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Y measures binding to soluble gH/gL. The loss of membrane
Mutant d57-61 is capable to promote close to wild-type membrane fusion but Soraprazan completely loses binding to soluble gH/gL as detected in CELISA. The longest peptide from gp42 residues 36 to 81, which has nanomolar binding to gH/gL, was unable to rescue membrane fusion with any with the gp42 mutants, such as the gp42 mutant lacking residues 45 to 89. These data indicate that the contiguity on the gp42 C-terminal lectin domain with N-terminal gp42/gH/gL complexes is very important for full fusogenic activity. EBV infection assay with gp42-derived peptide 36-81. In an effort to test the impact of peptide 36-81 on entry in the entire viru.Y measures binding to soluble gH/gL. The loss of membrane
Y measures binding to soluble gH/gL. The loss of membrane fusion activity for some gp42 mutants could possibly be due to a lack of binding to gH/gL or to deletion of gp42 residues otherwise significant for fusion activation. To investigate this hypothesis, a gH/gL-based CELISA was employed in addition to immunoprecipitation, along with the information revealed that some defective gp42 mutants are similar to wild-type gp42 in binding gH/gL, some show moderately diminished binding, and some completely drop any interaction with gH/gL. Correlating the capacity of mutants to function in membrane fusion with all the capacity to bind soluble gH/gL distinguishes 3 categories of mutants (Table 1): category 1, inconsequential mutants remaining totally functional; category 2, loss of fusion but maintenance of wild-type gH/gL binding; and category three, decreased or complete loss of fusion on account of altered binding to PubMed ID:https://www.ncbi.nlm.nih.gov/pubmed/27459367 gH/gL. Category 1 mutants are innocuous deletions and/or single substitutions which have no key impact on gp42 or gH/gL function. The d57-61 mutant seems to lack gH/gL binding within the CELISA but could mediate fusion. However, there are some discrepancies amongst PubMed ID:https://www.ncbi.nlm.nih.gov/pubmed/27513814 the immunoprecipitation information and CELISA measurements for the binding of gp42 mutants to gH/gL. These variations can be on account of interactions gp42 might have with transfected gH/gL during protein expression and folding, possibly inside the proteins‘ membrane spanning domains. Mutant d57-61 is capable to promote near wild-type membrane fusion but fully loses binding to soluble gH/gL as detected in CELISA. This is a peculiar mutant that was hard to detect in Western blotting although surface expression levels were regularly greater than wild-type gp42 (Fig. 1B and 2B). There could be a important contribution by the uncommon tetra-proline structure (residues 57 to 60) in binding gH/gL, but a almost wild-type degree of fusion is maintained in its absence. For HSV gD, that is a functional homolog for gp42, it is actually believed that a flexible proline-rich area becomes exposed upon receptor binding, thus activating gH/gL and gB for membrane fusion (5, 6, 9, 24). We reasoned that the N-FIG. 7. Peptide 36-81 inhibits EBV entry into epithelial cells. A graph of a representative EBV infection assay shows the inhibitory effect of gp42-derived peptide 36-81. Virus was incubated with antigH/gL antibody E1D1, soluble gp42, or peptide 36-81 at 20 nM.
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