Universitą degli studi di Pavia
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Covini research activity
Detailed studies about the maturation of antibody responses towards a model of an antigen, the hapten 2-phenyloxazolone (phOX), undertaken several years ago by the laboratory of C. Milstein, found that the maturation of affinity involves different strategies.
Although the system has been genetically and biochemically well characterized, from a structural point of view for many years the only available structure has been that of antibody fragment Fab NQ10/12.5. In order to clarify the structural basis of affinity maturation in this experimental system, the project of determine the crystal structure of nine scFv antibodies with different affinity has been set up: the antibodies derived, from three different classes defined according to the same genetic similarity.
Until now, the structure of four antibodies, anti-Phox, NQ10/1.12, NQ16/113.8, NQ2/16.2 and NQ11/7.12 has been determined.
My research project consists in improving the production of crystals of two antibodies NQ10/1.12 and NQ16/113.8, whose structures has already been obtained at a resolution of 2.7 Ǻ, using the most innovative and the most favourable conditions.
The structure of these antibodies, obtained at higher resolution, should thus help to resolve structural questions still existing and should contribute to a better understanding of affinity maturation in the phOX system and suggest new research lines based on the structures of anti-phOX antibody.
Although the system has been genetically and biochemically well characterized, from a structural point of view for many years the only available structure has been that of antibody fragment Fab NQ10/12.5. In order to clarify the structural basis of affinity maturation in this experimental system, the project of determine the crystal structure of nine scFv antibodies with different affinity has been set up: the antibodies derived, from three different classes defined according to the same genetic similarity.
Until now, the structure of four antibodies, anti-Phox, NQ10/1.12, NQ16/113.8, NQ2/16.2 and NQ11/7.12 has been determined.
My research project consists in improving the production of crystals of two antibodies NQ10/1.12 and NQ16/113.8, whose structures has already been obtained at a resolution of 2.7 Ǻ, using the most innovative and the most favourable conditions.
The structure of these antibodies, obtained at higher resolution, should thus help to resolve structural questions still existing and should contribute to a better understanding of affinity maturation in the phOX system and suggest new research lines based on the structures of anti-phOX antibody.
