tailieunhanh - Báo cáo khoa học: Aegyptin displays high-affinity for the von Willebrand factor binding site (RGQOGVMGF) in collagen and inhibits carotid thrombus formation in vivo

Aegyptin is a 30 kDa mosquito salivary gland protein that binds to collagen and inhibits platelet aggregation. We have studied the biophysical properties of aegyptin and its mechanism of action. Light-scattering plot showed that aegyptin has an elongated monomeric form, which explains the apparent molecular mass of 110 kDa estimated by gel-filtration chromatography. | Aegyptin displays high-affinity for the von Willebrand factor binding site RGQOGVMGF in collagen and inhibits carotid thrombus formation in vivo Eric Calvo1 z Fuyuki Tokumasu2 Daniella M. Mizurini3 Peter McPhie4 David L. Narum5 Jose Marcos C. Ribeiro1 Robson Q. Monteiro3 and Ivo M. B. Francischetti1 1 Section of Vector Biology Laboratory of Malaria and Vector Research National institute of Allergy and Infectious Diseases NIAID . NIH Bethesda MD USA 2 Malaria Genetics Section Laboratory of Malaria and Vector Research National institute of Allergy and Infectious Diseases NIAID . NIH Bethesda MD USA 3 Instituto de Bioquimica Medica Universidade Federaldo Rio de Janeiro Rio de Janeiro Brazil 4 Laboratory of Biochemistry and Genetics NationalInstituteof Diabetes and Digestive and Kidney Diseases NIDDK NIH Bethesda MD USA 5 Malaria Vaccine Development Branch NationalInstitute of Allergy and Infectious Diseases NIAID NIH Bethesda MD USA Keywords aegyptin blood-sucking GPVI thrombosis yellow fever Correspondence . Francischetti Laboratory of Malaria and Vector Research National Institute of Allergy and Infectious Diseases NIAID NIH 12735 Twinbrook Parkway Room 2E-28 Bethesda MD 20852 USA Fax 1 301 480 2571 Tel 1 301 402 2748 E-mail ifrancischetti@ Present address Food and Drug Administration Center for Drug Evaluation and Research Bethesda MD USA Received 27 April2009 revised 26 October 2009 accepted 12 November 2009 doi Aegyptin is a 30 kDa mosquito salivary gland protein that binds to collagen and inhibits platelet aggregation. We have studied the biophysical properties of aegyptin and its mechanism of action. Light-scattering plot showed that aegyptin has an elongated monomeric form which explains the apparent molecular mass of 110 kDa estimated by gel-filtration chromatography. Surface plasmon resonance identified the sequence RGQOGVMGF where O is hydroxyproline that mediates collagen interaction with von Willebrand .