Related Experiment Video
Updated: Aug 10, 2026

Immunoglobulin Gene Sequence Analysis In Chronic Lymphocytic Leukemia: From Patient Material To Sequence Interpretation
Published on: November 26, 2018
Usage of T cell receptor variable segments of the beta-chain in IgA nephropathy
Kaori Muro1, Kunihiro Yamagata, Masaki Kobayashi
1Institute of Clinical Medicine, University of Tsukuba, Ibaraki, Japan.
Background:
We previously reported that glomerulonephritis associated with Staphylococcus aureus infection (SAGN) showed an increased usage of T cell receptor Vbeta 5.3 and 8 in peripheral lymphocytes and mesangial IgA and IgG depositions. To elucidate the immunological mechanisms and pathogenesis of IgA nephropathy, we analyzed the usage of TCR Vbeta in both peripheral blood lymphocytes (PBLs) and renal infiltrating T cells from IgA-N patients.
Methods:
In 38 patients with IgA nephropathy and controls, the usage of TCR Vbeta in PBLs were analyzed using monoclonal antibodies against Vbeta 3.1, Vbeta 5.1, Vbeta 5.2 + 5.3, Vbeta 5.3, Vbeta 6.7, Vbeta 8, Vbeta 12.1, and Vbeta 13.1 + 13.3 with three-color flow cytometry. Furthermore, we examined immunohistochemically renal biopsy specimens using antibodies against Vbeta 5.3 and Vbeta 8.
Results:
The percentages of DR+CD4+CD8- cells, CD45RO+CD4+ cells, and CD45RO+CD4+DR+ cells in PBLs from IgA nephropathy were significantly higher than controls. The percentages of TCR Vbeta 5.3 positive cells and TCR Vbeta 8 positive cells in PBLs from patients were 1.3 +/- 0.1 and 3.1 +/- 0.2%, and both were significantly higher than controls. The percentage of renal interstitial TCR Vbeta 5.3 expression was significantly higher than that in PBLs. However, there was no significant difference between the TCR Vbeta 8 expression in the interstitium and that in PBLs.
Conclusions:
TCR Vbeta 5.3 and 8 usage and broad CD4+ T cell activation have occurred in IgA nephropathy. These changes were similar but weak compared with formerly reported SAGN.
Related Concept Videos
Antibody Structure
Antibodies, also known as immunoglobulins (Ig), are essential players of the adaptive immune system. These antigen-binding proteins are produced by B cells and make up 20 percent of the total blood plasma by weight. In mammals, antibodies fall into five different classes, which each elicits a different biological response upon antigen binding.
The Y-Shaped Structure of Antibodies Consists of Four Polypeptide Chains
Antibodies consist of four polypeptide chains: two identical heavy...
Immunoglobulin-like Cell Adhesion Molecules
Ig-CAMs exhibit either homophilic binding (to other Ig-CAMs) or heterophilic binding (to other ligands such as integrins). While most Ig-CAMs...
Diversity of Antigen Receptors
Before encountering any antigen, lymphocytes express these receptors. On B cells, the antigen receptor is a membrane-bound antibody molecule called BCR; on T cells, it is a T cell receptor or TCR. B and T cell receptors are composed of two...
T Cell Activation and Clonal Selection
Naive T cells that have not yet encountered an antigen express two primary CD...
Antibody Structure and Classes
The basic structure of an antibody consists of four protein chains: two identical heavy chains and two identical light chains. These chains are held together by disulfide bonds and other non-covalent interactions, forming a Y-shaped structure.

