Interaction between Hemagglutinin Protein of Peste des Petits Ruminants Virus and Signalling Lymphocyte Activation Molecule

This experiment was conducted to explore the interaction between PPRV Hemagglutinin(H)protein and signalling lymphocyte activation molecule(SLAM)by co-immunoprecipitation.In view of the truncated H protein still has normal binding capacity to cell receptor,the genes of tH,SLAMand its several deletion mutants which lacked transmembrane and intracellular fragments(m1),a signal peptide fragment(m2)or C-terminal fragment(amino acids 29-136,m3)or N-terminal fragment(amino acids 137-240,m4),were directionally cloned into eukaryotic expression vectors pcDNA3.1and pEGFP-N1,respectively.The recombinant plasmids were co-transfected into CHO-K1cells,and then the key amino acid regions of viral protein and SLAM protein interactions was identified initially by co-immunoprecipitation.The results showed that 1)The recombinant vectors were constructed successfully,and the proteins were expressed correctly in CHO cell;2)tH was identified can interact with SLAM,m1,m2and m3,and can not with m4by co-immunop recipitation.These results indicated that the N-terminal segment(amino acids 29-136)of SLAM was essential to bind to PPRV H protein.This finding is agreed with that of Morbillivirus receptor SLAM.