Structural and functional Studies of Na-FAR-1 a Novel Fatty Acid and Retinol Binding Protein from Necator Americanus

MARÍA FLORENCIA REY; EDUARDO DE GERÓNIMO; MARINA IBAÑEZ; MALCOLM W. KENNEDY; ALAN COOPER; BRIAN O. SMITH; BETINA CÓRSICO

San Miguel de Tucumán

Congreso; 45th Annual Meeting-Argentine Society for Biochemistry and Molecular Biology Research; 2009

Sociedad Argentina de Investigación Bioquímica y Biología Molecular (SAIB)

More than 740 million people throughout the world are infected with the human hookworm Necator americanus, which is an intestinal blood-feeding strongyloid nematode. Hookworms cause blood loss, anemia, growth stunting and affect intellectual development, leading to severe problems in developing and underdeveloped countries. Aboriginal communities in the north of Argentina screened for parasitic infections show 50% positivity to hookworms. Among the genes expressed by adult N.americanus, a FAR protein, Na-FAR-1, has been identified by sequence homology [2]. The FAR proteins(Fatty Acid and Retinol Binding Proteins) are a structurally novel class of helix rich fatty acid and retinol binding proteins with highly unusual structure that has no known counterpart.The retinol binding proteins described to date are all β-strand rich proteins which form β-barrel structures having a binding site for retinol in their interiors[3]. FARs are confined to Nematodes and are secreted by the parasites into the surrounding tissues of the host, playing a central role in the establishment of the infection[4].