Open AccessIdentification of a new European rabbit IgA with a serine-rich hinge region
Author(s) -
Ana Pinheiro,
Patrícia de Sousa-Pereira,
Tanja Strive,
Katherine L. Knight,
Jenny M. Woof,
Pedro J. Esteves,
Joana Abrantes
Publication year - 2018
Publication title -
plos one
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.99
H-Index - 332
ISSN - 1932-6203
DOI - 10.1371/journal.pone.0201567
Subject(s) - allotype , biology , serine , amino acid , peptide sequence , hinge , amino acid residue , sequence motif , genetics , antibody , gene , microbiology and biotechnology , mechanical engineering , phosphorylation , engineering
In mammals, the most striking IgA system belongs to Lagomorpha. Indeed, 14 IgA subclasses have been identified in European rabbits, 11 of which are expressed. In contrast, most other mammals have only one IgA, or in the case of hominoids, two IgA subclasses. Characteristic features of the mammalian IgA subclasses are the length and amino acid sequence of their hinge regions, which are often rich in Pro, Ser and Thr residues and may also carry Cys residues. Here, we describe a new IgA that was expressed in New Zealand White domestic rabbits of IGHV a1 allotype. This IgA has an extended hinge region containing an intriguing stretch of nine consecutive Ser residues and no Pro or Thr residues, a motif exclusive to this new rabbit IgA. Considering the amino acid properties, this hinge motif may present some advantage over the common IgA hinge by affording novel functional capabilities. We also sequenced for the first time the IgA14 CH2 and CH3 domains and showed that IgA14 and IgA3 are expressed.