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Articles by Fateme Sefid
Total Records ( 7 ) for Fateme Sefid
  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.
  Faeze Shafi Naderi , Fateme Sefid , Mahsa Khosravi , Fourozan Esmaili Dahaj , Haniye Ashkani , Fateme Sharaf Nahal and Golnaz Kalantari
  Vibrio harveyi is one of the important aquatic pathogens founded predominately in marine habitats. The gram-negative bacterium can cause infection in a broad range of marine vertebrates and invertebrates, involving fishsh, shrimp, lobster and mollusk. Until now, the traditional forms of vaccines against V. harveyi have been produced including killed whole bacterial cells (mostly) and extracellular products (in part). In addition to these vaccines, currently a number of protein-based (in fact recombinant subunit) vaccines have been manufactures and are shown to be effective against some V. harveyi starins.
  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.
  Haniye Eskandari and Fateme Sefid
  Leptospirosis is a widespread zoonosis caused by members of the genus Leptospira. These highly invasive spirochetal pathogens are capable of infecting a broad range of mammalian hosts through either direct contact with an infected animal or indirect contact with soil or water contaminated with urine from a chronically infected animal. In humans, acute leptospirosis accounts for roughly 10% of hospitalizations for acute febrile illness in tropical areas of the world.
  Fateme Sharaf Nahal , Fateme Sefid , Golnaz Kalantari , Faeze Shafi Naderi , Mahsa Khosravi , Fourozan Esmaili Dahaj and Haniye Ashkani
  Actinobacillus pleuropneumoniae is the causative agent of acute and chronic pleuroneumonia that is responsible for substantial morbidity and mortality in the pig industry. New improved vaccines that can protect against all serotypes and prevent colonization are required. Previous studies showed that whole cells of Propionibacterium acnes protected pigs from A. pleuropneumoniae serotype 1 and 5 and therefore the basis for a promising heterologous vaccine. The aim of this study was to identify those protein antigens of P. acnes responsible for protection against A. pleuropneumoniae infection. Antibodies that are induced by recombinant PASsb cross-react with epitopes in the ApxIV and ZnuA proteins of A. pleuropneumoniae. ZnuA is a known A. pleuropneumoniae immunogenic protein and is required for virulence.
  Farnoush Farjam , Mitra Fakhar Khorasgani , Mojtaba Kiany Boroujeni , Hooriyeh Ranjbaran , Tayebeh Abdpoursogh , Navid Farahmandian and Fateme Sefid
  Pseudomonas aeruginosa is an important cause of nosocomial infection and may lead to septicemia and death. P. aeruginosa septicaemia is associated with the highest mortality rate of all gram-negative infections. Because of the general resistance of the organism to antibiotics, research has been focused on immunotherapy. There are several bacterial cell components incorporated into subunit vaccines. Vaccine studies have often focussed on Lipo Poly Saccharide (LPS) and the outer membrane proteins (OPRs) due to its potent stimulation of the immune response. The pathophysiological nature of LPS and its serotype-specific immunological activities has limited LPS using for Pseudomona infection control whereas using major Outer Membrane Proteins of cell walls (mOMPs) of Pseudomonas aeruginosa and other gram-negative bacteria, not only is non-toxic and actively stimulate the immune system but also shows immunological cross-reactivity with mOMPs of other serotypes belonging to same species. Today, the protection of mOMPs in many pathogenic gram-negative bacteria against the corresponding etiologic factors have completely been approved. The major OPRs, OprF, OprL and OprI interested in the potential of OPRs as vaccines. Determination of these tertiary structure and theoretical methods for epitope prediction has been led to synthesis of such peptides that are important for immunodiagnostic tests and vaccines. Bioinformatic tools to better understanding and characterizing the OprF, OprL and Oprl structure of P. aeruginosa was used. For homology modeling, BLAST was run on the sequence in order to find the best template. The template was then served to model the 3D structure. Also, secondary structure of the proteins was predicted. Moreover, topology, signal peptide and B-cell epitopes of proteins were predicted.
  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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