Analysis of antibody binding specificities in twin and SNP-genotyped cohorts reveals that antiviral antibody epitope selection is a heritable trait

Immunity ◽  
2022 ◽  
Vol 55 (1) ◽  
pp. 174-184.e5 ◽  
Author(s):  
Thiagarajan Venkataraman ◽  
Cristian Valencia ◽  
Massimo Mangino ◽  
William Morgenlander ◽  
Steven J. Clipman ◽  
...  
Keyword(s):  
Antibody Binding ◽  
Antibody Epitope ◽  
Heritable Trait ◽  
Antiviral Antibody ◽  
Epitope Selection

Detection of Virus-Induced Membrane and Cytoplasmic Antigens: Comparison of the 125I-LabeIed Antiviral Antibody Binding Technique with Immunofluorescence

Intervirology ◽  
1973 ◽  
Vol 2 (1) ◽  
pp. 48-51 ◽  
Author(s):  
Kozaburo Hayashi ◽  
Akira Niwa ◽  
Joel Rosenthal ◽  
Abner Louis Notkins
Keyword(s):  
Antibody Binding ◽  
Induced Membrane ◽  
Antiviral Antibody

scholarly journals Antiviral Antibody Epitope Selection is a Heritable Trait

2021 ◽  
Author(s):  
Thiagarajan Venkataraman ◽  
Cristian Valencia ◽  
Massimo Mangino ◽  
William Morgenlander ◽  
Steven J. Clipman ◽  
...  
Keyword(s):  
Viral Load ◽  
Mhc Class Ii ◽  
Viral Infections ◽  
White Blood Cells ◽  
Selection Response ◽  
Barr Virus ◽  
Viral Epitope ◽  
Antibody Epitope ◽  
Epstein Barr ◽  
Epitope Selection

AbstractThere is enormous variability in human immune responses to viral infections. However, the genetic factors that underlie this variability are not well characterized. We used VirScan, a high-throughput viral epitope scanning technology, to analyze the antibody binding specificities of twins and SNP-genotyped individuals. These data were used to estimate the heritability and identify genomic loci associated with antibody epitope selection, response breadth, and the control of Epstein-Barr Virus (EBV) viral load. We identified 4 epitopes of EBV that were heritably targeted, and at least two EBNA-2 binding specificities that were associated with variants in the MHC class-II locus. We identified an EBV serosignature that predicted viral load in white blood cells and was associated with genetic variants in the MHC class-I locus. Our study provides a new framework for identifying genes important for pathogen immunity, with specific implications for the genetic architecture of EBV humoral responses and the control of viral load.Abstract Figure

Structural organization of escherichia coli ribosomes as determined by immuno electron microscopy

1978 ◽  
Vol 36 (2) ◽  
pp. 166-167 ◽  
Author(s):  
G. Stöffler ◽  
R.W. Bald ◽  
J. Dieckhoff ◽  
H. Eckhard ◽  
R. Lührmann ◽  
...  
Keyword(s):  
Electron Microscopy ◽  
Escherichia Coli ◽  
Ribosomal Proteins ◽  
Structural Organization ◽  
Three Dimensional ◽  
Ribosomal Subunit ◽  
Spatial Arrangement ◽  
Small Subunit ◽  
Antibody Binding ◽  
Immuno Electron Microscopy

A central step towards an understanding of the structure and function of the Escherichia coli ribosome, a large multicomponent assembly, is the elucidation of the spatial arrangement of its 54 proteins and its three rRNA molecules. The structural organization of ribosomal components has been investigated by a number of experimental approaches. Specific antibodies directed against each of the 54 ribosomal proteins of Escherichia coli have been performed to examine antibody-subunit complexes by electron microscopy. The position of the bound antibody, specific for a particular protein, can be determined; it indicates the location of the corresponding protein on the ribosomal surface.The three-dimensional distribution of each of the 21 small subunit proteins on the ribosomal surface has been determined by immuno electron microscopy: the 21 proteins have been found exposed with altogether 43 antibody binding sites. Each one of 12 proteins showed antibody binding at remote positions on the subunit surface, indicating highly extended conformations of the proteins concerned within the 30S ribosomal subunit; the remaining proteins are, however, not necessarily globular in shape (Fig. 1).

Solid-phase immunoelectron microscopy for rapid diagnosis of enteroviruses

1984 ◽  
Vol 42 ◽  
pp. 226-227 ◽  
Author(s):  
K. Pegg-Feige ◽  
F. W. Doane
Keyword(s):  
Electron Microscopy ◽  
Cell Culture ◽  
Immunoelectron Microscopy ◽  
Detection Method ◽  
Solid Phase ◽  
Protein A ◽  
Plant Viruses ◽  
Rapid Diagnosis ◽  
Virus Diagnosis ◽  
Antiviral Antibody

Immunoelectron microscopy (IEM) applied to rapid virus diagnosis offers a more sensitive detection method than direct electron microscopy (DEM), and can also be used to serotype viruses. One of several IEM techniques is that introduced by Derrick in 1972, in which antiviral antibody is attached to the support film of an EM specimen grid. Originally developed for plant viruses, it has recently been applied to several animal viruses, especially rotaviruses. We have investigated the use of this solid phase IEM technique (SPIEM) in detecting and identifying enteroviruses (in the form of crude cell culture isolates), and have compared it with a modified “SPIEM-SPA” method in which grids are coated with protein A from Staphylococcus aureus prior to exposure to antiserum.

IgE and monoclonal antibody binding by the mite allergen Der p 7

1996 ◽  
Vol 26 (3) ◽  
pp. 308-315 ◽  
Author(s):  
H.-D. SHEN ◽  
K. Y. CHUA ◽  
W. L. LIN ◽  
H. L. CHEN ◽  
K.-H. HSIEH ◽  
...  
Keyword(s):  
Monoclonal Antibody ◽  
Mite Allergen ◽  
Antibody Binding ◽  
Monoclonal Antibody Binding

Mapping Neutralizing Antibody Epitope Specificities to an HIV Env Trimer in Immunized and in Infected Rhesus Macaques

2020 ◽  
Author(s):  
Fangzhu Zhao ◽  
Collin Joyce ◽  
Alison Burns ◽  
Bartek Nogal ◽  
Alejandra Ramos ◽  
...  
Keyword(s):  
Rhesus Macaques ◽  
Neutralizing Antibody ◽  
Antibody Epitope
Sign in / Sign up

Export Citation Format

Share Document