ArticleClinical and vaccine immunology : CVI2015
Correlation between in vitro complement deposition and passive mouse protection of anti-pneumococcal surface protein A monoclonal antibodies.
Article in Clinical and vaccine immunology : CVI, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 13 citations in OpenAlex.
- Salmonella Typhimurium derived OMV nanoparticle displaying mixed heterologous O-antigens confers immunogenicity and protection against STEC infections in mice.Microbial cell factories · 2025Article
- Diverse Mechanisms of Protective Anti-Pneumococcal Antibodies.Frontiers in cellular and infection microbiology · 2022Review
- A high-throughput, bead-based, antigen-specific assay to assess the ability of antibodies to induce complement activation.Journal of immunological methods · 2019Article
- Antibodies to PcpA and PhtD protect mice against Streptococcus pneumoniae by a macrophage- and complement-dependent mechanism.Human vaccines & immunotherapeutics · 2018Article
- Semisynthetic glycoconjugate vaccine candidate againstProceedings of the National Academy of Sciences of the United States of America · 2017Article
- Role ofFrontiers in microbiology · 2017Review
- Towards Identifying Protective B-Cell Epitopes: The PspA Story.Frontiers in microbiology · 2017Review
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
The shortcomings of the licensed polysaccharide-based pneumococcal vaccine are driving efforts toward development of a protein-based vaccine that is serotype independent and effective in all age groups. An opsonophagocytic killing assay (OPKA) is used to evaluate the antibody response against polysaccharide-based pneumococcal vaccines. However, the OPKA is not reliable for noncapsular antigens. Thus, there is a need to develop an in vitro surrogate for protection for protein vaccine candidates like pneumococcal surface antigen A (PspA). PspA is a serologically variable cell surface virulence factor. Based on its sequence, PspA has been classified into families 1 (clade 1 and 2), 2 (clades 3, 4 and 5), and 3 (clade 6). Here, we report the characterization of 18 IgG anti-PspA monoclonal antibodies (anti-PspA(hkR36A) MAbs) generated from mice immunized with heat-killed strain R36A (clade 2). An enzyme-linked immunosorbent assay (ELISA)-based analysis of the reactivity of the MAbs with recombinant PspAs from the 6 clades indicated that they were family 1 specific. This was confirmed by flow cytometry using a hyperimmune serum generated against PspA from R36A. Eight MAbs that bind at least one clade 1- and clade 2-expressing strain were evaluated for complement deposition, bactericidal activity, and passive protection. The anti-PspA(hkR36A) MAb-dependent deposition of complement on pneumococci showed a positive correlation with passive protection against strain WU2 (r = 0.8783, P = 0.0041). All of our protective MAbs showed bactericidal activity; however, not all MAbs that exhibited bactericidal activity conferred protection in vivo. The protective MAbs described here can be used to identify conserved protection eliciting B cell epitopes for engineering a superior PspA-based vaccine.
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