Peptide Arrays for Highly Sensitive and Specific Antibody-Binding Fluorescence Assays

2002 ◽  
Vol 13 (4) ◽  
pp. 713-720 ◽  
Author(s):  
Oleg Melnyk ◽  
Xavier Duburcq ◽  
Christophe Olivier ◽  
Florence Urbès ◽  
Claude Auriault ◽  
...  
Keyword(s):  
Specific Antibody ◽  
Antibody Binding ◽  
Peptide Arrays ◽  
Highly Sensitive ◽  
Fluorescence Assays

Epitope scanning reveals gain and loss of strain specific antibody binding epitopes associated with the conversion of normal cellular prion to scrapie prion

2004 ◽  
Vol 90 (5) ◽  
pp. 1205-1217 ◽  
Author(s):  
Tao Pan ◽  
Ruliang Li ◽  
Shin-Cheng Kang ◽  
Boon-Seng Wong ◽  
Thomas Wisniewski ◽  
...  
Keyword(s):  
Specific Antibody ◽  
Antibody Binding ◽  
Gain And Loss

Technical report: xMAPr – High-dynamic-range (HDR) quantification of antigen-specific antibody binding

2020 ◽  
Vol 212 ◽  
pp. 103577 ◽  
Author(s):  
Tanja C. Meyer ◽  
Frank Schmidt ◽  
Jörn Steinke ◽  
Barbara M. Bröker ◽  
Uwe Völker ◽  
...  
Keyword(s):  
Specific Antibody ◽  
Dynamic Range ◽  
High Dynamic Range ◽  
Antibody Binding ◽  
Technical Report ◽  
High Dynamic

scholarly journals Differences in the Binding Affinity of an HIV-1 V2 Apex-Specific Antibody for the SIVsmm/macEnvelope Glycoprotein Uncouple Antibody-Dependent Cellular Cytotoxicity from Neutralization

mBio ◽  
2019 ◽  
Vol 10 (4) ◽  
Author(s):  
Benjamin von Bredow ◽  
Raiees Andrabi ◽  
Michael Grunst ◽  
Andres G. Grandea ◽  
Khoa Le ◽  
...  
Keyword(s):  
Binding Affinity ◽  
Specific Antibody ◽  
Neutralizing Antibody ◽  
Glycosylation Site ◽  
Antibody Binding ◽  
Cellular Cytotoxicity ◽  
Antibody Dependent Cellular Cytotoxicity ◽  
Broadly Neutralizing Antibody ◽  
Infected Cells ◽  
Hiv 1

ABSTRACTAs a consequence of their independent evolutionary origins in apes and Old World monkeys, human immunodeficiency virus type 1 (HIV-1) and simian immunodeficiency viruses of the SIVsmm/maclineage express phylogenetically and antigenically distinct envelope glycoproteins. Thus, HIV-1 Env-specific antibodies do not typically cross-react with the Env proteins of SIVsmm/macisolates. Here we show that PGT145, a broadly neutralizing antibody to a quaternary epitope at the V2 apex of HIV-1 Env, directs the lysis of SIVsmm/mac-infected cells by antibody-dependent cellular cytotoxicity (ADCC) but does not neutralize SIVsmm/macinfectivity. Amino acid substitutions in the V2 loop of SIVmac239 corresponding to the epitope for PGT145 in HIV-1 Env modulate sensitivity to this antibody. Whereas a substitution in a conserved N-linked glycosylation site (N171Q) eliminates sensitivity to ADCC, a lysine-to-serine substitution in this region (K180S) increases ADCC and renders the virus susceptible to neutralization. These differences in function correlate with an increase in the affinity of PGT145 binding to Env on the surface of virus-infected cells and to soluble Env trimers. To our knowledge, this represents the first instance of an HIV-1 Env-specific antibody that cross-reacts with SIVsmm/macEnv and illustrates how differences in antibody binding affinity for Env can differentiate sensitivity to ADCC from neutralization.IMPORTANCEHere we show that PGT145, a potent broadly neutralizing antibody to HIV-1, directs the lysis of SIV-infected cells by antibody-dependent cellular cytotoxicity but does not neutralize SIV infectivity. This represents the first instance of cross-reactivity of an HIV-1 Env-specific antibody with SIVsmm/macEnv and reveals that antibody binding affinity can differentiate sensitivity to ADCC from neutralization.

