Crystallization and preliminary X-ray analysis of Na-ASP-1, a multi-domain pathogenesis-related-1 protein from the human hookworm parasite Necator americanus

Acta Crystallographica. Section F, Structural Biology and Crystallization Communications
Oluwatoyin A AsojoPeter J Hotez

Abstract

Human hookworm infection is a major cause of anemia and malnutrition in the developing world. In an effort to control hookworm infection, the Human Hookworm Vaccine Initiative has identified candidate vaccine antigens from the infective larval stage (L3) of the parasite, including a family of pathogenesis-related-1 (PR-1) proteins known as the ancylostoma-secreted proteins (ASPs). The functions of the ASPs are unknown. In addition, it is unclear why some ASPs have one while others have multiple PR-1 domains. There are no known structures of a multi-domain ASP and in an effort to remedy this situation, recombinant Na-ASP-1 has been expressed, purified and crystallized. Na-ASP-1 is a 406-amino-acid multi-domain ASP from the prevalent human hookworm parasite Necator americanus. Useful X-ray data to 2.2 A have been collected from a crystal that belongs to the monoclinic space group P2(1) with unit-cell parameters a = 67.7, b = 74.27, c = 84.60 A, beta = 112.12 degrees. An initial molecular-replacement solution has been obtained with one monomer in the asymmetric unit.

Citations

Jan 4, 2008·Clinical Infectious Diseases : an Official Publication of the Infectious Diseases Society of America·David J DiemertPeter J Hotez
Jul 23, 2005·FASEB Journal : Official Publication of the Federation of American Societies for Experimental Biology·Jeffrey BethonyPeter J Hotez
May 6, 2011·Acta Crystallographica. Section D, Biological Crystallography·Oluwatoyin A Asojo
May 28, 2011·Parasite Immunology·C CantacessiR B Gasser
May 21, 2010·PLoS Neglected Tropical Diseases·Cinzia CantacessiRobin B Gasser

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