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BPSL1626: Reverse and Structural Vaccinology Reveal a Novel Candidate for Vaccine Design against Burkholderia pseudomallei.

Riccardo Capelli | Claudio Peri | Riccardo Villa | Arnone Nithichanon | Oscar Conchillo-Solé | Daniel Yero | Paola Gagni | Marcella Chiari | Ganjana Lertmemongkolchai | Marina Cretich | Xavier Daura | Martino Bolognesi | Giorgio Colombo | Louise J Gourlay
Antibodies (Basel, Switzerland) | 2018

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.

Pubmed ID: 31544878

Research resources used in this publication

None found

Additional research tools detected in this publication

Antibodies used in this publication

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Associated grants

  • Agency: Fondazione Cariplo,
    Id: 2009-3577
  • Agency: Ministero dell'Istruzione, dell'Università e della Ricerca,
    Id: 2015JTL4HL
  • Agency: Horizon 2020,
    Id: 785907
  • Agency: Regione Lombardia,
    Id: 229472

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This is a list of tools and resources that we have found mentioned in this publication.


ProFunc (tool)

RRID:SCR_004450

The ProFunc server had been developed to help identify the likely biochemical function of a protein from its three-dimensional structure. It uses both sequence- and structure-based methods including fold matching, residue conservation, surface cleft analysis, and functional 3D templates, to identify both the protein''''s likely active site and possible homologues in the PDB. Often, where one method fails to provide any functional insight another may be more helpful. You can submit your own structure, analyze an existing PDB entry, or retrieve the results of a previously submitted run. The files are usually stored for about 6 months before being deleted. However, they are stored on a partition that is not backed up; so, in principle, they could disappear at any time.

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