Cloning and Characterization of the IgA Fc Receptor from Swine

J Microbiol Biotechnol. 2016 Dec 28;26(12):2192-2198. doi: 10.4014/jmb.1607.07011.

Abstract

The myeloid-specific IgA Fc receptor (FcαR) is a cell surface molecule on immunocytes that provides a fundamental connection between humoral and cellular immunity. In this study, the full-length cDNA sequence of swine FcαRI (swFcαRI) was isolated and characterized and found to contain a 792-base-pair open reading frame, encoding a 264-amino-acid transmembrane glycoprotein with a predicted molecular mass of 29.4 kDa. The swFcαRI shares high amino acid sequence homology (>50%) with its counterparts from cattle, seal, and horse. Rosetting analysis confirmed that COS-7 cells transfected with an swFcαRI expression plasmid was able to combine with chicken erythrocytes sensitized with porcine IgA, but not IgG.

Keywords: FcαRI; IgA Fc receptor; Swine.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Base Sequence
  • Cattle
  • Cloning, Molecular*
  • Humans
  • Immunoglobulin A / genetics
  • Immunoglobulin A / metabolism*
  • Mammals / classification
  • Mammals / genetics
  • Molecular Sequence Data
  • Open Reading Frames
  • Phylogeny
  • Protein Conformation
  • Protein Domains
  • Receptors, Fc / chemistry
  • Receptors, Fc / genetics*
  • Receptors, Fc / metabolism
  • Sequence Alignment
  • Swine

Substances

  • Immunoglobulin A
  • Receptors, Fc