5N2B

The crystal structure of Burkholderia pseudomallei antigen and type I fimbria protein BPSL1626.

Summary for 5N2B

• Entry DOI: 10.2210/pdb5n2b/pdb
• Descriptor: Putative fimbrial subunit type 1, 1,2-ETHANEDIOL (3 entities in total)
• Functional Keywords: melioidosis, antigen, fimbrial subunit, incomplete immunoglobulin-like fold, immune system
• Biological source: Burkholderia pseudomallei
• Total number of polymer chains: 2
• Total formula weight: 37877.67

Authors

Gourlay, L.J.,Bolognesi, M. (deposition date: 2017-02-07, release date: 2018-01-17, Last modification date: 2024-05-08)

Primary citation

Capelli, R.,Peri, C.,Villa, R.,Nithichanon, A.,Conchillo-Sole, O.,Yero, D.,Gagni, P.,Chiari, M.,Lertmemongkolchai, G.,Cretich, M.,Daura, X.,Bolognesi, M.,Colombo, G.,Gourlay, L.J.
BPSL1626: Reverse and Structural Vaccinology Reveal a Novel Candidate for Vaccine Design againstBurkholderia pseudomallei.
Antibodies, 7:-, 2018

PubMed 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 , which is responsible for the disease melioidosis. 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 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: 31544878
DOI: 10.3390/antib7030026

Experimental method

X-RAY DIFFRACTION (1.9 Å)