Porcine CD83 is a glycosylated dimeric protein existing naturally in membrane-bound and soluble forms.

Abstract Human and mouse CD83 have been well characteized, however, the other mammalian CD83 genes have not been cloned and characterized. In this study, the porcine CD83 (pCD83) was cloned, expressed and characterized, and showed that the pCD83 gene has 81% and 74% homologies with humans and mice, respectively, which was identified to be glycosylated when expressed in eukaryotic cells, existing naturally in two forms: membrance-bound CD83 (mCD83) and soluble CD83 (sCD83), the latter was identified to be generated mainly from mCD83 by proteolytic shedding. The pCD83 was a dimmer mediated by intermolecular disulfide bond formed by the fifth cysteine in the exrtracellular domain. Functionally, the recombinant porcine sCD83 was preliminarily tested to have the ability to inhibit DC-mediated T cell activition. This study provided necessary fundation for further investigation on pCD83 functions. Highlights • The pCD83 gene was cloned and its sequence was analyzed. • The pCD83 is highly glycosylated dimeric protein. • The pCD83 existed in membrane-bound and soluble forms. • Soluble pCD83 inhibits dendritic cell-mediated T cell activation. [ABSTRACT FROM AUTHOR]