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

Mehmet İnan, Queensland Institute of Medical Research
Oluwatoyin A. Asojo, Nebraska Medical Center
Alex Lucas, George Washington University Medical Center
Rick Barent, University of Nebraska-Lincoln
Jicai Huang, University of Nebraska-Lincoln
Brad Plantz, University of Nebraska-Lincoln
Amber Swanson, University of Nebraska-Lincoln
Mark Gouthro, University of Nebraska-Lincoln
Michael M. Meagher, University of Nebraska-Lincoln
Peter J. Hotez, George Washington University Medical Center

Date of this Version

3-10-2005

Citation

Structural Biology and Crystallization Communications: Acta Crystallographica Section F (2005) F61: 391–394

Comments

Copyright © 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 Å 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.