Immunoglobulin V(H) gene structure and diversity in Heterodontus, a phylogenetically primitive shark Journal Article

   


Authors: Litman, G. W.; Berger, L.; Murphy, K.; Litman, R.; Hinds, K.; Erickson, B. W.
Article Title: Immunoglobulin V(H) gene structure and diversity in Heterodontus, a phylogenetically primitive shark
Abstract: A mouse V(H) probe has been used to identify and isolate V(H) homologs in a DNA library of Heterodontus francisci (horned shark). The complete nucleotide sequence of one V(H) gene, HXIA, has been determined and found to exhibit striking organizational homology and nucleotide identity with mammalian prototype V(H) genes. Metric analysis of the complete sequence is consistent with the early phylogenetic diversification of framework and complementarity-determining regions (CDR). Both the predicted amino acid sequence and the specific hybridization of the CDR-2-specific, synthetic oligodeoxynucleotide probe in spleen mRNA suggest that HXIA is functionally expressed. A probe consisting of the entire coding region of this gene hybridizes with multiple components in Southern blot analysis of Heterodontus genomic DNA and together with the identification of additional unique V+(H)-λ clones indicates that considerable complexity is associated with the germline V(H) gene family in a contemporary species that represents an early stage in the phylogenetic development of the vertebrates.
Keywords: genetics; nonhuman; animal cell; mouse; animal; mice; heredity; genetic variability; evolution; immunoglobulin heavy chain; genetic recombination; immunoglobulin gene; immunoglobulin variable region; amino acid sequence; genetic engineering; recombination, genetic; nucleotide sequence; base sequence; antibody specificity; radioisotope; fish; gene structure; hybridization; variation (genetics); antibody diversity; shark; priority journal; article; gene pool; support, u.s. gov't, p.h.s.; hybridization, genetic; immunoglobulins, heavy-chain; immunoglobulins, heavy chain; sharks
Journal Title: Proceedings of the National Academy of Sciences of the United States of America
Volume: 82
Issue: 7
ISSN: 0027-8424
Publisher: National Academy of Sciences  
Date Published: 1985-04-01
Start Page: 2082
End Page: 2086
Language: English
DOI: 10.1073/pnas.82.7.2082
PROVIDER: scopus
PMCID: PMC397496
PUBMED: 3920659
DOI/URL:

https://www.scopus.com/inward/record.uri?eid=2-s2.0-0022050744&doi=10.1073%2fpnas.82.7.2082&partnerID=40&md5=32189998a24f25dba5457f488657cf06
Notes: Article -- Export Date: 26 October 2021 -- Source: Scopus
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