BPSL1626 : reverse and structural vaccinology reveal a novel candidate for vaccine design against Burkholderia pseudomallei

Autor: Oscar Conchillo-Solé, Marina Cretich, Martino Bolognesi, Arnone Nithichanon, Claudio Peri, Louise J. Gourlay, Riccardo Capelli, Daniel Yero, Marcella Chiari, Giorgio Colombo, Ganjana Lertmemongkolchai, Xavier Daura, Paola Gagni, Riccardo Villa
Rok vydání: 2021
Předmět:
Zdroj: Recercat: Dipósit de la Recerca de Catalunya
Varias* (Consorci de Biblioteques Universitáries de Catalunya, Centre de Serveis Científics i Acadèmics de Catalunya)
Recercat. Dipósit de la Recerca de Catalunya
instname
Antibodies
Volume 7
Issue 3
Antibodies, Vol 7, Iss 3, p 26 (2018)
'Antibodies ', vol: 7, pages: 26-1-26-14 (2018)
Antibodies 7(3), 26-(2018). doi:10.3390/antib7030026
Dipòsit Digital de Documents de la UAB
Universitat Autònoma de Barcelona
ISSN: 2073-4468
DOI: 10.3390/antib7030026
Popis: 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.
Databáze: OpenAIRE