Anti-acetylcholine receptor antibodies （AAR） are considered pathognomonic and pathogenetic for myasthenia gravis （MG）. AAR detection confirms clinical diagnosis of MG. However, AAR is rarely detected in patients w...Anti-acetylcholine receptor antibodies （AAR） are considered pathognomonic and pathogenetic for myasthenia gravis （MG）. AAR detection confirms clinical diagnosis of MG. However, AAR is rarely detected in patients without MG. The underlying pathophysiological mechanisms in a normal subject without MG have not been adequately addressed in previous studies. The present study reports on a case study of a healthy, elderly man with high AAR titers for 14 years. Pathophysiological mechanisms could be due to AAR heterogeneity in specificity, affinity, and multiform, and to muscle variability in response to AAR.展开更多
Single-chain variable domain fragment （scFv） 637 is an antigen-specific scFv of myasthenia gravis. In this study, scFv and human serum albumin genes were conjugated and the fusion pro-tein was expressed in Pichia pa...Single-chain variable domain fragment （scFv） 637 is an antigen-specific scFv of myasthenia gravis. In this study, scFv and human serum albumin genes were conjugated and the fusion pro-tein was expressed in Pichia pastoris. The afifnity of scFv-human serum albumin fusion protein to bind to acetylcholine receptor at the neuromuscular junction of human intercostal muscles was detected by immunolfuorescence staining. The ability of the fusion protein to block myas-thenia gravis patient sera binding to acetylcholine receptors and its stability in healthy serum were measured by competitive ELISA. The results showed that the inhibition rate was 2.0-77.4%, and the stability of fusion protein in static healthy sera was about 3 days. This approach suggests the scFv-human serum albumin is a potential candidate for speciifc immunosuppressive therapy of myasthenia gravis.展开更多
文摘Anti-acetylcholine receptor antibodies （AAR） are considered pathognomonic and pathogenetic for myasthenia gravis （MG）. AAR detection confirms clinical diagnosis of MG. However, AAR is rarely detected in patients without MG. The underlying pathophysiological mechanisms in a normal subject without MG have not been adequately addressed in previous studies. The present study reports on a case study of a healthy, elderly man with high AAR titers for 14 years. Pathophysiological mechanisms could be due to AAR heterogeneity in specificity, affinity, and multiform, and to muscle variability in response to AAR.
基金supported by the National Natural Science Foundation of China,No.30360100,30760234,30860260,81160373,81360458
文摘Single-chain variable domain fragment （scFv） 637 is an antigen-specific scFv of myasthenia gravis. In this study, scFv and human serum albumin genes were conjugated and the fusion pro-tein was expressed in Pichia pastoris. The afifnity of scFv-human serum albumin fusion protein to bind to acetylcholine receptor at the neuromuscular junction of human intercostal muscles was detected by immunolfuorescence staining. The ability of the fusion protein to block myas-thenia gravis patient sera binding to acetylcholine receptors and its stability in healthy serum were measured by competitive ELISA. The results showed that the inhibition rate was 2.0-77.4%, and the stability of fusion protein in static healthy sera was about 3 days. This approach suggests the scFv-human serum albumin is a potential candidate for speciifc immunosuppressive therapy of myasthenia gravis.
