ArticleInfection and immunity2003
Functional activity of antibodies against the recombinant OpaJ protein from Neisseria meningitidis.
Article in Infection and immunity, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 23 citations in OpenAlex.
- Single Domain Antibodies Targeting Receptor Binding Pockets of NadA Restrain Adhesion ofFrontiers in molecular biosciences · 2020Article
- Saponins fromMolecules (Basel, Switzerland) · 2019Review
- Defining the Ail Ligand-Binding Surface: Hydrophobic Residues in Two Extracellular Loops Mediate Cell and Extracellular Matrix Binding To Facilitate Yop Delivery.Infection and immunity · 2017Article
- A versatile assay to determine bacterial and host factors contributing to opsonophagocytotic killing in hirudin-anticoagulated whole blood.Scientific reports · 2017Article
- Neisserial Opa Protein-CEACAM Interactions: Competition for Receptors as a Means of Bacterial Invasion and Pathogenesis.Biochemistry · 2016Article
- Structure of the Neisserial outer membrane protein Opa₆₀: loop flexibility essential to receptor recognition and bacterial engulfment.Journal of the American Chemical Society · 2014Article
- Domain exchange at the 3' end of the gene encoding the fratricide meningococcal two-partner secretion protein A.BMC genomics · 2013Article
- Construction of Opa-positive and Opa-negative strains of Neisseria meningitidis to evaluate a novel meningococcal vaccine.PloS one · 2012Article
- Functional characterization of antibodies against Neisseria gonorrhoeae opacity protein loops.PloS one · 2009Article
- Pathogenic neisseriae: surface modulation, pathogenesis and infection control.Nature reviews. Microbiology · 2009Review
- The effect of immune selection on the structure of the meningococcal opa protein repertoire.PLoS pathogens · 2008Article
- Meningococcal vaccines.Paediatric drugs · 2004Review
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Authors and funding
7 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The opacity proteins belong to the major outer membrane proteins of the pathogenic Neisseria and are involved in adhesion and invasion. We studied the functional activity of antibodies raised against the OpaJ protein from strain H44/76. Recombinant OpaJ protein was obtained from Escherichia coli in two different ways: cytoplasmic expression in the form of inclusion bodies followed by purification and refolding and cell surface expression followed by isolation of outer membrane complexes (OMCs). Immunization with purified protein and Quillaja saponin A (QuilA) induced high levels of Opa-specific antibodies, whereas the E. coli OMC preparations generally induced lower levels of antibodies. Two chimeric Opa proteins, hybrids between OpaB and OpaJ, were generated to demonstrate that the hypervariable region 2 is immunodominant. Denatured OpaJ with QuilA induced high levels of immunoglobulin G2a (IgG2a) in addition to IgG1, whereas refolded OpaJ with QuilA induced IgG1 exclusively. These sera did not induce significant complement-mediated killing. However, all sera blocked the interaction of OpaJ-expressing bacteria to CEACAM1-transfected cells. In addition, cross-reactive blocking of OpaB-expressing bacteria to both CEACAM1- and CEA-transfected cells was found for all sera. Sera raised against purified OpaJ and against OpaJ-containing meningococcal OMCs also blocked the nonopsonic interaction of Opa-expressing meningococci with human polymorphonuclear leukocytes.
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