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Significant differences in physicochemical properties of human immunoglobulin kappa and lambda CDR3 regions

Townsend, CL, Laffy, JMJ, Wu, Y-C, O’Hare, JS, Martin, V, Kipling, D, Fraternali, F and Dunn-Walters, Deborah (2016) Significant differences in physicochemical properties of human immunoglobulin kappa and lambda CDR3 regions Frontiers in Immunology, 216.

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Abstract

Antibody variable regions are composed of a heavy and a light chain and in humans there are two light chain isotypes: kappa and lambda. Despite their importance in receptor editing, the light chain is often overlooked in the antibody literature, with the focus being on the heavy chain CDR-H3 region. In this paper, we set out to investigate the physicochemical and structural differences between human kappa and lambda light chain CDR regions. We constructed a dataset containing over 29,000 - light chain variable region sequences from IgM-transcribing, newly formed B cells isolated from human bone marrow and peripheral blood. We also used a published human naïve dataset to investigate the CDR-H3 properties of heavy chains paired with kappa and lambda light chains, and probed the Protein Data Bank (PDB) to investigate the structural differences between kappa and lambda antibody CDR regions. We found that kappa and lambda light chains have very different CDR physicochemical and structural properties, whereas the heavy chains with which they are paired do not differ significantly. We also observed that the mean CDR3 N nucleotide addition in the kappa, lambda and heavy chain gene rearrangements are correlated within donors, but can differ between donors. This indicates that TdT may work with differing efficiencies between different people, but the same efficiency in the different classes of immunoglobulin chain within one person. We have observed large differences in the physicochemical and structural properties of kappa and lambda light chain CDR regions. This may reflect different roles in the humoral immune response.

Item Type: Article
Subjects : Biosciences and Medicine
Divisions : Faculty of Health and Medical Sciences > School of Biosciences and Medicine
Authors :
NameEmailORCID
Townsend, CLUNSPECIFIEDUNSPECIFIED
Laffy, JMJUNSPECIFIEDUNSPECIFIED
Wu, Y-CUNSPECIFIEDUNSPECIFIED
O’Hare, JSUNSPECIFIEDUNSPECIFIED
Martin, VUNSPECIFIEDUNSPECIFIED
Kipling, DUNSPECIFIEDUNSPECIFIED
Fraternali, FUNSPECIFIEDUNSPECIFIED
Dunn-Walters, Deborahd.dunn-walters@surrey.ac.ukUNSPECIFIED
Date : 27 September 2016
Identification Number : 10.3389/fimmu.2016.00388
Copyright Disclaimer : Copyright © 2016 Townsend, Laffy, Wu, Silva O’Hare, Martin, Kipling, Fraternali and Dunn-Walters. This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) or licensor are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.
Uncontrolled Keywords : antibody, Light chains, Kappa, LAMBDA, CDR3, TDT, N nucleotide addition, immunoglobulin
Related URLs :
Depositing User : Symplectic Elements
Date Deposited : 16 Sep 2016 13:19
Last Modified : 31 Oct 2017 18:43
URI: http://epubs.surrey.ac.uk/id/eprint/812201

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