ArticleVaccine2018
The diversity of the proline-rich domain of pneumococcal surface protein A (PspA): Potential relevance to a broad-spectrum vaccine.
Article in Vaccine, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 33 citations in OpenAlex.
- Development and Validation of a Functional Antibody Assay for Evaluating Protein-Based Pneumococcal Vaccines.Vaccines · 2026Article
- In silico design and characterization of a novel multi-epitope mRNA vaccine candidate against Streptococcus pneumoniae.Scientific reports · 2025Article
- Safety and efficacy of an intramuscular bivalent vaccine against influenza and Streptococcus pneumoniae infections in mice.Medical microbiology and immunology · 2025Article
- Article
- Emerging vaccine strategies against the incessant pneumococcal disease.NPJ vaccines · 2023Review
- Immunoinformatics-aided design of a new multi-epitope vaccine adjuvanted with domain 4 of pneumolysin against Streptococcus pneumoniae strains.BMC bioinformatics · 2023Article
- In-silico design and evaluation of an epitope-based serotype-independent promising vaccine candidate for highly cross-reactive regions of pneumococcal surface protein A.Journal of translational medicine · 2023Article
- Recent progress in pneumococcal protein vaccines.Frontiers in immunology · 2023Review
- A new candidate epitope-based vaccine against PspA PhtD ofFrontiers in cellular and infection microbiology · 2023Article
- Maternal immunization with pneumococcal surface protein A provides the immune memories of offspring against pneumococcal infection.Frontiers in cellular and infection microbiology · 2023Article
- Development of a bivalent protein-based vaccine candidate against invasive pneumococcal diseases based on novel pneumococcal surface protein A in combination with pneumococcal histidine triad protein D.Frontiers in immunology · 2023Article
- A Jack of All Trades: The Role of Pneumococcal Surface Protein A in the Pathogenesis ofFrontiers in cellular and infection microbiology · 2022Review
- Pneumococcal Surface Proteins as Virulence Factors, Immunogens, and Conserved Vaccine Targets.Frontiers in cellular and infection microbiology · 2022Review
- Streptococcus pneumoniae Binds to Host Lactate Dehydrogenase via PspA and PspC To Enhance Virulence.mBio · 2021Article
- Molecular analyses identifies new domains and structural differences among Streptococcus pneumoniae immune evasion proteins PspC and Hic.Scientific reports · 2021Article
- PspA Diversity, Serotype Distribution and Antimicrobial Resistance of Invasive Pneumococcal Isolates from Paediatric Patients in Shenzhen, China.Infection and drug resistance · 2021Article
- Article
- An in vivo atlas of host-pathogen transcriptomes duringProceedings of the National Academy of Sciences of the United States of America · 2020Article
- Development of Next GenerationVaccines · 2020Review
- Insights From Analysis of Human Antigen-Specific Memory B Cell Repertoires.Frontiers in immunology · 2018Review
Corrections and comments
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Authors and funding
8 authors at 3 institutions in 1 country.
Funding
Abstract
Pneumococcal surface protein A (PspA) is a surface exposed, highly immunogenic protein of Streptococcus pneumoniae. Its N-terminal α-helical domain (αHD) elicits protective antibody in humans and animals that can protect mice from fatal infections with pneumococci and can be detected in vitro with opsonophagocytosis assays. The proline-rich domain (PRD) in the center of the PspA sequence can also elicit protection. This study revealed that although the sequence of PRD was diverse, PRD from different pneumococcal isolates contained many shared elements. The inferred amino acid sequences of 123 such PRDs, which were analyzed by assembly and alignment-free (AAF) approaches, formed three PRD groups. Of these sequences, 45 were classified as Group 1, 19 were classified as Group 2, and 59 were classified as Group 3. All Group 3 sequences contained a highly conserved 22-amino acid non-proline block (NPB). A significant polymorphism was observed, however, at a single amino acid position within NPB. Each of the three PRD groups had characteristic patterns of short amino acid repeats, with most of the repeats being found in more than one PRD group. One of these repeats, PKPEQP as well as the NPB were previously shown to elicit protective antibodies in mice. In this study, we found that sera from 12 healthy human adult volunteers contained antibodies to all three PRD groups. This suggested that a PspA-containing vaccine containing carefully selected PRDs and αHDs could redundantly cover the known diversity of PspA. Such an approach might reduce the chances of PspA variants escaping a PspA vaccine's immunity.
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