Plasma Proteomic Analysis Of Severe Acute Respiratory Syndrome

Severe acute respiratory syndrome (SARS) was a severe infectious disease that had affected many countries and regions since 2002. A novel member of coronavirus (SARS-CoV) was identified as the causative agent. But the pathogenesis of SARS is still elusive. In this study, we used two dimensional difference gel electrophoresis (2D-DIGE) and mass spectrometry to analyze the protein profile of the plasma with SARS, in order to search for disease progression associated alerteration that could provide some clue for pathogenesis research. Albumin and IgG count 70% in all the proteins of human plasma, so we depleted them before 2DE. By comparing the plasma of SARS patients with the normal plasma, we found several proteins with significant change. The up-regulated proteins were identified as: alpha-1-acid glycoprotein, haptoglobin, alpha-1 antichymotrypsin, and fetuin. The down-regulated proteins were: apolipoprotein A-I, serotransferrin and transthyretin. Furthermore, we confirmed the alterations of fetuin and antichymotrypsin by western blot. Most of these altered proteins showed significant changes in the acute progressive phase, and then back to normal level during convalescent phase. Because all the up-regulated proteins took part in the inflammation control as anti-inflammation roles, the results above strongly suggested that the body start up inflammation inhibition to sustain the inflammatory response balance in the progression of SARS. Moreover , the variants of akpha-1-acid glycoprotein, transthyretin and haptoglohin made different alteration in each groups, which suggested some special moderation played important role in the progression of SARS.