scholarly journals In-depth determination and analysis of the human paired heavy- and light-chain antibody repertoire

2014 ◽  
Vol 21 (1) ◽  
pp. 86-91 ◽  
Author(s):  
Brandon J DeKosky ◽  
Takaaki Kojima ◽  
Alexa Rodin ◽  
Wissam Charab ◽  
Gregory C Ippolito ◽  
...  
Keyword(s):  
Light Chain ◽  
Antibody Repertoire ◽  
Depth Determination ◽  
Light Chain Antibody

scholarly journals Simple paired heavy- and light-chain antibody repertoire sequencing using endoplasmic reticulum microsomes

2018 ◽  
Vol 10 (1) ◽  
Author(s):  
Praneeth Reddy Devulapally ◽  
Jörg Bürger ◽  
Thorsten Mielke ◽  
Zoltán Konthur ◽  
Hans Lehrach ◽  
...  
Keyword(s):  
Endoplasmic Reticulum ◽  
Light Chain ◽  
Antibody Repertoire ◽  
Repertoire Sequencing ◽  
Light Chain Antibody

scholarly journals The Structural Basis of Repertoire Shift in an Immune Response to Phosphocholine

2000 ◽  
Vol 191 (12) ◽  
pp. 2101-2112 ◽  
Author(s):  
McKay Brown ◽  
Maria A. Schumacher ◽  
Gregory D. Wiens ◽  
Richard G. Brennan ◽  
Marvin B. Rittenberg
Keyword(s):  
Immune Response ◽  
Light Chain ◽  
Indirect Effects ◽  
Somatic Mutations ◽  
Variable Region ◽  
Primary Response ◽  
Structural Basis ◽  
Antibody Repertoire ◽  
High Affinity

The immune response to phosphocholine (PC)–protein is characterized by a shift in antibody repertoire as the response progresses. This change in expressed gene combinations is accompanied by a shift in fine specificity toward the carrier, resulting in high affinity to PC–protein. The somatically mutated memory hybridoma, M3C65, possesses high affinity for PC–protein and the phenyl-hapten analogue, p-nitrophenyl phosphocholine (NPPC). Affinity measurements using related PC–phenyl analogues, including peptides of varying lengths, demonstrate that carrier determinants contribute to binding affinity and that somatic mutations alter this recognition. The crystal structure of an M3C65–NPPC complex at 2.35-Å resolution allows evaluation of the three light chain mutations that confer high-affinity binding to NPPC. Only one of the mutations involves a contact residue, whereas the other two have indirect effects on the shape of the combining site. Comparison of the M3C65 structure to that of T15, an antibody dominating the primary response, provides clear structural evidence for the role of carrier determinants in promoting repertoire shift. These two antibodies express unrelated variable region heavy and light chain genes and represent a classic example of the effect of repertoire shift on maturation of the immune response.

scholarly journals Antibody Repertoire Development in Fetal and Neonatal Pigs. VII. Characterization of the Preimmune κ Light Chain Repertoire

2004 ◽  
Vol 173 (11) ◽  
pp. 6794-6805 ◽  
Author(s):  
John E. Butler ◽  
Nancy Wertz ◽  
Jishan Sun ◽  
Huang Wang ◽  
Patrick Chardon ◽  
...  
Keyword(s):  
Light Chain ◽  
Antibody Repertoire ◽  
Neonatal Pigs ◽  
Repertoire Development
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