Get 20M+ Full-Text Papers For Less Than $1.50/day. Start a 14-Day Trial for You or Your Team.

Learn More →

Crystal structure of an anti‐idiotype variable lymphocyte receptor

Crystal structure of an anti‐idiotype variable lymphocyte receptor Variable lymphocyte receptors (VLRs), the leucine‐rich repeat (LRR)‐based antigen receptors of jawless fish, have great utility in a wide variety of biochemical and biological applications, similar to classical Ig‐based antibodies. VLR‐based reagents may be particularly useful when traditional antibodies are not available. An anti‐idiotype lamprey VLR, VLR39, has previously been identified that recognizes the heavy‐chain CDR3 of the B‐cell receptor (BCR) of a leukemic clone from a patient with chronic lymphocytic leukemia (CLL). VLR39 was used successfully to track the re‐emergence of this clone in the patient following chemotherapy. Here, the crystal structure of VLR39 is presented at 1.5 Å resolution and compared with those of other protein‐specific VLRs. VLR39 adopts a curved solenoid fold and exhibits substantial structural similarity to other protein‐binding VLRs. VLR39 has a short LRRCT loop that protrudes outwards away from the concave face and is similar to those of its protein‐specific VLR counterparts. Analysis of the VLR39–BCR interaction by size‐exclusion chromatography and biolayer interferometry using the scFv version of the BCR confirms that VLR39 recognizes the BCR Fv region. Such VLR‐based reagents may be useful for identifying and monitoring leukemia in CLL patients and in other clinical diagnostic assays. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Acta Crystallographica Section F Wiley

Loading next page...
 
/lp/wiley/crystal-structure-of-an-anti-idiotype-variable-lymphocyte-receptor-wVeuTuIqvm
Publisher
Wiley
Copyright
Copyright © 2017 Wiley Subscription Services
ISSN
2053-230X
eISSN
2053-230X
DOI
10.1107/S2053230X1701620X
pmid
29199989
Publisher site
See Article on Publisher Site

Abstract

Variable lymphocyte receptors (VLRs), the leucine‐rich repeat (LRR)‐based antigen receptors of jawless fish, have great utility in a wide variety of biochemical and biological applications, similar to classical Ig‐based antibodies. VLR‐based reagents may be particularly useful when traditional antibodies are not available. An anti‐idiotype lamprey VLR, VLR39, has previously been identified that recognizes the heavy‐chain CDR3 of the B‐cell receptor (BCR) of a leukemic clone from a patient with chronic lymphocytic leukemia (CLL). VLR39 was used successfully to track the re‐emergence of this clone in the patient following chemotherapy. Here, the crystal structure of VLR39 is presented at 1.5 Å resolution and compared with those of other protein‐specific VLRs. VLR39 adopts a curved solenoid fold and exhibits substantial structural similarity to other protein‐binding VLRs. VLR39 has a short LRRCT loop that protrudes outwards away from the concave face and is similar to those of its protein‐specific VLR counterparts. Analysis of the VLR39–BCR interaction by size‐exclusion chromatography and biolayer interferometry using the scFv version of the BCR confirms that VLR39 recognizes the BCR Fv region. Such VLR‐based reagents may be useful for identifying and monitoring leukemia in CLL patients and in other clinical diagnostic assays.

Journal

Acta Crystallographica Section FWiley

Published: Jan 1, 2017

Keywords: ; ; ; ; ; ; ;

There are no references for this article.