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Epitope mapping of cross-reactive monoclonal antibodies specific for the influenza A virus PA and PB2 polypeptides.
Abstract: Characterization of the epitopes recognized by 21 monoclonal antibodies (MAbs) specific for the influenza A virus PA (13 MAbs) and PB2 (8 MAbs) polypeptides (Bárcena et al. (1994) J. Virol. 68, 6900-6909) raised against denatured polypeptides produced in E. coli is described. MAbs were characterized by: (1) competitive binding ELISAs; (2) mapping of the protein regions that specify their binding sites; and (3) analyses of their ability to recognize the corresponding viral protein in a number of viral isolates. Five and three non-overlapping antigenic areas were defined by the anti-PA and anti-PB2 MAbs, respectively. Five of the anti-PA MAbs recognized antigenic determinants located within the amino-terminal 157 amino acids of the PA protein, and 6 others reacted strongly with a PA fragment comprising the first 236 amino acids. All 8 anti-PB2 antibodies reacted strongly with a polypeptide fragment containing amino acids 1-113 of the PB2 protein. Analyses of the reactivities of 4 anti-P antibodies with 23 influenza A virus reference strains isolated over a period of 61 years and recovered from humans, pigs, birds and horses, showed that the epitopes were conserved among all viral isolates. The application of these antibodies as research and diagnostic tools is discussed.
Publication Date: 1995-08-01 PubMed ID: 8533465DOI: 10.1016/0168-1702(95)00039-sGoogle Scholar: Lookup The Equine Research Bank provides access to a large database of publicly available scientific literature. Inclusion in the Research Bank does not imply endorsement of study methods or findings by Mad Barn.
- Journal Article
- Research Support
- Non-U.S. Gov't
Summary
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The article discusses the study of 21 monoclonal antibodies specific for the influenza A virus PA and PB2 polypeptides, their origins, characteristics, recognition properties, reactions with respective protein, and their potential use in research and diagnostics.
Research Design and Methods
- Monoclonal Antibodies (MAbs) used in the study were produced against denatured polypeptides in E. coli.
- The researchers utilized three main methods to characterize the MAbs: Competitive Binding ELISAs (Enzyme-linked Immunosorbent Assay), mapping the proteins region that stipulates their binding sites, and analyzing their capacity to recognize the respective viral proteins across different viral strains.
Results and Findings
- Upon analysis, five and three distinct antigenic areas were identified by anti-PA and anti-PB2 MAbs respectively.
- Five of the thirteen anti-PA Monoclonal Antibodies identified antigenic determinants situated within the amino-terminal 157 amino acids of the PA protein.
- Another six reacted strongly with a PA fragment containing the first 236 amino acids.
- All eight anti-PB2 antibodies reacted significantly with an area consisting of the first 1-113 amino acids of the PB2 protein.
Conservation of Epitopes and Their Importance
- Analyses of the reactivity of 4 anti-P antibodies were done with 23 influenza A virus reference strains isolated over a period of 61 years and recovered from different hosts (humans, pigs, birds, and horses).
- This analysis revealed that the epitopes (specific part of an antigen to which an antibody binds) were preserved amongst all viral isolates, indicating possible evolutionary conservation.
- This trait, therefore, underlines their diagnostic value since tests based on these epitopes would presumably work across different strains and hosts.
Potential Applications
- The study emphasizes the potential of these antibodies to be used as research tools because they can provide more detail about the virus’s structure and function.
- Given the conserved nature of the epitopes, these antibodies can also be deployed as diagnostic tools to detect the presence of influenza A virus across various hosts.
Cite This Article
APA
Ochoa M, Bárcena J, de la Luna S, Melero JA, Douglas AR, Nieto A, Ortín J, Skehel JJ, Portela A.
(1995).
Epitope mapping of cross-reactive monoclonal antibodies specific for the influenza A virus PA and PB2 polypeptides.
Virus Res, 37(3), 305-315.
https://doi.org/10.1016/0168-1702(95)00039-s Publication
Researcher Affiliations
- Instituto de Salud Carlos III, Centro Nacional de Biología Celular y Retrovirus, Madrid, Spain.
MeSH Terms
- Animals
- Antibodies, Monoclonal / immunology
- Antibodies, Viral / immunology
- Antibody Specificity
- Cross Reactions
- DNA-Directed RNA Polymerases / immunology
- Epitope Mapping
- Humans
- Influenza A virus / immunology
- RNA-Dependent RNA Polymerase
- Viral Proteins / immunology
Citations
This article has been cited 17 times.- Ren Y, Long S, Cao S. Molecular Docking and Virtual Screening of an Influenza Virus Inhibitor That Disrupts Protein-Protein Interactions. Viruses 2021 Nov 5;13(11).
- Meyerson NR, Zhou L, Guo YR, Zhao C, Tao YJ, Krug RM, Sawyer SL. Nuclear TRIM25 Specifically Targets Influenza Virus Ribonucleoproteins to Block the Onset of RNA Chain Elongation. Cell Host Microbe 2017 Nov 8;22(5):627-638.e7.
- Liu CH, Zhou L, Chen G, Krug RM. Battle between influenza A virus and a newly identified antiviral activity of the PARP-containing ZAPL protein. Proc Natl Acad Sci U S A 2015 Nov 10;112(45):14048-53.
- Ver LS, Marcos-Villar L, Landeras-Bueno S, Nieto A, Ortín J. The Cellular Factor NXP2/MORC3 Is a Positive Regulator of Influenza Virus Multiplication. J Virol 2015 Oct;89(19):10023-30.
- Chen G, Liu CH, Zhou L, Krug RM. Cellular DDX21 RNA helicase inhibits influenza A virus replication but is counteracted by the viral NS1 protein. Cell Host Microbe 2014 Apr 9;15(4):484-93.
- Landeras-Bueno S, Jorba N, Pérez-Cidoncha M, Ortín J. The splicing factor proline-glutamine rich (SFPQ/PSF) is involved in influenza virus transcription. PLoS Pathog 2011 Nov;7(11):e1002397.
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- Siebenga JJ, Lemey P, Kosakovsky Pond SL, Rambaut A, Vennema H, Koopmans M. Phylodynamic reconstruction reveals norovirus GII.4 epidemic expansions and their molecular determinants. PLoS Pathog 2010 May 6;6(5):e1000884.
- Coloma R, Valpuesta JM, Arranz R, Carrascosa JL, Ortín J, Martín-Benito J. The structure of a biologically active influenza virus ribonucleoprotein complex. PLoS Pathog 2009 Jun;5(6):e1000491.
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