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Cross-reactivity

Cross-reactivity

T Cell Activation and Clonal Selection

T Cell Activation and Clonal Selection

T cells are integral to our adaptive immune system, recognizing and effectively responding to foreign antigens. T cell activation and clonal selection are pivotal in orchestrating this immune response. This article elucidates these mechanisms, detailing the roles of cluster of differentiation (CD) markers, major histocompatibility complex (MHC) molecules, costimulatory signals, and the process of clonal selection.
Naive T cells that have not yet encountered an antigen express two primary CD...

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Related Experiment Video

Updated: Apr 7, 2026

Measurement of T Cell Alloreactivity Using Imaging Flow Cytometry

Measurement of T Cell Alloreactivity Using Imaging Flow Cytometry

Published on: April 19, 2017

Improved structural method for T-cell cross-reactivity prediction.

Marcus F A Mendes¹, Dinler A Antunes², Maurício M Rigo¹

¹NBLI - Núcleo de Bioinformática do Laboratório de Imunogenética, Departamento de Genética, Universidade Federal do Rio Grande do Sul, Av. Bento Gonçalves 9500, Building 43323, room 225, Brazil; Programa de Pós-Graduação em Genética e Biologia Molecular (PPGBM), Universidade Federal do Rio Grande do Sul (UFRGS), Rio Grande do Sul, Porto Alegre, Brazil.

Molecular Immunology

|July 5, 2015

Summary

This summary is machine-generated.

Cytotoxic T-lymphocytes (CTLs) recognize viral epitopes via peptide-loaded major histocompatibility complexes class I (pMHC-I). This study predicts CTL cross-reactivity using pMHC-I structural features, aiding vaccine design for targeted immunity or avoiding adverse responses.

Keywords:

ASA Cross-reactivity HCA Pvclust Vaccine development pMHC-I

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Single-cell Screening Method for the Selection and Recovery of Antibodies with Desired Specificities from Enriched Human Memory B Cell Populations

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Single-cell Screening Method for the Selection and Recovery of Antibodies with Desired Specificities from Enriched Human Memory B Cell Populations

Single-cell Screening Method for the Selection and Recovery of Antibodies with Desired Specificities from Enriched Human Memory B Cell Populations

Published on: August 22, 2019

Area of Science:

Immunology
Structural Biology
Computational Biology

Background:

Cytotoxic T-lymphocytes (CTLs) are crucial for adaptive immunity, identifying infected cells via peptide-loaded major histocompatibility complexes class I (pMHC-I).
CTLs exhibit cross-reactivity, recognizing multiple pMHC-I complexes, a phenomenon with implications for vaccine development and immune response prediction.
Understanding the structural basis of pMHC-I cross-reactivity is essential for designing effective vaccines and predicting immune responses.

Purpose of the Study:

To develop a standardized, structure-based method for predicting cross-reactivity among viral epitopes.
To utilize multivariate statistical methods and pMHC-I structural features for accurate cross-reactivity predictions.
To apply the developed approach to hepatitis C virus (HCV) and dengue virus epitopes.

Main Methods:

Employing multivariate statistical methods with pMHC-I structural features (charges, accessible surface area) as input.
Utilizing an R package (pvclust) for hierarchical cluster analysis and uncertainty assessment.
Validating predictions using multiscale bootstrap resampling and existing in vitro experimental data.

Main Results:

Successfully identified cross-reactive targets among 28 naturally occurring HCV variants.
Accurately predicted cross-reactivity among eight epitopes from four dengue virus serotypes.
Demonstrated that combined charge and accessible surface area data effectively assess structural features driving cross-reactive responses.

Conclusions:

The developed structure-based prediction method accurately identifies cross-reactive viral epitopes.
This approach provides statistical support for interpreting cross-reactivity, enhancing vaccine design strategies.
The methods can guide the selection of vaccine candidates for broad immunity or identify potentially undesirable epitope targets.