IDEHU   05542
INSTITUTO DE ESTUDIOS DE LA INMUNIDAD HUMORAL PROF. RICARDO A. MARGNI
Unidad Ejecutora - UE
congresos y reuniones científicas
Título:
Kinetic and thermodynamic studies of the interaction between activating and inhibitory LY49 Natural Killer receptors and MHC-I molecules
Autor/es:
ROMASANTA, PABLO N.; SARRATEA, BELÉN; TODONE MARCOS; ANTONOGLOU, BELÉN; NOLI TRUANT SOFIA; FERNÁNDEZ LYNCH MARÍA JULIETA; DE MARZI MAURICIO; CURTO, LUCRECIA; DELFINO, JOSE MARÍA; FERNÁNDEZ MARISA MARIEL; MALCHIODI EMILIO LUIS
Lugar:
Mar del Plata, Buenos Aires, Argentina
Reunión:
Congreso; LXII REUNIÓN CIENTÍFICA DE LA SOCIEDAD ARGENTINA DE INMUNOLOGÍA; 2014
Institución organizadora:
Sociedad Argentina de Inmunologia (SAI)
Resumen:
The interactions between mice Natural Killer (NK) cell receptors Ly49 and the endogenous mayor histocompatibility complex type I (MHC-I) ligands are of capital importance for the regulation of viral infections and tumorigenic processes. The interactions Ly49H/H-2Dd, Ly49I/H-2Dd and Ly49G/H-2Dk were particularly studied. They embrace the structural heterogeneity of Ly49 and interact with different MHC-I alleles. Thermodynamic and kinetic experiments were carried out in order to elucidate the Ly49/MHC-I binding mechanism. Combining surface plasmon resonance (SPR), fluorescence anisotropy (FA), and far-UV circular dichroism (CD), an identical and independent binding sites model was determined, where the MHC-I binds to Ly49 with a ~106 M-1 binding constant. There is no evidence of a strong positive cooperativity such as seen with the interactions between Ly49 and m157, a murine cytomegalovirus decoy molecule. The rate-limiting step of the overall mechanism is the diffusion of the molecules. Using SPR we also studied the Ly49G/MHC-I peptide insensitivity, and identified for the first time interactions between activating Ly49H and endogenous ligands in the absence of viral molecules.