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@ARTICLE{Capelli:859645,
      author       = {Capelli, Riccardo and Peri, Claudio and Villa, Riccardo and
                      Nithichanon, Arnone and Conchillo-Solé, Oscar and Yero,
                      Daniel and Gagni, Paola and Chiari, Marcella and
                      Lertmemongkolchai, Ganjana and Cretich, Marina and Daura,
                      Xavier and Bolognesi, Martino and Colombo, Giorgio and
                      Gourlay, Louise J.},
      title        = {{BPSL}1626: {R}everse and {S}tructural {V}accinology
                      {R}eveal a {N}ovel {C}andidate for {V}accine {D}esign
                      {A}gainst {B}urkholderia pseudomallei},
      journal      = {Antibodies},
      volume       = {7},
      number       = {3},
      issn         = {2073-4468},
      address      = {Basel},
      publisher    = {MDPI},
      reportid     = {FZJ-2019-00493},
      pages        = {26 -},
      year         = {2018},
      abstract     = {Due to significant advances in computational biology,
                      protein prediction, together with antigen and epitope
                      design, have rapidly moved from conventional methods, based
                      on experimental approaches, to in silico-based
                      bioinformatics methods. In this context, we report a reverse
                      vaccinology study that identified a panel of 104 candidate
                      antigens from the Gram-negative bacterial pathogen
                      Burkholderia pseudomallei, which is responsible for the
                      disease melioidosis. B. pseudomallei can cause fatal sepsis
                      in endemic populations in the tropical regions of the world
                      and treatment with antibiotics is mostly ineffective. With
                      the aim of identifying potential vaccine candidates, we
                      report the experimental validation of predicted antigen and
                      type I fimbrial subunit, BPSL1626, which we show is able to
                      recognize and bind human antibodies from the sera of
                      Burkholderia infected patients and to stimulate
                      T-lymphocytes in vitro. The prerequisite for a melioidosis
                      vaccine, in fact, is that both antibody- and cell-mediated
                      immune responses must be triggered. In order to reveal
                      potential antigenic regions of the protein that may aid
                      immunogen re-design, we also report the crystal structure of
                      BPSL1626 at 1.9 Å resolution on which structure-based
                      epitope predictions were based. Overall, our data suggest
                      that BPSL1626 and three epitope regions here-identified can
                      represent viable candidates as potential antigenic
                      molecules.},
      cin          = {IAS-5},
      ddc          = {540},
      cid          = {I:(DE-Juel1)IAS-5-20120330},
      pnm          = {899 - ohne Topic (POF3-899)},
      pid          = {G:(DE-HGF)POF3-899},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000448330700006},
      doi          = {10.3390/antib7030026},
      url          = {https://juser.fz-juelich.de/record/859645},
}