Journal of Engineering and Applied Sciences
ISSN: Online 1818-7803ISSN: Print 1816-949x
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Abstract
Iron is essential for the growth of most bacteria but in nature the element is highly insoluble in an aerobic environment and therefore unavailable to most organisms. Inside the human body, most iron is in the cell in the form of hemoglobin or other iron-containing proteins or is stored as ferritin. Trace amounts of iron are found outside the cell complexed to high-affinity iron-binding proteins such as lactoferrin or transferrin. Inside the human body, most iron is in the cell in the form of hemoglobin or other iron-containing proteins or is stored as ferritin. Vibrio cholera, the intestinal pathogen that causes the disease cholera can acquire iron in two ways. Under low-iron conditions, the organism synthesizes and secretes the siderophore vibriobactin which binds ferric iron. To survive in such conditions, Vibrio cholera expresses HutA in its outer membrane. Evidence suggests that HutA is a useful antigen for inclusion in an effective vaccine hence, the identification of its structure and functionally and structurally important residues is very important.
How to cite this article:
Hamed Karamizade, Fateme Sefid, Nazgol Emamian, Vahide Saeidjavan and Sepide Akhgari. Identification of Functionally and Structurally Important Residues of HutA Protein in Vibrio cholera.
DOI: https://doi.org/10.36478/jeasci.2017.1152.1158
URL: https://www.makhillpublications.co/view-article/1816-949x/jeasci.2017.1152.1158