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Towards the Immunoproteome of Neisseria meningitidis
by
Mendum, Tom A.
, McFadden, Johnjoe
, Newcombe, Jane
, McNeilly, Celia L.
in
Animals
/ Antigens
/ Antigens, Bacterial - chemistry
/ Cell surface
/ Cytometry
/ Cytoplasm - metabolism
/ E coli
/ Epidemics
/ Escherichia coli
/ Female
/ Flow cytometry
/ Gels
/ Health aspects
/ Humans
/ Identification
/ Immune System
/ Immunity
/ Immunoglobulin G
/ Immunoglobulin G - chemistry
/ Immunology
/ Immunology/Immune Response
/ Mass spectrometry
/ Mass Spectrometry - methods
/ Mass spectroscopy
/ Meningitis
/ Meningitis, Meningococcal - immunology
/ Metabolism
/ Mice
/ Microbiology/Immunity to Infections
/ Microbiology/Medical Microbiology
/ Neisseria meningitidis
/ Neisseria meningitidis - immunology
/ Neisseria meningitidis - metabolism
/ Patients
/ Physiological aspects
/ Polyamines
/ Polysaccharides
/ Proteins
/ Proteome
/ Proteomics
/ Proteomics - methods
/ Recombinant proteins
/ Recombinant Proteins - chemistry
/ Scientific imaging
/ Sepsis - immunology
/ Streptococcus infections
/ Vaccines
/ Western blotting
2009
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Towards the Immunoproteome of Neisseria meningitidis
by
Mendum, Tom A.
, McFadden, Johnjoe
, Newcombe, Jane
, McNeilly, Celia L.
in
Animals
/ Antigens
/ Antigens, Bacterial - chemistry
/ Cell surface
/ Cytometry
/ Cytoplasm - metabolism
/ E coli
/ Epidemics
/ Escherichia coli
/ Female
/ Flow cytometry
/ Gels
/ Health aspects
/ Humans
/ Identification
/ Immune System
/ Immunity
/ Immunoglobulin G
/ Immunoglobulin G - chemistry
/ Immunology
/ Immunology/Immune Response
/ Mass spectrometry
/ Mass Spectrometry - methods
/ Mass spectroscopy
/ Meningitis
/ Meningitis, Meningococcal - immunology
/ Metabolism
/ Mice
/ Microbiology/Immunity to Infections
/ Microbiology/Medical Microbiology
/ Neisseria meningitidis
/ Neisseria meningitidis - immunology
/ Neisseria meningitidis - metabolism
/ Patients
/ Physiological aspects
/ Polyamines
/ Polysaccharides
/ Proteins
/ Proteome
/ Proteomics
/ Proteomics - methods
/ Recombinant proteins
/ Recombinant Proteins - chemistry
/ Scientific imaging
/ Sepsis - immunology
/ Streptococcus infections
/ Vaccines
/ Western blotting
2009
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Towards the Immunoproteome of Neisseria meningitidis
by
Mendum, Tom A.
, McFadden, Johnjoe
, Newcombe, Jane
, McNeilly, Celia L.
in
Animals
/ Antigens
/ Antigens, Bacterial - chemistry
/ Cell surface
/ Cytometry
/ Cytoplasm - metabolism
/ E coli
/ Epidemics
/ Escherichia coli
/ Female
/ Flow cytometry
/ Gels
/ Health aspects
/ Humans
/ Identification
/ Immune System
/ Immunity
/ Immunoglobulin G
/ Immunoglobulin G - chemistry
/ Immunology
/ Immunology/Immune Response
/ Mass spectrometry
/ Mass Spectrometry - methods
/ Mass spectroscopy
/ Meningitis
/ Meningitis, Meningococcal - immunology
/ Metabolism
/ Mice
/ Microbiology/Immunity to Infections
/ Microbiology/Medical Microbiology
/ Neisseria meningitidis
/ Neisseria meningitidis - immunology
/ Neisseria meningitidis - metabolism
/ Patients
/ Physiological aspects
/ Polyamines
/ Polysaccharides
/ Proteins
/ Proteome
/ Proteomics
/ Proteomics - methods
/ Recombinant proteins
/ Recombinant Proteins - chemistry
/ Scientific imaging
/ Sepsis - immunology
/ Streptococcus infections
/ Vaccines
/ Western blotting
2009
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Journal Article
Towards the Immunoproteome of Neisseria meningitidis
2009
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Overview
Despite the introduction of conjugated polysaccharide vaccines for many of the Neisseria meningitidis serogroups, neisserial infections continue to cause septicaemia and meningitis across the world. This is in part due to the difficulties in developing a, cross-protective vaccine that is effective against all serogroups, including serogroup B meningococci. Although convalescent N. meningitidis patients develop a natural long-lasting cross-protective immunity, the antigens that mediate this response remain unknown. To help define the target of this protective immunity we identified the proteins recognized by IgG in sera from meningococcal patients by a combination of 2D protein gels, western blots and mass spectrometry. Although a number of outer membrane antigens were identified the majority of the antigens were cytoplasmic, with roles in cellular processes and metabolism. When recombinant proteins were expressed and used to raise sera in mice, none of the antigens elicited a positive SBA result, however flow cytometry did demonstrate that some, including the ribosomal protein, RplY were localised to the neisserial cell surface.
Publisher
Public Library of Science,Public Library of Science (PLoS)
Subject
/ Antigens
/ Antigens, Bacterial - chemistry
/ E coli
/ Female
/ Gels
/ Humans
/ Immunity
/ Immunoglobulin G - chemistry
/ Meningitis, Meningococcal - immunology
/ Mice
/ Microbiology/Immunity to Infections
/ Microbiology/Medical Microbiology
/ Neisseria meningitidis - immunology
/ Neisseria meningitidis - metabolism
/ Patients
/ Proteins
/ Proteome
/ Recombinant Proteins - chemistry
/ Vaccines
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