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Crystallization and preliminary X‐ray analysis of Na ‐ASP‐1, a multi‐domain pathogenesis‐related‐1 protein from the human hookworm parasite Necator americanus
Author(s) -
Inan Mehmet,
Loukas Alex,
Huang Jicai,
Asojo Oluwatoyin A.,
Barent Rick,
Plantz Brad,
Hotez Peter J.,
Swanson Amber,
Gouthro Mark,
Meagher Michael M.
Publication year - 2005
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309105007748
Subject(s) - necator americanus , biology , hookworm infections , ancylostoma , hookworm infection , ancylostoma duodenale , pathogenesis , virology , immunology , helminths , ascaris lumbricoides
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 P 2 1 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.

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