International Immunology, Vol 9, 1503-1515, Copyright © 1997 by Oxford University Press
FM Raaphorst, CS Raman, J Tami, M Fischbach and I Sanz
Ig repertoires generated at various developmental stages differ markedly in
diversity. It is well documented that Ig H chain genes in human fetal liver
are limited with regard to N-regional diversity and use of diversity
elements. It is unclear whether these characteristics persist in pre-B cell
H chain genes of adult bone marrow. Using Ig H chain CDR3 fingerprinting
and sequence analysis, we analyzed the diversity of Ig H chain third
complementarity determining regions (HCDR3) in adult bone marrow pre-B and
mature B lymphocytes. Pre-B cell HCDR3 sequences exhibited adult
characteristics with respect to HCDR3 size, distribution of N regions and
usage of diversity elements. This suggested that pre-B cells in adults are
distinct from fetal B cell precursors with regard to Ig H chain
diversification mechanisms. At the DNA sequence level, HCDR3 diversity in
mature B cells was similar to that in pre-B cells. Pre-B HCDR3s, however,
frequently contained a consecutive stretch of hydrophobic amino acids,
which were rare in mature B cells. We propose that highly hydrophobic pre-B
HCDR3s may be negatively selected on the basis of structural limitations
imposed by the antigen binding site. At the same time, usage of hydrophilic
HCDR3 sequences (thought to support HCDR3 loop formation) may be promoted
by positive selection.
ARTICLES
Human Ig heavy chain CDR3 regions in adult bone marrow pre-B cells display an adult phenotype of diversity: evidence for structural selection of DH amino acid sequences
Department of Medicine, University of Texas Health Science Center, San Antonio 78284, USA.
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