caa a22 4500 605497486 CHVBK 20210128100541.0 cr unu---uuuuu 210128e20150601xx s 000 0 eng 10.1007/s10441-015-9251-2 doi (NATIONALLICENCE)springer-10.1007/s10441-015-9251-2 Functional Exposed Amino Acids of BauA as Potential Immunogen Against Acinetobacter baumannii [Elektronische Daten] [Fatemeh Sefid, Iraj Rasooli, Abolfazl Jahangiri, Hadise Bazmara] Multidrug-resistant Acinetobacter baumannii 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 under such conditions, bacteria express new proteins on their outer membrane and also secrete iron chelators called siderophores. Antibodies directed against these proteins associated with iron uptake exert a bacteriostatic or bactericidal effect against A. baumanii in vitro, by blocking siderophore mediated iron uptake pathways. Attempts should be made to discover peptides that could mimic protein epitopes and possess the same immunogenicity as the whole protein. Subsequently, theoretical methods for epitope prediction have been developed leading to synthesis of such peptides that are important for development of immunodiagnostic tests and vaccines. The present study was designed to in silico resolving the major obstacles in the control or in prevention of the diseases caused by A. baumannii. We exploited bioinformatic tools to better understand and characterize the Baumannii acinetobactin utilization structure of A. baumannii and select appropriate regions as effective B cell epitopes. In conclusion, amino acids 26-191 of cork domain and 321-635 of part of the barrel domain including L4-L9, were selected as vaccine candidates. These two regions contain functional exposed amino acids with higher score of B cell epitopes properties. Majority of amino acids are hydrophilic, flexible, accessible, and favorable for B cells from secondary structure point of view. Springer Science+Business Media Dordrecht, 2015 Acinetobacter baumannii nationallicence BauA nationallicence Iron uptake protein nationallicence B cell epitope prediction nationallicence Sefid Fatemeh Department of Biology, Shahed University, Tehran-Qom Express Way, Opposite Imam Khomeini's Shrine, 3319118651, Tehran, Iran aut Rasooli Iraj Department of Biology, Shahed University, Tehran-Qom Express Way, Opposite Imam Khomeini's Shrine, 3319118651, Tehran, Iran aut Jahangiri Abolfazl Department of Biology, Shahed University, Tehran-Qom Express Way, Opposite Imam Khomeini's Shrine, 3319118651, Tehran, Iran aut Bazmara Hadise Department of Biology, Shahed University, Tehran-Qom Express Way, Opposite Imam Khomeini's Shrine, 3319118651, Tehran, Iran aut Acta Biotheoretica Springer Netherlands 63/2(2015-06-01), 129-149 0001-5342 63:2<129 2015 63 10441 https://doi.org/10.1007/s10441-015-9251-2 text/html Onlinezugriff via DOI BK010053 XK010053 XK010000 Metadata rights reserved Springer special CC-BY-NC licence nationallicence 1 research-article jats NATIONALLICENCE NATIONALLICENCE NL-springer NATIONALLICENCE 856 40 https://doi.org/10.1007/s10441-015-9251-2 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Sefid Fatemeh Department of Biology, Shahed University, Tehran-Qom Express Way, Opposite Imam Khomeini's Shrine, 3319118651, Tehran, Iran aut NATIONALLICENCE 700 1- Rasooli Iraj Department of Biology, Shahed University, Tehran-Qom Express Way, Opposite Imam Khomeini's Shrine, 3319118651, Tehran, Iran aut NATIONALLICENCE 700 1- Jahangiri Abolfazl Department of Biology, Shahed University, Tehran-Qom Express Way, Opposite Imam Khomeini's Shrine, 3319118651, Tehran, Iran aut NATIONALLICENCE 700 1- Bazmara Hadise Department of Biology, Shahed University, Tehran-Qom Express Way, Opposite Imam Khomeini's Shrine, 3319118651, Tehran, Iran aut NATIONALLICENCE 773 0- Acta Biotheoretica Springer Netherlands 63/2(2015-06-01), 129-149 0001-5342 63:2<129 2015 63 10441