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Ig light chain variability in DNP494-KLH immunised sea bass (Dicentrarchus labrax L.): Evidence for intramolecular-induced suppression.

  • N. M. S. Dos Santos
  • , T. T. Hermsen
  • , J. H. W. Rombout
  • , L. Pilstroem
  • , Rene Josephus Maria Stet

Research output: Contribution to journalArticlepeer-review

Abstract

The coding sequence of the sea bass light chain was obtained by sequential anchored PCR on a head kidney cDNA library of a DNP494-KLH immunised sea bass. The cDNA sequence obtained codes for a leader peptide of 21 aa and a mature IgL chain of 223 aa. Both the amino acid sequence comparisons and neighbour-joining trees showed that the IgL chain of sea bass obtained is of the L1/G type. To study the variability of the light chain, additional PCRs on the cDNA library and cDNA from pooled head kidneys were performed. Multiple alignment of unique sequences (N = 17) could be performed without introducing gaps, and showed extremely low variability in CDR1, and no variability in CDR2 or CDR3. A possible explanation for this tow variability of the IgL1 chain might be the enhanced expression of monospecific anti-DNP antibodies. The isolation and characterisation of partial genomic and cDNA IgL sequences, which showed normal variability, corroborate this explanation. (C) 2001 Elsevier Science Ltd. All rights reserved.

Original languageEnglish
Pages (from-to)387-401
Number of pages14
JournalDevelopmental and Comparative Immunology
Volume25
DOIs
Publication statusPublished - 2001

Keywords

  • Dicentrarchus labrax
  • immunoglobulin light chain
  • expression
  • variability
  • DNP494-KLH
  • TROUT ONCORHYNCHUS-MYKISS
  • CYPRINUS-CARPIO L.
  • SALMO-SALAR L
  • RAINBOW-TROUT
  • GENOMIC ORGANIZATION
  • ANTIBODY-RESPONSES
  • CHANNEL CATFISH
  • IMMUNOGLOBULIN
  • FISH
  • GENES

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