Crystallization and preliminary X-ray analysis ofNa-ASP-1, a multi-domain pathogenesis-related-1 protein from the human hookworm parasiteNecator americanus
| Autor: | Amber Swanson, Oluwatoyin A. Asojo, Michael M. Meagher, Mark A. Gouthro, Mehmet Inan, Rick Barent, Peter J. Hotez, Alex Loukas, Brad Plantz, Jicai Huang |
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| Rok vydání: | 2005 |
| Předmět: |
Necator americanus
Biophysics Polymerase Chain Reaction Biochemistry law.invention Pathogenesis X-Ray Diffraction Structural Biology law parasitic diseases Genetics Animals Humans Parasite hosting Cloning Molecular Crystallization X ray analysis biology Condensed Matter Physics biology.organism_classification Molecular biology Recombinant Proteins Multi domain Ancylostoma Crystallization Communications Antigens Helminth Immunology |
| Zdroj: | Acta Crystallographica Section F Structural Biology and Crystallization Communications. 61:391-394 |
| ISSN: | 1744-3091 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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