Research Article

Characterization of Riemerella anatipestifer CH-1 gldJ gene and GldJ protein

Published: October 20, 2014
Genet. Mol. Res. 13 (4) : 8329-8341 DOI: https://doi.org/10.4238/2014.October.20.9
Cite this Article:
(2014). Characterization of Riemerella anatipestifer CH-1 gldJ gene and GldJ protein. Genet. Mol. Res. 13(4): gmr3843. https://doi.org/10.4238/2014.October.20.9
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Abstract

Riemerella anatipestifer (RA) CH-1, a highly virulent field strain, was isolated and identified by our laboratory. The gldJ gene was conserved in RA, and it had a typical TATA promoter region and AU-rich sequence within the 5' untranslated region. The GldJ protein was an outer-membrane lipoprotein with a signal peptide cleavage site between amino acids 20 and 21. GldJ was also a member of proteins involved in gliding motility. The RA GldJ protein had 16 phosphorylation sites and 4 N-glycosylation sites. These functional sites played an important role in the posttranslational modification of the GldJ protein. In addition, the GldJ protein of RA CH-1 had strong immunogenicity. Fifteen B-cell epitopes were identified in the GldJ protein, which might be a good biological material for the development of a subunit vaccine and diagnostic reagents. The GldJ protein also had the activity of formylglycine-generating sulfatase enzyme. The 3-dimensional structure models of GldJ were constructed based on 2 templates using the SwissModel automatic modeling mode in the SWISS-MODEL workplace. Here, we characterized the RA gldJ gene and GldJ protein to contribute to the functional annotation for the GldJ protein.

Riemerella anatipestifer (RA) CH-1, a highly virulent field strain, was isolated and identified by our laboratory. The gldJ gene was conserved in RA, and it had a typical TATA promoter region and AU-rich sequence within the 5' untranslated region. The GldJ protein was an outer-membrane lipoprotein with a signal peptide cleavage site between amino acids 20 and 21. GldJ was also a member of proteins involved in gliding motility. The RA GldJ protein had 16 phosphorylation sites and 4 N-glycosylation sites. These functional sites played an important role in the posttranslational modification of the GldJ protein. In addition, the GldJ protein of RA CH-1 had strong immunogenicity. Fifteen B-cell epitopes were identified in the GldJ protein, which might be a good biological material for the development of a subunit vaccine and diagnostic reagents. The GldJ protein also had the activity of formylglycine-generating sulfatase enzyme. The 3-dimensional structure models of GldJ were constructed based on 2 templates using the SwissModel automatic modeling mode in the SWISS-MODEL workplace. Here, we characterized the RA gldJ gene and GldJ protein to contribute to the functional annotation for the GldJ protein.

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