cDNA Cloning of a Mannose-Binding Lectin-Associated Serine Protease (MASP) Gene from Hagfish (Eptatretus burgeri)

Autor: Tamotsu Fujii, Yoshiaki Sugawara, Liqiu Song, Kazufumi Takamune
Rok vydání: 2005
Předmět:
Zdroj: Zoological Science. 22:897-904
ISSN: 0289-0003
DOI: 10.2108/zsj.22.897
Popis: Hagfish, agnathan cyclostome, is the most primitive extant vertebrate and its complement (C) system seems to be a primordial system in comparison with a well-developed C system in gnathostome vertebrates. From a phylogenic perspective of defense mechanisms, we have isolated complement C3 from the serum of hagfish (Eptatretus burgeri). In this study, we first attempted to identify a hagfish Bf or C2 as a C3 convertase by RT-PCR using degenerative primers designed on the basis of the conserved amino acid stretches among the several kinds of serine proteases. Contrary to our expectation, homology search of cloned RT-PCR product suggested that there was a partial cDNA encoding the homologue of neither Bf nor C2 but a mannose-binding lectin-associated serine protease (MASP). Analyses of a full-length cDNA clone isolated from a hagfish liver cDNA library by using the partial cDNA as a probe indicated that this cDNA encoded hagfish MASP 1. This evidence strongly suggests that the hagfish defends itself against pathogens at least by the complement system composed of lectin pathway.
Databáze: OpenAIRE