ArticleInternational journal of molecular sciences2014
Mass spectrometry analysis coupled with de novo sequencing reveals amino acid substitutions in nucleocapsid protein from influenza A virus.
Article in International journal of molecular sciences, 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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3 citing papers in PubMed, 8 citations in OpenAlex.
- Mass spectrometry-based proteomics in basic and translational research of SARS-CoV-2 coronavirus and its emerging mutants.Clinical proteomics · 2021Review
- Extraction and purification of the H9N2 virus nucleoprotein: A simple and practical method.Medical journal of the Islamic Republic of Iran · 2018Article
- Rapid and generic identification of influenza A and other respiratory viruses with mass spectrometry.Journal of virological methods · 2015Article
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Authors and funding
6 authors at 3 institutions in 2 countries.
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Abstract
Amino acid substitutions in influenza A virus are the main reasons for both antigenic shift and virulence change, which result from non-synonymous mutations in the viral genome. Nucleocapsid protein (NP), one of the major structural proteins of influenza virus, is responsible for regulation of viral RNA synthesis and replication. In this report we used LC-MS/MS to analyze tryptic digestion of nucleocapsid protein of influenza virus (A/Puerto Rico/8/1934 H1N1), which was isolated and purified by SDS poly-acrylamide gel electrophoresis. Thus, LC-MS/MS analyses, coupled with manual de novo sequencing, allowed the determination of three substituted amino acid residues R452K, T423A and N430T in two tryptic peptides. The obtained results provided experimental evidence that amino acid substitutions resulted from non-synonymous gene mutations could be directly characterized by mass spectrometry in proteins of RNA viruses such as influenza A virus.
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