Predicted proteins of Neisseria meningitidis as potential vaccine candidates: from in silico analyses to experimental corroboration

Neisseria meningitidis serogroup B infections are a serious health threat to the world that cannot be prevented by vaccination. Here, we report an analysis of the MC58 Neisseria meningitidis genome aimed at the identification of new potential vaccine candidates. 'Hypothetical' and 'co...

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Main Authors: Darien García, Daniel Yero, Olivia Niebla, Karem Cobas, Yasser Perera, Evelin Caballero, Maite Delgado, Rolando Pajón
Format: Article
Language:English
Published: Elfos Scientiae
Series:Biotecnología Aplicada
Subjects:
Online Access:http://scielo.sld.cu/scielo.php?script=sci_arttext&pid=S1027-28522012000100004&lng=en&tlng=en
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spelling doaj-e46f174a7a4d4aa3bc88554a83b5e7822020-11-25T03:59:21ZengElfos ScientiaeBiotecnología Aplicada1027-28522912228S1027-28522012000100004Predicted proteins of Neisseria meningitidis as potential vaccine candidates: from in silico analyses to experimental corroborationDarien García0Daniel Yero1Olivia Niebla2Karem Cobas3Yasser Perera4Evelin Caballero5Maite Delgado6Rolando Pajón7International Centre for Genetic Engineering and BiotechnologyFinlay InstituteInternational Centre for Genetic Engineering and BiotechnologyInternational Centre for Genetic Engineering and BiotechnologyInternational Centre for Genetic Engineering and BiotechnologyInternational Centre for Genetic Engineering and BiotechnologyInternational Centre for Genetic Engineering and BiotechnologyUniversity of CalgaryNeisseria meningitidis serogroup B infections are a serious health threat to the world that cannot be prevented by vaccination. Here, we report an analysis of the MC58 Neisseria meningitidis genome aimed at the identification of new potential vaccine candidates. 'Hypothetical' and 'conserved hypothetical' annotated genes, together with those with putative functions related to the cell envelope, were subjected to extensive sequence similarity searches, as well as motif, cellular location, and domain analyses complemented with manual curation. As a result, a set of 35 uncharacterized ORFs, predicted to encode for surface exposed or virulence related proteins, was identified. The candidates were subdivided in three categories: 1) predicted outer membrane proteins (OMPs) unique of the Neisseria genus; 2) conserved OMPs from various genus and 3) proteins homologous to known OMPs or to proteins previously found to be immunogenic in animal models. Two of the final candidates, nmb1126 and nmb0181, were cloned and expressed in Escherichia coli. The resulting products were purified by Metal Chelating Chromatography and used to immunize mice. The recombinant proteins were capable of inducing antibodies against the native antigen in preparations of a panel of three strains and displayed bactericidal activity against the homologous strains.http://scielo.sld.cu/scielo.php?script=sci_arttext&pid=S1027-28522012000100004&lng=en&tlng=enneisseriain silico analysesopen reading framesantigenvaccine
collection DOAJ
language English
format Article
sources DOAJ
author Darien García
Daniel Yero
Olivia Niebla
Karem Cobas
Yasser Perera
Evelin Caballero
Maite Delgado
Rolando Pajón
spellingShingle Darien García
Daniel Yero
Olivia Niebla
Karem Cobas
Yasser Perera
Evelin Caballero
Maite Delgado
Rolando Pajón
Predicted proteins of Neisseria meningitidis as potential vaccine candidates: from in silico analyses to experimental corroboration
Biotecnología Aplicada
neisseria
in silico analyses
open reading frames
antigen
vaccine
author_facet Darien García
Daniel Yero
Olivia Niebla
Karem Cobas
Yasser Perera
Evelin Caballero
Maite Delgado
Rolando Pajón
author_sort Darien García
title Predicted proteins of Neisseria meningitidis as potential vaccine candidates: from in silico analyses to experimental corroboration
title_short Predicted proteins of Neisseria meningitidis as potential vaccine candidates: from in silico analyses to experimental corroboration
title_full Predicted proteins of Neisseria meningitidis as potential vaccine candidates: from in silico analyses to experimental corroboration
title_fullStr Predicted proteins of Neisseria meningitidis as potential vaccine candidates: from in silico analyses to experimental corroboration
title_full_unstemmed Predicted proteins of Neisseria meningitidis as potential vaccine candidates: from in silico analyses to experimental corroboration
title_sort predicted proteins of neisseria meningitidis as potential vaccine candidates: from in silico analyses to experimental corroboration
publisher Elfos Scientiae
series Biotecnología Aplicada
issn 1027-2852
description Neisseria meningitidis serogroup B infections are a serious health threat to the world that cannot be prevented by vaccination. Here, we report an analysis of the MC58 Neisseria meningitidis genome aimed at the identification of new potential vaccine candidates. 'Hypothetical' and 'conserved hypothetical' annotated genes, together with those with putative functions related to the cell envelope, were subjected to extensive sequence similarity searches, as well as motif, cellular location, and domain analyses complemented with manual curation. As a result, a set of 35 uncharacterized ORFs, predicted to encode for surface exposed or virulence related proteins, was identified. The candidates were subdivided in three categories: 1) predicted outer membrane proteins (OMPs) unique of the Neisseria genus; 2) conserved OMPs from various genus and 3) proteins homologous to known OMPs or to proteins previously found to be immunogenic in animal models. Two of the final candidates, nmb1126 and nmb0181, were cloned and expressed in Escherichia coli. The resulting products were purified by Metal Chelating Chromatography and used to immunize mice. The recombinant proteins were capable of inducing antibodies against the native antigen in preparations of a panel of three strains and displayed bactericidal activity against the homologous strains.
topic neisseria
in silico analyses
open reading frames
antigen
vaccine
url http://scielo.sld.cu/scielo.php?script=sci_arttext&pid=S1027-28522012000100004&lng=en&tlng=en
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