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Immunoglobulins of the non-galliform birds: Antibody expression and repertoire in the duck

Posted by on in 2006
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 Mats L. Lundqvist (a) Darlene L. Middleton (a) Cynthia Radford (b) Gregory W. Warr (a) and Katharine E. Magor (b)*

Dev Comp Immunol. Author manuscript; available in PMC 2006 July 1.
Published in final edited form as: Dev Comp Immunol. 2006; 30(1-2): 93-100. doi: 10.1016/j.dci.2005.06.019.
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Abstract

Galliform and non-galliform birds express three immunoglobulin isotypes, IgM, IgA and IgY. Beyond this we should not generalize because differences in gene organization may have functional consequences reflected in the immune response.

At present, studies on non-galliform birds are largely restricted to ducks. Ducks express an alternatively spliced form of their IgY heavy chain (?) gene, the IgY(Fc), that lacks the Fc region and Fc-associated secondary effector functions.

It is not known how common the expression of the IgY(Fc) is among birds, nor the functional consequences. It is also not known whether the unusual organization of the duck IgH locus, also shared with the chicken, having the gene order of µ, a and ?, with a inverted in the locus, is unique to the galloanseriform lineage.

Ducks, like chickens, have a single immunoglobulin light chain of the lambda (?) type. Evidence suggests that ducks, like chickens, generate their immunoglobulin repertoire through a single functional rearrangement of the variable (V) region, and generate diversity through gene conversion from a pool of pseudogenes. In Southern blots of germline and rearranged bursal DNA, both the heavy and light chain loci of ducks appear to each undergo one major rearrangement event. For both heavy and light chains, the functional V region element and the pseudogenes appear to consist of a single gene family.

Further analysis of 26 heavy chain joining (JH) and 27 light chain JL segments shows there is use of a single J segment in ducks, which is diversified presumably through somatic mutations and gene conversion events.

Despite this limitation on the rearrangement of immunoglobulin genes, analysis of 26 DH and 122 VL sequences suggests that extensive sequence diversity is generated.

(a) Marine Biomedicine and Environmental Sciences Center and Department of Biochemistry, Medical University of South Carolina, Charleston, SC, USA
(b) Department of Biological Sciences, University of Alberta, CW405 Biological Sciences Building, Edmonton, Alta., Canada T6G 2E9

* Corresponding author.
Tel.: +1 780 492 5498; fax: +1 780 492 9234.
E-mail address:kmagor@ualberta.ca (K.E. Magor).
The publisher's final edited version of this article is available at Dev Comp Immunol.

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