ArticleMonoclonal antibodies in immunodiagnosis and immunotherapy2014
Generation and characterization of a monoclonal antibody against prM protein of West Nile virus.
Article in Monoclonal antibodies in immunodiagnosis and immunotherapy, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
3 citing papers in PubMed, 5 citations in OpenAlex.
- Adenoviral Vectors Expressing Optimized preM/E Genes of WNV Deliver Long-Term Protection Against Lethal West Nile Virus Challenge.Vaccines · 2025Article
- West Nile virus infectious replicon particles generated using a packaging-restricted cell line is a safe reporter system.Scientific reports · 2017Article
- Newcastle disease virus-vectored West Nile fever vaccine is immunogenic in mammals and poultry.Virology journal · 2016Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
West Nile virus (WNV), which is an emerging pathogenic flavivirus with increasing distribution worldwide, is the cause of major human and animal health concerns. The pre-membrane (prM) protein of WNV is cleaved during maturation by the furin protease into the structural protein M and a pr-segment. In this study we generated and characterized a monoclonal antibody (MAb) against the WNV prM protein. Western blot analysis showed that the MAb reacted with WNV prM specifically. Immunohistochemistry assays demonstrated that the MAb recognized native prM protein in transfected BHK-21 cells. Preliminary studies were performed to identify the epitope recognized by the MAb using a set of synthesized overlapping peptides spanning the whole length of the prM protein. The MAb reported here may provide a valuable tool for the further exploration of the biological properties and functions of the prM protein and may also be developed for potential clinical applications.
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