Structural relationship between the two IgY of the duck, Anas platyrhynchos: molecular genetic evidence

Autor: Katharine Magor, Warr, G. W., Middleton, D., Wilson, M. R., Higgins, D. A.
Rok vydání: 1992
Předmět:
Zdroj: Scopus-Elsevier
ISSN: 1550-6606
0022-1767
DOI: 10.4049/jimmunol.149.8.2627
Popis: cDNA clones encoding the H chains of the 7.8S and 5.7S IgY of the White Pekin duck have been isolated and sequenced. The H chain of the 7.8S IgY possesses four C region domains and thus resembles the H chain of chicken IgY with which it shows, in the C region, 54% inferred amino acid sequence identity, and complete conservation of the C region cysteine and tryptophan residues. The H chain of the 5.7S IgY possesses only two C region domains, that are virtually identical to CH1 and CH2 of the 7.8S IgY H chain. Although Southern blot genomic analysis did not resolve whether the two transcripts encoding the H chains of the 7.8S and 5.7S IgY are derived from one or two H chain-encoding genes, the CH 1, 2, 3, and 4 exons are apparently colinear, and no evidence was found for a separate locus in which CH1 and 2 exons were present and CH3 and 4 exons were lacking. The VH domain-encoding sequences of the cDNA for the two IgY H chains showed high similarity in the inferred VH gene (93% nucleotide and 91% inferred amino acid identity) and in the inferred JH segment (89% nucleotide and 93% inferred amino acid identity) but low similarity in the D region (26% nucleotide and 7% inferred amino acid identity). Genomic Southern blot hybridization analysis showed multiple VH-hybridizing sequences represented on up to 20 restriction fragments.
Databáze: OpenAIRE
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