ArticlePloS one2011
Identification of a highly antigenic linear B cell epitope within Plasmodium vivax apical membrane antigen 1 (AMA-1).
Article in PloS one, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
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Who cites it
33 citing papers in PubMed, 52 citations in OpenAlex.
- Immunodominant B-cell epitopes for precision surveillance ofEmerging microbes & infections · 2026Article
- A rapid immunochromatographic test for antibody detection as a new tool for monitoring malaria caused by Plasmodium vivax.PLoS neglected tropical diseases · 2026Article
- Identifying promising peptide targets for leprosy serological tests: From prediction to ELISA.Journal, genetic engineering & biotechnology · 2025Article
- Immunogenicity ofFrontiers in cellular and infection microbiology · 2025Article
- Natural selection on apical membrane antigen 1 (AMA1) of an emerging zoonotic malaria parasite Plasmodium inui.Scientific reports · 2024Article
- Development and longevity of naturally acquired antibody and memory B cell responses against Plasmodium vivax infection.PLoS neglected tropical diseases · 2024Review
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- Computational Vaccine Design for Poxviridae Family Viruses.Methods in molecular biology (Clifton, N.J.) · 2023Article
- mRNA-Based Vaccine Designing against Epstein-Barr Virus to Induce an Immune Response Using Immunoinformatic and Molecular Modelling Approaches.International journal of environmental research and public health · 2022Article
- In silico designing of a multi-epitope vaccine against Burkholderia pseudomallei: reverse vaccinology and immunoinformatics.Journal, genetic engineering & biotechnology · 2022Article
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- Annotation of Potential Vaccine Targets and Design of a Multi-Epitope Subunit Vaccine againstVaccines · 2021Article
- Genetic diversity in two leading Plasmodium vivax malaria vaccine candidates AMA1 and MSP119 at three sites in India.PLoS neglected tropical diseases · 2021Article
- New highly antigenic linear B cell epitope peptides from PvAMA-1 as potential vaccine candidates.PloS one · 2021Article
- Immunodominant and Neutralizing Linear B-Cell Epitopes Spanning the Spike and Membrane Proteins of Porcine Epidemic Diarrhea Virus.Frontiers in immunology · 2021Article
- Computational tools for modern vaccine development.Human vaccines & immunotherapeutics · 2020Review
- High-density Peptide Arrays Help to Identify Linear Immunogenic B-cell Epitopes in Individuals Naturally Exposed to Malaria Infection.Molecular & cellular proteomics : MCP · 2019Article
- Antibody Responses AgainstFrontiers in immunology · 2019Article
- Temporal genetic changes in Plasmodium vivax apical membrane antigen 1 over 19 years of transmission in southern Mexico.Parasites & vectors · 2017Article
Corrections and comments
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Authors and funding
12 authors at 6 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Apical membrane antigen 1 (AMA-1) is considered to be a major candidate antigen for a malaria vaccine. Previous immunoepidemiological studies of naturally acquired immunity to Plasmodium vivax AMA-1 (PvAMA-1) have shown a higher prevalence of specific antibodies to domain II (DII) of AMA-1. In the present study, we confirmed that specific antibody responses from naturally infected individuals were highly reactive to both full-length AMA-1 and DII. Also, we demonstrated a strong association between AMA-1 and DII IgG and IgG subclass responses. We analyzed the primary sequence of PvAMA-1 for B cell linear epitopes co-occurring with intrinsically unstructured/disordered regions (IURs). The B cell epitope comprising the amino acid sequence 290-307 of PvAMA-1 (SASDQPTQYEEEMTDYQK), with the highest prediction scores, was identified in domain II and further selected for chemical synthesis and immunological testing. The antigenicity of the synthetic peptide was identified by serological analysis using sera from P. vivax-infected individuals who were knowingly reactive to the PvAMA-1 ectodomain only, domain II only, or reactive to both antigens. Although the synthetic peptide was recognized by all serum samples specific to domain II, serum with reactivity only to the full-length protein presented 58.3% positivity. Moreover, IgG reactivity against PvAMA-1 and domain II after depletion of specific synthetic peptide antibodies was reduced by 18% and 33% (P = 0.0001 for both), respectively. These results suggest that the linear epitope SASDQPTQYEEEMTDYQK is highly antigenic during natural human infections and is an important antigenic region of the domain II of PvAMA-1, suggesting its possible future use in pre-clinical studies.
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