Affinity ranking of influenza neuraminidase mutants with monoclonal antibodies using an optocal biosensor comparison with ELISA and slot blot assays

The structure of a complex between the NC10 antibody and influenza virus neuraminidase and comparison with the overlapping binding site of the NC41 antibody

“…The association constant of the NC10 Fab-whale N9 neuraminidase complex calculated from sedimentation equilibrium data (2x10 7 M -1 ) [37] is similar to that of the NC41 Fab-tern N9 neuraminidase complex (1.2x 10 7 M -1 ) [37]. These values are approximately 100 times lower than those yielded by measuring (with an optical biosensor) the binding of neuraminidase to immobilized Fab [38]. As mentioned above, the shape complementarity values S c for the two complexes are similar being 0.65 for the NC10 complex and 0.66 for the NC41 complex.…”

Influenza virus neuraminidase: Structure, antibodies, and inhibitors

“…However, there are also data that illustrate that in some settings more dramatic structural changes can be tolerated. For example, an Ile to Arg substitution within the interface of one of the neuraminidase-antibody complexes is tolerated with a loss of a factor of 1-2 orders of magnitude in the association constant (Webster et al, 1987;Gruen et al, 1994). In this case, the structure of the mutant complex shows that amino acid side chains on the mutant antigen have different conformation in the free and complexed structures, and that side chains of the antibody have different conformation in the wild-type and mutant complexes (Tulip et al, 1992b).…”

Surface plasmon resonance: approaches and perspectives of application for virus-specific interactions investigations

“…Gruen et al [25] у своїй роботі порівнювали можливості імуноферментного аналізу і ППР на прикладі нейрамінідази вірусу грипу. Автори досліджували здатність різних варіантів нейрамінідази вірусу грипу G70C з одиничними амінокислотними замінами зв'язуватися з моноклональними антитілами NC-10 і NC-41 і їх іммобілізованими Fab-фрагментами.…”