TY  - JOUR
T1  - In Silico Determination and Validation of FhuE Structure and Ligand Binding Site as a Vaccine Candidate in <i>Acinetobacter Baumannii</i>
AU - Sefid, Fateme AU - Baharie, Bahare AU - Ragheb, Reihane AU - Saeidjavan, Vahide AU - Karamizade, Hamed AU - Akhgari, Sepide AU - Emamian, Nazgol 
JO  - Journal of Engineering and Applied Sciences
VL  - 12
IS  - 5
SP  - 1140
EP  - 1146
PY  - 2017
DA  - 2001/08/19
SN  - 1816-949x
DO  - jeasci.2017.1140.1146
UR  - https://makhillpublications.co/view-article.php?doi=jeasci.2017.1140.1146
KW  - Acinetobacter baumannii
KW  -fhuE
KW  -3D structure
KW  -uptake protein
KW  -bacteriostatic
AB  - <i>Acinetobacter baumannii</i> is a gram-negative bacterium that causes serious infections in compromised patients. This pathogen grows under a wide range of conditions including iron-limiting conditions. Multidrug resistant <i>Acinetobacter baumannii</i> is recognized to be among the most difficult antimicrobial-resistant gram negative bacilli to control and treat. One of the major challenges that the pathogenic bacteria face in their host is the scarcity of freely available iron. To survive in such conditions, bacteria express new proteins in their outer membrane and also secrete iron chelators called siderophores. In the case of human hosts, the free iron availability is 10<sup>&#150;18</sup> M which is far less than what is needed for the survival of the invading bacterial pathogen. To survive in such conditions, <i>Acinetobacter baumannii</i> expresses fhue in its outer membrane. Evidence suggests that fhue iron uptake protein is a useful antigen for inclusion in an effective vaccine, hence the identification of its structure is very important.
ER  -