Restricted Use of Cationic Germline VH Gene Segments in Human Rh(D) Red Cell Antibodies

Author:

Boucher Gérard1,Broly Hervé1,Lemieux Réal1

Affiliation:

1. From The Canadian Red Cross Society, Blood Services, Ste-Foy, Québec; and the Department of Microbiology, Faculty of Medicine, Laval University Ste-Foy, Québec, Canada; and Centre Régional de Tranfusion Sanguine, Lille, France.

Abstract

AbstractThe human red cell Rh(D) antigen elicits the production of high-affinity IgG antibodies, which can prevent blood transfusion and cause hemolytic disease of the newborn. It has been known for 20 years that Rh(D) antibodies are among the most positively charged human serum IgGs. Analysis by IEF of 9 human anti-Rh(D) monoclonal antibodies showed that their isoelectric points (pI) (8.3 to 8.6) were also significantly higher than the average pI of serum IgGs (7.0 to 8.5). Sequencing of the anti-Rh(D) H and L chains cDNAs showed a preferential use of VH1 , VH3, JH6, and Vκ1 gene segments. The high pIs in IEF were correlated with a higher number of cationic amino acid residues in the H chain V regions without clustering in the complementary determining region. Computer analysis indicated that the germline VH used in anti-Rh(D) was selected among the most cationic segments available in the human VH repertoire or expressed in normal B cells. These results indicate that the selection of cationic VH segments may be an important early step in the formation of clinically relevant anti-Rh(D) and other red cell antibodies, possibly to facilitate epitope binding in the negatively charged red cell membrane environment.

Publisher

American Society of Hematology

Subject

Cell Biology,Hematology,Immunology,Biochemistry

Reference66 articles.

1. Molecular genetic basis of the human Rhesus blood group system.;Mouro;Nat Genet,1993

2. Defining the Rh blood group antigens.;Cartron;Blood Rev,1994

3. Charge differences between human IgG isoantibodies associated with specificity.;Frame;Immunology,1969

Cited by 32 articles. 订阅此论文施引文献 订阅此论文施引文献,注册后可以免费订阅5篇论文的施引文献,订阅后可以查看论文全部施引文献

同舟云学术

1.学者识别学者识别

2.学术分析学术分析

3.人才评估人才评估

"同舟云学术"是以全球学者为主线,采集、加工和组织学术论文而形成的新型学术文献查询和分析系统,可以对全球学者进行文献检索和人才价值评估。用户可以通过关注某些学科领域的顶尖人物而持续追踪该领域的学科进展和研究前沿。经过近期的数据扩容,当前同舟云学术共收录了国内外主流学术期刊6万余种,收集的期刊论文及会议论文总量共计约1.5亿篇,并以每天添加12000余篇中外论文的速度递增。我们也可以为用户提供个性化、定制化的学者数据。欢迎来电咨询!咨询电话:010-8811{复制后删除}0370

www.globalauthorid.com

TOP

Copyright © 2019-2024 北京同舟云网络信息技术有限公司
京公网安备11010802033243号  京ICP备18003416号-3