Online citations, reference lists, and bibliographies.

Mapping Epitope Structure And Activity: From One-Dimensional Prediction To Four-Dimensional Description Of Antigenic Specificity

M. H. Regenmortel
Published 1996 · Biology

Cite This
Download PDF
Analyze on Scholarcy
Share
Abstract Our knowledge of antigenic specificity has greatly increased in recent years mainly through X-ray crystallographic studies of proteins and peptides complexed with monoclonal antibodies. However, our ability to predict the location of antigenic sites in proteins remains limited partly because prediction algorithms reduce the complexity of epitopes to one-dimensional, linear peptide models. Epitopes and paratopes are relational entities definable by their mutual complementarity and adaptation potential as well as by their activity. A complete account of antigenic specificity demands the integration of both structural and binding activity data that can be achieved only through a spatiotemporal four-dimensional analysis. Failure to include the fourth dimension, i.e., time, in the analysis of antigen–antibody complementarity amounts to considering proteins as rigid bodies and ignores the mutual adaptation that occurs when the two partners interact. Reducing four-dimensional protein systems to three-dimensional or two-dimensional representations inevitably distorts our perception of the dynamic nature of epitopes.



This paper is referenced by
10.1002/pro.716
Generation of monospecific antibodies based on affinity capture of polyclonal antibodies.
Barbara Hjelm (2011)
10.1110/ps.073347208
The epitope space of the human proteome.
Lisa Berglund (2008)
10.1016/j.vaccine.2009.10.135
Design of antibody-reactive peptides from discontinuous parts of scorpion toxins.
L. Alvarenga (2010)
10.1016/J.JMB.2003.09.002
The mapping and reconstitution of a conformational discontinuous B-cell epitope of HIV-1.
D. Enshell-Seijffers (2003)
Analysis Of Ige Reactivity To Pru Du 6, An 11s Globulin From Almond Nut, And Identification Of Both Sequential And Conformational Epitopes
L. N. Willison (2013)
10.1107/97809553602060000706
Molecular‐dynamics simulations of biological macromolecules
C. Post (2006)
10.1201/9780203212196.CH1
Principles of antigens antibody recognition
D. Altschuh (2002)
10.3109/08916934.2012.682667
Localization of key amino acid residues in the dominant conformational epitopes on thyroid peroxidase recognized by mouse monoclonal antibodies
Marlena Godlewska (2012)
10.1002/jmr.2210
Epitope structure and binding affinity of single chain llama anti-β-amyloid antibodies revealed by proteolytic excision affinity-mass spectrometry.
Gabriela Paraschiv (2013)
10.13130/SCARABELLI-GUIDO_PHD2010-12-15
MOLECULAR DYNAMICS SIMULATIONS OF BIOLOGICAL MACROMOLECULES: APPLICATIONS TO STRUCTURAL VACCINOLOGY AND PEPTIDE DESIGN
G. Scarabelli (2010)
10.1093/hmg/ddn265
The A3243G tRNALeu(UUR) MELAS mutation causes amino acid misincorporation and a combined respiratory chain assembly defect partially suppressed by overexpression of EFTu and EFG2.
F. Sasarman (2008)
10.5923/J.BIOINFORMATICS.20110101.02
On Predicting Conformational B-cell Epitopes: a Comparative Study and a New Model
Khaled A. Hassan (2012)
10.14288/1.0067000
Purification and mass spectrometric characterization of human CXCR4
Julie P Wong (2008)
10.1016/J.VACCINE.2007.07.066
Selection of mimotopes of Bovine Viral Diarrhoea Virus using a solid-phase peptide library.
A. T. Kalaycıoğlu (2007)
10.1089/VIM.2007.0029
Multiple antigenic peptides as vaccine platform for the induction of humoral responses against dengue-2 virus.
G. Amexis (2007)
10.1016/j.virusres.2019.197824
Molecular evolution of the hemagglutinin-neuraminidase (HN) gene in human respirovirus 3.
Jumpei Aso (2019)
10.1007/978-3-030-32459-9
HIV/AIDS: Immunochemistry, Reductionism and Vaccine Design: A Review of 20 Years of Research
Marc H V van Regenmortel (2019)
10.1002/prot.24527
Cation-π, amino-π, π-π, and H-bond interactions stabilize antigen-antibody interfaces.
Georgios A. Dalkas (2014)
10.1016/J.CCA.2006.07.013
Molecular dissection of an hCG-beta epitope using single-step solid phase radioimmunoassay.
P. V. Prasad (2007)
10.1016/B978-012374410-4.00583-5
Antigenicity and Immunogenicity of Viral Proteins
M. Regenmortel (2008)
10.1007/s10354-007-0496-5
Von der Allergenerkennung durch Antikörper zu neuen therapeutischen Konzepten
B. Hantusch (2007)
10.1016/j.molimm.2012.04.002
IgE epitopes of intact and digested Ara h 1: a comparative study in humans and rats.
K. L. Bøgh (2012)
10.1007/s10142-012-0302-3
The epitopes in wheat proteins for defining toxic units relevant to human health
Angéla Juhász (2012)
10.1016/j.bios.2014.09.090
Kinetic epitope mapping of monoclonal antibodies raised against the Yersinia pestis virulence factor LcrV.
Thomas E. Read (2015)
10.1016/j.jprot.2019.103572
Intact Transition Epitope Mapping - Thermodynamic Weak-force Order (ITEM - TWO).
Bright D Danquah (2019)
10.1159/000323887
Cloning, Expression and Patient IgE Reactivity of Recombinant Pru du 6, an 11S Globulin from Almond
L. N. Willison (2011)
10.1016/J.CLIM.2006.06.007
Model of stimulation-responsive splicing and strategies in identification of immunogenic isoforms of tumor antigens and autoantigens.
F. Yang (2006)
DISEASE MODELS IgE – the main player of food allergy
H. Broekman (2016)
10.1097/00130832-200404000-00005
Natural rubber latex allergens: new developments
H. Yeang (2004)
10.1109/TCBB.2011.49
Antibody-Specified B-Cell Epitope Prediction in Line with the Principle of Context-Awareness
Liang Zhao (2011)
THE HARMONIZER Science, Philosophy, Religion, and Art
Sri Chaitanya (2014)
antibodies Using structural analysis to generate parasite-selective monoclonal data
Michael A. Kron ()
See more
Semantic Scholar Logo Some data provided by SemanticScholar