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

Authors

Oluwatoyin A. Asojo, Eppley Institute for Research in Cancer and Allied Diseases, Omaha, NEFollow
Alex Loukas, The George Washington University Medical Center
Mehmet Inan, University of Nebraska–LincolnFollow
Rick Barent, University of Nebraska–Lincoln
Jicai Huang, University of Nebraska–Lincoln
Brad Plantz, University of Nebraska–Lincoln
Amber Swanson, University of Nebraska–LincolnFollow
Mark Gouthro, University of Nebraska–Lincoln
Michael M. Meagher, University of Nebraska-LincolnFollow
Peter J. Hotez, The George Washington University Medical CenterFollow

Date of this Version

2005

Document Type

Article

Citation

Acta Crystallographica Section F Structural Biology and Crystallization Communications (2005). F61, 391–394. doi:10.1107/S1744309105007748

Comments

(c) 2005 International Union of Crystallography. Used by permission.

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 P21 with unit-cell parameters a = 67.7, b = 74.27, c = 84.60 Å, β = 112.12°. An initial molecular-replacement solution has been obtained with one monomer in the asymmetric unit.