scholarly journals Novel Bead-Based Epitope Assay is a sensitive and reliable tool for profiling epitope-specific antibody repertoire in food allergy

2019 ◽  
Vol 9 (1) ◽  
Author(s):  
Maria Suprun ◽  
Robert Getts ◽  
Rohit Raghunathan ◽  
Galina Grishina ◽  
Marc Witmer ◽  
...  
Keyword(s):  
Food Allergy ◽  
Specific Antibody ◽  
Allergic Sensitization ◽  
Specific Ige ◽  
Antibody Binding ◽  
Peptide Microarrays ◽  
Short Period ◽  
Reading Order ◽  
Multiple Sample ◽  
The Relationship

AbstractIdentification of allergenic IgE epitopes is instrumental for the development of novel diagnostic and prognostic methods in food allergy. In this work, we present the quantification and validation of a Bead-Based Epitope Assay (BBEA) that through multiplexing of epitopes and multiple sample processing enables completion of large experiments in a short period of time, using minimal quantities of patients’ blood. Peptides that are uniquely coupled to beads are incubated with serum or plasma samples, and after a secondary fluorophore-labeled antibody is added, the level of fluorescence is quantified with a Luminex reader. The signal is then normalized and converted to epitope-specific antibody binding values. We show that the effect of technical artifacts, i.e. well position or reading order, is minimal; and batch effects - different individual microplate runs - can be easily estimated and eliminated from the data. Epitope-specific antibody binding quantified with BBEA is highly reliable, reproducible and has greater sensitivity of epitope detection compared to peptide microarrays. IgE directed at allergenic epitopes is a sensitive biomarker of food allergy and can be used to predict allergy severity and phenotypes; and quantification of the relationship between epitope-specific IgE and IgG4 can further improve our understanding of the immune mechanisms behind allergic sensitization.

A new paradigm in molecular recognition? specific antibody binding to membrane-inserted HIV-1 epitopes

2011 ◽  
Vol 24 (4) ◽  
pp. 642-646 ◽  
Author(s):  
José L. Nieva ◽  
Beatriz Apellaniz ◽  
Nerea Huarte ◽  
Maier Lorizate
Keyword(s):  
Molecular Recognition ◽  
Specific Antibody ◽  
Antibody Binding ◽  
New Paradigm ◽  
Hiv 1

A way to identify archaellins in Halobacterium salinarum archaella by FLAG-tagging

2013 ◽  
Vol 8 (9) ◽  
pp. 828-834 ◽  
Author(s):  
Sergei Beznosov ◽  
Michael Pyatibratov ◽  
Pavan Veluri ◽  
Sagar Mitra ◽  
Oleg Fedorov
Keyword(s):  
Electron Microscopy ◽  
Specific Antibody ◽  
Insertion Site ◽  
Antibody Binding ◽  
Halobacterium Salinarum ◽  
Transformed Cells ◽  
Filament Length ◽  
Flag Peptide ◽  
First Time ◽  
Filament Surface

AbstractIn the current study, haloarchaea Halobacterium salinarum cells were transformed individually with each of the modified archaellin genes (flaA1, flaA2 and flaB2) containing an oligonucleotide insert encoding the FLAG peptide (DYKDDDDK). The insertion site was selected to expose the FLAG peptide on the archaella filament surface. Three types of transformed cells synthesizing archaella, containing A1, A2, or B2 archaellin modified with FLAG peptide were obtained. Electron microscopy of archaella has demonstrated that in each case the FLAG peptide is available for the specific antibody binding. It was shown for the first time that the B2 archaellin, like archaellins A1 and A2, is found along the whole filament length.

scholarly journals Specific antibody binding to the APP672–699 region shifts APP processing from α- to β-cleavage

2014 ◽  
Vol 5 (8) ◽  
pp. e1374-e1374 ◽  
Author(s):  
S Li ◽  
J Deng ◽  
H Hou ◽  
J Tian ◽  
B Giunta ◽  
...  
Keyword(s):  
Specific Antibody ◽  
Antibody Binding ◽  
App Processing
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