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Snakes antibodies.

Posted by on in 2012
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Gambón-Deza FSánchez-Espinel CMirete-Bachiller SMagadán-Mompó S. 2012. Dev Comp Immunol.38:1-9. doi: 10.1016/j.dci.2012.03.001. Epub 2012 Mar 14.

Servicio Gallego de Salud (SERGAS) Unidad de Inmunología, Hospital do Meixoeiro, Carretera de Madrid s/n, Vigo, Pontevedra, Spain. fgambon@gmail.com

Abstract

Immunoglobulins are basic molecules of the immune system of vertebrates. In previous studies we described the immunoglobulins found in two squamata reptiles, Anolis carolinensis and Eublepharis macularius. Snakes are squamata reptiles too but they have undergone an extreme evolutionary process. We therefore wanted to know how these changes affected their immunoglobulin coding genes. To perform this analysis we studied five snake transcriptomes and two genome draft sequences. Sequences coding for immunoglobulin M (IgM), immunoglobulin D (IgD) and two classes of immunoglobulin Y (IgY - named IgYa and IgYb-) were found in all of them. Moreover, the Thamnophis elegans transcriptome and Python molurus genome draft sequences showed a third class of IgY, the IgYc, whose constant region only presents three domains and lacks the CH2. All data suggest that the IgYb is the evolutionary origin of this IgYc. An exhaustive search of the light chains were carried out, being lambda the only light chain found in snakes. The results provide a clear picture of the immunoglobulins present in the suborder Serpentes.

Copyright © 2012 Elsevier Ltd. All rights reserved.

PMID:
22426516
[PubMed - indexed for MEDLINE]
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