mAbs) was generated with the aim of facilitating in-depth analysis of cell wall glycans. An enzyme-linked immunosorbent assay-based screen against a diverse panel of 54 plant polysaccharides was used to characterize the binding patterns of these new mAbs, together with 50 other previously generated mAbs, against plant cell wall glycans. Hierarchical clustering analysis was used to group these mAbs based on the polysaccharide recognition patterns observed. The mAb groupings in the resulting cladogram were further verified by immunolocalization studies in Arabidopsis (Arabidopsis thaliana) stems. The mAbs could be resolved into 19 clades of antibodies that recognize distinct epitopes present on all major classes of plant cell wall glycans, including arabinogalactans (both protein-and polysaccharide-linked), pectins (homogalacturonan, rhamnogalacturonan I), xyloglucans, xylans, mannans, and glucans. In most cases, multiple subclades of antibodies were observed to bind to each glycan class, suggesting that the mAbs in these subgroups recognize distinct epitopes present on the cell wall glycans. The epitopes recognized by many of the mAbs in the toolkit, particularly those recognizing arabinose-and/or galactose-containing structures, are present on more than one glycan class, consistent with the known structural diversity and complexity of plant cell wall glycans. Thus, these cell wall glycan-directed mAbs should be viewed and utilized as epitope-specific, rather than polymer-specific, probes. The current world-wide toolkit of approximately 180 glycan-directed antibodies from various laboratories provides a large and diverse set of probes for studies of plant cell wall structure, function, dynamics, and biosynthesis.

show abstract

“…Streptococcus pyogenes Group A type 4, strain J17A4 bacteria were heat-killed and pepsin-digested to expose the cell-wall polysaccharide, as described [21,25] ; kindly provided by Pitner [26] . The original treatment with pepsin was reported by Krause et al [25] , to remove most of protein and expose the cellwall carbohydrate antigens.…”

Section: Methodsmentioning

confidence: 99%

“…1), cross-reactive with an anti-CWPS monoclonal antibody, SA-3, was identified [20] . SA-3 recognizes a branched trisaccharide repeating unit L-Rha-α-(1→2)-[D-GlcNAc-β-(1→3)]-α-L-Rha as an epitope [21] . Detailed immunochemical studies of the recognition of DRPVPY by SA-3 showed that the mechanism of peptide binding differs from that of the carbohydrate [20] .…”

Section: Introductionmentioning

confidence: 99%

Immunological Evidence for Peptide-Carbohydrate Mimicry with a Group A Streptococcus Polysaccharide-Mimetic Peptide

Borrelli¹,

Hossany²,

Findlay³

et al. 2006

American J. of Immunology

View full text Add to dashboard Cite

Abstract:The immunogenicity of a peptide-protein conjugate developed by linking a peptide mimic DRPVPY of the Group A Streptococcus cell-wall polysaccharide (GAS-CWPS), to tetanus toxoid (TT) was examined. BALB/c mice were immunized three times subcutaneously following homologous or heterologous prime/boost strategies at 4-or 6-week intervals in two different experiments. DRPVPY-TT, CWPS-TT, heat-killed, pepsin-treated GAS bacteria (with exposed polysaccharide) and TT, were used as immunogens with alum as adjuvant. Antibody titers were determined by ELISA with GAS bacteria (with exposed polysaccharide) and DRPVPY-linked to bovine serum albumin (BSA, DRPVPY-BSA) as solid phase antigens. All mice primed with DRPVPY-TT developed high IgG antipeptide and anti-GAS titers. The binding of polyclonal anti-peptide antibodies to GAS could be inhibited by purified CWPS, synthetic oligosaccharides corresponding to CWPS, DRPVPY-BSA, DRPVPY and DRPVP, as assessed by competitive-inhibition ELISA. Anti-oligosaccharide titers were also obtained upon titration of anti-peptide sera with synthetic oligosaccharide-BSA conjugates. All mice primed with CWPS-TT and mice primed and boosted with GAS developed IgG anti-peptide titers. These data demonstrate conclusively the cross-reactivity of the immune responses and support the hypothesis of antigenic mimicry of the GAS-CWPS by the hexapeptide DRPVPY. However, mice boosted with DRPVPY-TT, after 6-8 weeks, showed a decrease in IgG anti-GAS titers, but an increase in IgG anti-peptide titers, suggesting carrier-induced suppression of the response to polysaccharide. Strategies are outlined for further refinement of a DRPVPY conjugate as a surrogate of the cell-wall polysaccharide for use in vaccines against Group A Streptococcus.

show abstract

Immunochemical characterization of polyclonal and monoclonal Streptococcus group A antibodies by chemically defined glycoconjugates and synthetic oligosaccharides

Cited by 32 publications

References 16 publications

Doubly Branched Hexasaccharide Epitope on the Cell Wall Polysaccharide of Group A Streptococci Recognized by Human and Rabbit Antisera

Doubly Branched Hexasaccharide Epitope on the Cell Wall Polysaccharide of Group A Streptococci Recognized by Human and Rabbit Antisera

A Comprehensive Toolkit of Plant Cell Wall Glycan-Directed Monoclonal Antibodies

Immunological Evidence for Peptide-Carbohydrate Mimicry with a Group A Streptococcus Polysaccharide-Mimetic Peptide

Contact Info

Product

Resources

About