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Articles by Hamed Karamizade
Total Records ( 3 ) for Hamed Karamizade
  Bahare Baharie , Fateme Sefid , Reihane Ragheb , Vahide Saeidjavan , Hamed Karamizade , Sepide Akhgari and Nazgol Emamian
  Acinetobacter baumannii 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 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 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 10–18 M which is far less than what is needed for the survival of the invading bacterial pathogen. To survive in such conditions, Acinetobacter baumannii 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.
  Hamed Karamizade , Fateme Sefid , Nazgol Emamian , Vahide Saeidjavan and Sepide Akhgari
  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.
  Nazgol Emamian , Fateme Sefid , Vahide Saeidjavan , Sepide Akhgari and Hamed Karamizade
  Haemophilus parasuis is a gram-negative bacterium belonging to the Pasteurellaceae family. This organism is an important respiratory-tract pathogen in swine and the etiological agent of porcine polyserositis, meningitis and arthritis syndrome known as Glasser’s disease. Among the 15 known serovars, serotype 5 shows high virulence and is one of the most prevalent serotypes. Attempts to control the H. parasuis infection are hindered by a lack of thorough knowledge of the virulence factors and protective antigens of the bacterium, the existence of diverse genetic make-ups and the evolution of multidrug-resistant strains. Initial studies about the immune response developed against H. parasuis have detected antibodies to Outer Membrane Proteins (OMPs) but not against lipopolysaccharide or capsule, suggesting that the OMPs are more immunogenic than other components of bacteria. In recent years, interest has shifted toward protein based vaccines. It has been shown that recombinant vaccines based on OMPs provided partial protection against challenge with H. parasuis.
 
 
 
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