Anti-idiotypic monoclonal antibody 409.5.3 is raised against an antibody that neutralizes feline Infectious peritonitis virus. This antibody, used as an immunogen, elicits the production of anti-anti-idiotypic antibodies that in turn neutralize the virus. The crystal structure of the complex between anti-idiotypic Fab 409.5.3 and idiotypic Fab fragment of virus-neutraling antibody has been solved by molecular replacement using real-space Patterson search and filtering by Patterson correlation-coefficient refinement. The structure has been refined to an R value of 0.21 based on 21,310 unique reflections between 40.0 and 2.9 A. The three-dimensional structure reveals extensive, specific interactions that involve 118 van der Waals contacts and at least 9 probable hydrogen bonds. The two Fabs are rotated 610 with respect to each other around the approximate long axis ofthe complex and are within 26°of being aligned along their major axes.According to the Jerne hypothesis (1), the immune system responds to foreign substances as a regulatory network composed of idiotypes (Abis)
A scale of relative affinities of a series of 2'-deoxycytidine and cytidine (CD) derivatives was established based on the data of cross-reactivities of these compounds as well as the displacements obtained from a competitive ELISA. No correlation could be established between the nucleosides modifying structures and the affinities. This can be explained by the possibilities of the modifying structures of intra- and intermolecular nonimmunospecific interactions owing to their degree of functionalization.
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