sialidase การใช้

• Rational design of potent sialidase-based inhibitors of influenza virus replication.
• The sialidase is one of the most important enzymes of the sialic acid catabolism.
• Sialidase has also been shown to enhance recovery from spinal cord contusion injury when injected in rats.
• Glycoside hydrolase family 34 CAZY GH _ 34 comprises enzymes with only one known activity; sialidase or neuraminidase.
• The enzymatic mechanism of influenza virus sialidase has been studied by Taylor et al ., shown in Figure 1.
• One is the lectin haemagglutinin protein with three relatively shallow sialic acid-binding sites and the other is enzyme sialidase with the active site in a pocket.
• S and s antigens are not affected by treatment with trypsin or sialidase but are destroyed or much depressed by treatment with papain, pronase or alpha-chymotrypsin.
• One experiment has demonstrated that, by using the enzyme sialidase, the genetic defect can be effectively bypassed and GM2 gangliosides can be metabolized so that they become almost inconsequential.
• Structure of trans-sialidase includes a catalytic beta-propeller domain, a N-terminal lectin-like domain and an irregular beta-stranded domain inserted into the catalytic domain.
• The ganglioside-converting enzyme plasma membrane ganglioside sialidase ( PMGS ), which is involved in the activation of TrkA at the tip of neutrites, is required for the elongation of axons.
• If a safe pharmacological treatment can be developed, one that causes the increased expression of lysosomal sialidase in neurons, a new form of therapy, essentially curing the disease, could be on the horizon.
• The 1.8 A structure of trans-sialidase from leech ( " Macrobdella decora ", ) in complex with 2-deoxy-2, 3-didehydro-NeuAc was solved.
• The first step involves the distortion of the ?-sialoside from a 2 C 5 chair conformation ( the lowest-energy form in solution ) to a pseudoboat conformation when the sialoside binds to the sialidase.
• Because of the relative deep active site in which low-molecular-weight inhibitors can make multiple favorable interactions and approachable methods of designing transition-state analogues in the hydrolysis of sialosides, the sialidase becomes more attractive anti-influenza drug target than the haemagglutinin.
• These interactions are quite specific; no binding could be detected between these siglecs and unsulfated sialyl Lewis X or sialyl Lewis X sulfated at carbon 6 of GlcNAc ( 6-sulfo-sialyl Lewis X ) rather than carbon 6 of galactose as in 62-sulfo-sialyl Lewis X . Similarly, no other siglecs bind effectively to these Siglec-8 ligands, as demonstrated by selective binding to eosinophils in human blood of a polymer decorated with 62-sulfo-sialyl Lewis X . The natural ligand or ligands for Siglec-8 have not yet been positively identified, but ongoing studies have determined that there are sialidase-sensitive glycoprotein ligands for Siglec-F in mouse airways that require the activity of the ?2, 3 sialyltransferase 3 ( ST3Gal-III ) enzyme for their generation.