Abstract
Giardiasis is the most prevalent diarrheal disease globally and affects humans and animals. It is a significant problem in developing countries, the number one cause of travelers' diarrhea and affects children and immunocompromised individuals, especially HIV-infected individuals. Giardiasis is treated with antibiotics (tinidazole and metronidazole) that are also used for other infections such as trichomoniasis. The ongoing search for new therapeutics for giardiasis includes characterizing the structure and function of proteins from the causative protozoan Giardia lamblia. These proteins include hypothetical proteins that share 30% sequence identity or less with proteins of known structure. Here, the atomic resolution structure of a 15.6 kDa protein was determined by molecular replacement. The structure has the two-layer αβ-sandwich topology observed in the prototypical endoribonucleases L-PSPs (liver perchloric acid-soluble proteins) with conserved allosteric active sites containing small molecules from the crystallization solution. This article is an educational collaboration between Hampton University and the Seattle Structural Genomics Center for Infectious Disease.
Highlights
The flagellated protozoa Giardia lamblia is the most commonly identified intestinal parasite globally, causing giardiasis, otherwise known as travelers’ diarrhea (Daniels et al, 2015; Escobedo et al, 2015)
Characterizing the structures and functions of G. lamblia proteins is the first step towards identifying new therapeutics for giardiasis
The PCR product was cloned into expression vector pAVA0421 (Choi et al, 2011) by ligation-independent cloning (LIC; Aslanidis & de Jong, 1990)
Summary
The flagellated protozoa Giardia lamblia is the most commonly identified intestinal parasite globally, causing giardiasis, otherwise known as travelers’ diarrhea (Daniels et al, 2015; Escobedo et al, 2015). Giardia is an endemic neglected tropical disease, and outbreaks of giardiasis from contaminated water or food sources are common in developing countries because of poor sanitation (McIntyre et al, 2014). One of these hypothetical proteins is a 141-amino-acid protein (UniProt ID A8BD71, XP_001707732.1). We present the atomic resolution crystal structure of this hypothetical protein as a first step towards clarifying its possible functions
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