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J Biol Chem, Vol. 274, Issue 44, 31456-31462, October 29, 1999

Mapping the Interaction Between Murine IgA and Murine Secretory Component Carrying Epitope Substitutions Reveals a Role of Domains II and III in Covalent Binding to IgA

Pascal Crottet and Blaise Corthésy^¶

From the  Institut Suisse de Recherches Expérimentales sur le Cancer, CH-1066 Epalinges and ^¶ Division d'immunologie et d'allergie, Centre Hospitalier Universitaire Vaudois, CH-1011 Lausanne, Switzerland

We have identified sites for epitope insertion in the murine secretory component (SC) by replacing individual surface-exposed loops in domains I, II, and III with the FLAG sequence (Crottet, P., Peitsch, M. C., Servis, C., and Corthésy, B. (1999) J. Biol. Chem. 274, 31445-31455). We had previously shown that epitope-carrying SC reassociated with dimeric IgA (IgA_d) can serve as a mucosal delivery vehicle. When analyzing the capacity of SC mutants to associate with IgA_d, we found that all domain II and III mutants bound specifically with immobilized IgA_d, and their affinity for IgA_d was comparable to that of the wild type protein (IC₅₀ ~ 1 nM). We conclude that domains II and III in SC are permissive to local mutation and represent convenient sites to antigenize the SC molecule. No mutant bound to monomeric IgA. SC mutants exposing the FLAG at their surface maintained this property once bound to IgA_d, thereby defining regions not required for high affinity binding to IgA_d. Association of IgA_d with SC mutants carrying a buried FLAG did not expose de novo the epitope, consistent with limited, local changes in the SC structure upon binding. Only wild type and two mutant SCs bound covalently to IgA_d, thus implicating domains II and III in the correct positioning of the reactive cysteine in SC. This establishes that the integrity of murine SC domains II and III is not essential to preserve specific IgA_d binding but is necessary for covalency to take place. Finally, SC mutants existing in the monomeric and dimeric forms exhibited the same IgA_d binding capacity as monomeric wild type SC known to bind with a 1:1 stoichiometry.

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