Open AccessCrystallization and preliminary X‐ray analysis of Na‐SAA‐2 from the human hookworm parasite Necator americanus
Author(s) -
Asojo Oluwatoyin A.,
Goud Gaddam N.,
Zhan Bin,
Ordonez Katherine,
Sedlacek Meghan,
Homma Kohei,
Deumic Vehid,
Gupta Richi,
Brelsford Jill,
Price Merelyn K.,
Ngamelue Michelle N.,
Hotez Peter J.
Publication year - 2010
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309109051616
Subject(s) - necator americanus , biology , hookworm infections , nematode , antigen , helminths , parasite hosting , host (biology) , feces , microbiology and biotechnology , virology , immunology , ecology , ascaris lumbricoides , world wide web , computer science
Human hookworms are among the most pathogenic soil‐transmitted helminths. These parasitic nematodes have co‐evolved with the host and are able to maintain a high worm burden for decades without killing the human host. However, it is possible to develop vaccines against laboratory‐challenge hookworm infections using either irradiated third‐state infective larvae (L3) or enzymes from the adult parasites. In an effort to control hookworm infection globally, the Human Hookworm Vaccine Initiative, a product‐development partnership with the Sabin Vaccine Institute to develop new control tools including vaccines, has identified a battery of protein antigens, including surface‐associated antigens (SAAs) from L3. SAA proteins are characterized by a 13 kDa conserved domain of unknown function. SAA proteins are found on the surface of infective L3 stages (and some adult stages) of different nematode parasites, suggesting that they may play important roles in these organisms. The atomic structures and function of SAA proteins remain undetermined and in an effort to remedy this situation recombinant Na‐SAA‐2 from the most prevalent human hookworm parasite Necator americanus has been expressed, purified and crystallized. Useful X‐ray data have been collected to 2.3 Å resolution from a crystal that belonged to the monoclinic space group C 2 with unit‐cell parameters a = 73.88, b = 35.58, c = 42.75 Å, β = 116.1°.