ArticleClinical and diagnostic laboratory immunology2003
Mimotopes of the Vi antigen of Salmonella enterica serovar typhi identified from phage display peptide library.
Article in Clinical and diagnostic laboratory immunology, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 27 citations in OpenAlex.
- Factors Influencing the Behavioural Intention to Use Cryptocurrency in Emerging Economies During the COVID-19 Pandemic: Based on Technology Acceptance Model 3, Perceived Risk, and Financial Literacy.Frontiers in psychology · 2021Article
- Chimeric epitope vaccine against Leptospira interrogans infection and induced specific immunity in guinea pigs.BMC microbiology · 2016Article
- Phage display creates innovative applications to combat hepatitis B virus.World journal of gastroenterology · 2014Review
- Profiling the IgOme: meeting the challenge.FEBS letters · 2014Review
- Identification of mimotopes with diagnostic potential for Trypanosoma brucei gambiense variant surface glycoproteins using human antibody fractions.PLoS neglected tropical diseases · 2012Article
- Identification of peptide mimotopes of Trypanosoma brucei gambiense variant surface glycoproteins.PLoS neglected tropical diseases · 2011Article
- Identification and characterization of peptide mimics of blood group A antigen.Journal of Huazhong University of Science and Technology. Medical sciences = Hua zhong ke ji da xue xue bao. Yi xue Ying De wen ban = Huazhong keji daxue xuebao. Yixue Yingdewen ban · 2008Article
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Authors and funding
6 authors at 4 institutions in 4 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The capsular polysaccharide Vi antigen (ViCPS) is an essential virulence factor and also a protective antigen of Salmonella enterica serovar Typhi. A random 12-mer phage-displayed peptide library was used to identify mimotopes (epitope analogues) of this antigen by panning against a ViCPS-specific monoclonal antibody (MAb) ATVi. Approximately 75% of the phage clones selected in the fourth round carried the peptide sequence TSHHDSHGLHRV, and the rest of the clones harbored ENHSPVNIAHKL and other related sequences. These two sequences were also obtained in a similar panning process by using pooled sera from patients with a confirmed diagnosis of typhoid fever, suggesting they mimic immunodominant epitopes of ViCPS antigens. Binding of MAb ATVi to the mimotopes was specifically blocked by ViCPS, indicating that they interact with the same binding site (paratope) of the MAb. Data and reagents generated in this study have important implications for the development of peptide-base diagnostic tests and peptide vaccines and may also provide a better understanding of the pathogenesis of typhoid fever.
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