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Memczak, H.; Lauster, D.; Kar, P.; Lella, S.D.; Volkmer, R.; Knecht, V.; Herrmann, A.; Ehrentreich-Förster, E.; Bier, F.F.; Stöcklein, W.F.M. "Anti-hemagglutinin antibody derived lead peptides for inhibitors of influenza virus binding" (2016) PLoS ONE. 11(7)
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Abstract:

Antibodies against spike proteins of influenza are used as a tool for characterization of viruses and therapeutic approaches. However, development, production and quality control of antibodies is expensive and time consuming. To circumvent these difficulties, three peptides were derived from complementarity determining regions of an antibody heavy chain against influenza A spike glycoprotein. Their binding properties were studied experimentally, and by molecular dynamics simulations. Two peptide candidates showed binding to influenza A/Aichi/2/68 H3N2. One of them, termed PeB, with the highest affinity prevented binding to and infection of target cells in the micromolar region without any cytotoxic effect. PeB matches best the conserved receptor binding site of hemagglutinin. PeB bound also to other medical relevant influenza strains, such as human-pathogenic A/California/7/2009 H1N1, and avian-pathogenic A/Mute Swan/Rostock/R901/2006 H7N1. Strategies to improve the affinity and to adapt specificity are discussed and exemplified by a double amino acid substituted peptide, obtained by substitutional analysis. The peptides and their derivatives are of great potential for drug development as well as biosensing. © 2016 Memczak et al. This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.

Registro:

Documento: Artículo
Título:Anti-hemagglutinin antibody derived lead peptides for inhibitors of influenza virus binding
Autor:Memczak, H.; Lauster, D.; Kar, P.; Lella, S.D.; Volkmer, R.; Knecht, V.; Herrmann, A.; Ehrentreich-Förster, E.; Bier, F.F.; Stöcklein, W.F.M.
Filiación:Department of Bioanalytics and Biosensorics, Fraunhofer Institute for Cell Therapy and Immunology, Branch Bioanalytics and Bioprocesses, Potsdam, Germany
Institute of Biochemistry and Biology, University of Potsdam, Potsdam, Germany
Department of Biology, Humboldt Universität zu Berlin, Berlin, Germany
Department of Theory and Bio-Systems, Max-Planck-Institute of Colloids and Interfaces, Potsdam, Germany
Departamento de Química Biológica E IQUIBICEN-CONICET, Facultad de Ciencias Exactas Y Naturales, Universidad de Buenos Aires, Buenos Aires, Argentina
Institute of Immunology, Charité, Berlin, Germany
Department of Biosystem Integration and Automation, Fraunhofer Institute for Cell Therapy and Immunology, Branch Bioanalytics and Bioprocesses, Potsdam, Germany
Center for Biosciences and Biomedical Engineering, Indian Institute of Technology Indore, Indore, MP, India
Department of Biomolecular Dynamics, Institute of Physics, Albert Ludwigs University, Freiburg, Germany
Palabras clave:antivirus agent; Influenza virus hemagglutinin antibody derivative; peptide PeA; peptide PeB; peptide PeC; unclassified drug; virus spike protein; epitope; Influenza virus hemagglutinin; neutralizing antibody; virus antibody; amino acid substitution; animal cell; antiviral activity; Article; binding affinity; binding competition; circular dichroism; complementarity determining region; concentration response; controlled study; drug binding site; drug design; drug synthesis; genetic procedures; hemagglutination inhibition test; human; human cell; Influenza A virus; Influenza A virus (A/Aichi/2/68(H3N2)); Influenza A virus (A/California/7/2009(H1N1)); Influenza A virus (A/Mute Swan/Rostock/R901/2006(H7N1)); inhibition kinetics; microarray analysis; molecular dynamics; nonhuman; protein modification; surface plasmon resonance; target cell; virus cell interaction; virus neutralization; virus strain; animal; cell line; dog; immunology; influenza; virology; virus attachment; Animals; Antibodies, Neutralizing; Antibodies, Viral; Cell Line; Dogs; Epitopes; Hemagglutinin Glycoproteins, Influenza Virus; Humans; Influenza, Human; Molecular Dynamics Simulation; Virus Attachment
Año:2016
Volumen:11
Número:7
DOI: http://dx.doi.org/10.1371/journal.pone.0159074
Título revista:PLoS ONE
Título revista abreviado:PLoS ONE
ISSN:19326203
CODEN:POLNC
CAS:Antibodies, Neutralizing; Antibodies, Viral; Epitopes; Hemagglutinin Glycoproteins, Influenza Virus
Registro:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_19326203_v11_n7_p_Memczak

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Citas:

---------- APA ----------
Memczak, H., Lauster, D., Kar, P., Lella, S.D., Volkmer, R., Knecht, V., Herrmann, A.,..., Stöcklein, W.F.M. (2016) . Anti-hemagglutinin antibody derived lead peptides for inhibitors of influenza virus binding. PLoS ONE, 11(7).
http://dx.doi.org/10.1371/journal.pone.0159074
---------- CHICAGO ----------
Memczak, H., Lauster, D., Kar, P., Lella, S.D., Volkmer, R., Knecht, V., et al. "Anti-hemagglutinin antibody derived lead peptides for inhibitors of influenza virus binding" . PLoS ONE 11, no. 7 (2016).
http://dx.doi.org/10.1371/journal.pone.0159074
---------- MLA ----------
Memczak, H., Lauster, D., Kar, P., Lella, S.D., Volkmer, R., Knecht, V., et al. "Anti-hemagglutinin antibody derived lead peptides for inhibitors of influenza virus binding" . PLoS ONE, vol. 11, no. 7, 2016.
http://dx.doi.org/10.1371/journal.pone.0159074
---------- VANCOUVER ----------
Memczak, H., Lauster, D., Kar, P., Lella, S.D., Volkmer, R., Knecht, V., et al. Anti-hemagglutinin antibody derived lead peptides for inhibitors of influenza virus binding. PLoS ONE. 2016;11(7).
http://dx.doi.org/10.1371/journal.pone.0159074