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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},
}