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COMMON ORIGIN AND EVOLUTION OF VARIABLE AND CONSTANT REGIONS OF IMMUNOGLOBULINS
Author(s) -
Wuilmart C.,
Urbain J.
Publication year - 1976
Publication title -
international journal of immunogenetics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.41
H-Index - 47
eISSN - 1744-313X
pISSN - 1744-3121
DOI - 10.1111/j.1744-313x.1976.tb00551.x
Subject(s) - homology (biology) , phylogenetic tree , gene , genetics , biology , glycophorin , evolutionary biology , computational biology , membrane
SUMMARY Sequence data show that the immunoglobulins evolved from two sets of paralogous genes: a gene set coding for the V regions and another for the different C regions. A comparison of sequences from these two gene sets shows homology between the V and C sets of genes: this homology is only significant when V H is compared with Cμ1, Cμ2 and Cγ1. There is a close agreement between our data drawn from sequence comparisons and the data of Poljak et al. (1974) drawn from crystallographic data. This finding is in agreement with the results of the phylogenetic trees of the C and V gene sets: they suggest that the V H subgroups and the first constant domain of the heavy chains are the most ancient. Moreover homology between the red blood cell glycophorin and Cμ2 suggests that immunoglobulins could have a common origin with some membrane proteins.