By François-Xavier Theillet, Pierre Chassagne (auth.), Paul Kosma, Sven Müller-Loennies (eds.)
Many pathogens and aberrant malignant cells show exact carbohydrates on their floor representing beautiful goals for vaccine layout. enormous growth has lately been made within the id of novel carbohydrate dependent vaccines and a multitude has reached scientific part reviews. The good fortune of a number of authorized carbohydrate dependent vaccines opposed to bacterial pathogens similar to Haemophilus influenzae variety b, Neisseria meningitidis or Streptococcus pneumoniae demonstrates their nice strength. besides the fact that, the research of anti-carbohydrate antibodies is technically difficult and partially as a result of low affinities and promiscuous specificity they've got no longer been medically exploited to complete capability. The examine of antibody specificities and id of protecting carbohydrate epitopes lies on the middle of profitable vaccine layout. as well as remedy, antibodies more often than not function diagnostic instruments in clinical and clinical laboratories. during this surroundings excessive affinity and beautiful specificity are very important components for his or her profitable use. “Anticarbohydrate Antibodies – from molecular foundation to medical software” compiles present wisdom at the immunological reputation of carbohydrates through the adaptive immune process from a molecular point of view delivering primary perception wanted for advancing clinically proper diagnostics and healing purposes. in response to major development within the fields of glycoimmunology and structural biology in recent times, the e-book comprehensively stories the cutting-edge in defining the major components of carbohydrate popularity via antibodies, the molecular mimicry of carbohydrate epitopes in addition to the molecular positive aspects resulting in particular and secure binding modes. Backed-up through a mix of contemporary applied sciences to clarify structural info of carbohydrate-antibody interactions, biomedically vital carbohydrate antigens from viral, bacterial, parasite, insect and tumor cells were analyzed in in-depth stories written by way of recognized specialists within the box. basic wisdom of those molecular mechanisms ultimately presents a rational foundation to enhance efficacy of carbohydrate-based vaccines and to additional refine diagnostic instruments in detection of pathogens and malignant cells.
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Extra info for Anticarbohydrate Antibodies: From Molecular Basis to Clinical Application
Proc Natl Acad Sci USA 97:8433–8438 Vulliez-Le Normand B, Saul FA, Phalipon A, Belot F, Guerreiro C, Mulard LA, Bentley GA (2008) Structures of synthetic O-antigen fragments from serotype 2a Shigella flexneri in complex with a protective monoclonal antibody. Proc Natl Acad Sci USA 105:9976–9981 Vyas NK, Vyas MN, Chervenak MC, Johnson MA, Pinto BM, Bundle DR, Quiocho FA (2002) Molecular recognition of oligosaccharide epitopes by a monoclonal Fab specific for Shigella flexneri Y lipopolysaccharide: X-ray structures and thermodynamics.
Contacting or buried atoms of the Ab are in deep blue. Residues A2, B2, and C2 are represented with green carbons, residues D2 with yellow carbons and residues E2 with magenta carbons. Left: Model of the interaction of F22-4 with an O-Ag segment extended at the nonreducing side of the decasaccharide (Vulliez-Le Normand et al. 2008). This extension was built with dihedral angles set to the values adopted by the corresponding glycosidic linkages in the crystal. For the sake of visibility, residues of the extension are alternatively represented with cyan and black carbons 1 Multidisciplinary Approaches to Study O-Antigen 25 the SYA/J6:A2B2C2D2A20 complex (Vyas et al.
2002) 1 Multidisciplinary Approaches to Study O-Antigen 19 although the minimal OS size necessary for inhibition varied from one Ab to another. Groove type combining site Abs recognizing intrachain antigenic determinants were hypothesized. In agreement with the observed differences in epitope size, LPS crossreactivities were at variance. In particular, MASF Y2, which accommodates epitopes larger than an octasaccharide had a specificity restricted to SFY. Overall, in addition to emphasizing the contributions of well-characterized OSs in probing the fine specificity of O-Ag:Ab complementarity, these findings revealed the complexity of the SFY O-Ag antigenic repertoire (Carlin et al.