ABSTRACT
Objective :To explore influence on prognosis in patients with coronary critical lesion assessed by coronary angiography (CAG) ,CAG combined coronary fractional flow reserve test (FFR) and CAG combined frequency do-main optical coherence tomography (FD-OCT ).Methods : Patients with coronary critical lesion who don't need stenting were screened by three detection programs , they were divided into CAG group (n＝ 45 , only received CAG) ,CAG+ FFR group (n＝45 ,received CAG+FFR) and CAG+ FD-OCT group (n＝45 ,received CAG+ FD-OCT).All three groups received secondary prevention of stable coronary heart disease for half a year .Incidence rates of angina pectoris (aggravated ) ,myocardial infarction and target vessel revascularization rate were observed and compared among three groups .Results :Compared with CAG group ,there were significant reductions in inci-dence rates of angina pectoris (33.3% vs.4.4%,6.7%) ,myocardial infarction (20.0% vs.4.4%,2.2%) and target vessel revascularization rate (26.6% vs.6.7%,2.2%) in CAG+FFR group and CAG+FD-OCT group ,P＜0.05 or ＜0.01. There were no significant difference between CAG + FFR group and CAG+ FD-OCT group , P＞0.05 all.Conclusion : Compared with pure CAG ,CAG combined FFR or FD-OCT can more effectively assess cardi-ac blood supply ,and improvement prognosis in patients with critical lesion .
ABSTRACT
<p><b>OBJECTIVE</b>To prepare and characterize monoclonal antibodies (mAbs) against the recombinant nucleocapsid (N) protein of 3 human coronaviruses SARS-CoV, 229E and OC43 and study the antigenic relationship between the 3 N proteins.</p><p><b>METHODS</b>BALB/c mice were immunized with the recombinant N proteins of SARS-CoV, 229E and OC43 to obtain the mAbs by means of hybridoma. Screening and identification of the mAbs were performed using indirect enzyme-linked immunosorbent assay (ELISA), Western blotting and indirect immunofluorescence assay. Cross-reactivity between the N proteins of the 3 coronaviruses was analyzed with the prepared mAbs.</p><p><b>RESULTS</b>The mAbs against the recombinant N proteins of SARS-CoV, 229E and OC43 were obtained, which reacted specifically with the corresponding viral N protein as shown by indirect ELISA, Western blotting and indirect immunofluorescence assay. No cross-reactivity was found between the 3 N proteins.</p><p><b>CONCLUSION</b>The prepared mAbs against the recombinant N proteins may provide valuable assistance in studying antigenic relationships of N proteins between the 3 human coronaviruses.</p>
Subject(s)
Animals , Female , Humans , Mice , Antibodies, Monoclonal , Allergy and Immunology , Blotting, Western , Coronavirus 229E, Human , Genetics , Allergy and Immunology , Coronavirus OC43, Human , Genetics , Allergy and Immunology , Cross Reactions , Allergy and Immunology , Enzyme-Linked Immunosorbent Assay , Fluorescent Antibody Technique, Indirect , Mice, Inbred BALB C , Nucleocapsid Proteins , Genetics , Allergy and Immunology , Recombinant Proteins , Allergy and Immunology , Severe acute respiratory syndrome-related coronavirus , Genetics , Allergy and ImmunologyABSTRACT
<p><b>OBJECTIVE</b>The present study aimed to clone and express three fragments of genomic RNA derived from SARS associated coronavirus (SARS-CoV) S1 domain and to study its immunogenicity.</p><p><b>METHODS</b>The S1 domain gene was amplified by PCR with specific primers and was inserted into the prokaryotic expression vector pQE-30. Three fragments (40-751, 746-1344 and 746-2001 bp) derived from S1 domain produced after the recombinant plasmid (pQE-30/S1) was digested by restriction endonucleases. The three fragments were cloned into pQE-30 and expressed in M15 strains of Escherichia coli. The expression products, designated S1a, S1b and S1c respectively, were purified by Ni affinity chromatography. The immunogenicity was analyzed by Western Blot and ELISA using serologically confirmed sera from SARS patients and the sera from healthy donors was used as control at the same assay.</p><p><b>RESULTS</b>Three recombinant plasmids (pQE-30/S1a, pQE-30/S1b, pQE-30/S1c) were constructed.Fusion proteins with relative molecular mass of 26,700, 22,500 and 46,000 dalton were successfully expressed with amounts of 35%, 35% and 30% of total cell protein and purified by Ni affinity chromatography, respectively. Western Blot and ELISA analysis showed that the S1c protein could be specifically recognized by the sera from SARS patients.</p><p><b>CONCLUSION</b>The recombinant S1c protein was a good immunogen and has the potential to be used as a vaccine against SARS-CoV infection.</p>