Structural Features of the Peptide Homologous to 6-25 Fragment of Influenza A PB1 Protein

doi:10.1155/2013/370832

. 2013:2013:370832.

doi: 10.1155/2013/370832. Epub 2013 Dec 24.

Structural Features of the Peptide Homologous to 6-25 Fragment of Influenza A PB1 Protein

Affiliations

¹ Department of Molecular Virology, FSBI Research Institute of Influenza, Ministry of Health of the Russian Federation, 15/17, Professor Popova Street, Saint Petersburg 197376, Russia ; Department of Molecular and Radiation Biophysics, Kurchatov Institute, FSBI St. Petersburg Nuclear Physics Institute, Orlova Roscha, Gatchina 188300, Russia.
² Department of Molecular Virology, FSBI Research Institute of Influenza, Ministry of Health of the Russian Federation, 15/17, Professor Popova Street, Saint Petersburg 197376, Russia ; Faculty of Chemistry, Saint Petersburg State University, Saint Petersburg 198504, Russia.
³ Department of Molecular Virology, FSBI Research Institute of Influenza, Ministry of Health of the Russian Federation, 15/17, Professor Popova Street, Saint Petersburg 197376, Russia.
⁴ Department of Molecular and Radiation Biophysics, Kurchatov Institute, FSBI St. Petersburg Nuclear Physics Institute, Orlova Roscha, Gatchina 188300, Russia.

PMID: 24454411
PMCID: PMC3886529
DOI: 10.1155/2013/370832

Structural Features of the Peptide Homologous to 6-25 Fragment of Influenza A PB1 Protein

Vladimir V Egorov et al. Int J Pept. 2013.

. 2013:2013:370832.

doi: 10.1155/2013/370832. Epub 2013 Dec 24.

Affiliations

¹ Department of Molecular Virology, FSBI Research Institute of Influenza, Ministry of Health of the Russian Federation, 15/17, Professor Popova Street, Saint Petersburg 197376, Russia ; Department of Molecular and Radiation Biophysics, Kurchatov Institute, FSBI St. Petersburg Nuclear Physics Institute, Orlova Roscha, Gatchina 188300, Russia.
² Department of Molecular Virology, FSBI Research Institute of Influenza, Ministry of Health of the Russian Federation, 15/17, Professor Popova Street, Saint Petersburg 197376, Russia ; Faculty of Chemistry, Saint Petersburg State University, Saint Petersburg 198504, Russia.
³ Department of Molecular Virology, FSBI Research Institute of Influenza, Ministry of Health of the Russian Federation, 15/17, Professor Popova Street, Saint Petersburg 197376, Russia.
⁴ Department of Molecular and Radiation Biophysics, Kurchatov Institute, FSBI St. Petersburg Nuclear Physics Institute, Orlova Roscha, Gatchina 188300, Russia.

PMID: 24454411
PMCID: PMC3886529
DOI: 10.1155/2013/370832

Abstract

A mirror-symmetry motif was discovered in the N-terminus of the influenza virus PB1 protein. Structure of peptide comprised of the corresponding part of PB1 (amino acid residues 6-25) was investigated by circular dichroism and in silico modeling. We found that peptide PB1 (6-25) in solution assumes beta-hairpin conformation. A truncated peptide PB1 (6-13), containing only half of the mirror-symmetry motif, appeared to stabilize the beta-structure of the original peptide and, at high concentrations, was capable of reacting with peptide to form insoluble aggregates in vitro. Ability of PB1 (6-13) peptide to interact with the N-terminal domain of PB1 protein makes it a potential antiviral agent that inhibits PA-PB1 complex formation by affecting PB1 N-terminus structure.

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Figures

**Figure 1**
MSM in the sequence of the N-terminal domain of PB1. Amino acid residues in symmetrical positions are printed in bold. Amino acid residues involved in the interaction with PA, according to the data [4, 5], are underlined.

**Figure 2**
Average 3-dimensional structure of the mirror-symmetric motif 6-25 PB1 according to the data of computer modeling. Beta-strands are represented as arrows. Numbers of residues begin from 1. Visualization using the ICM Molsoft software.

**Figure 3**
Circular dichroism spectrum of peptide PB1 (6-25).

**Figure 4**
Results of laser correlation spectroscopy of the aggregates formed in the solution as the result of the interaction of peptides PB1 (6-25) and PB1 (6-13).

**Figure 5**
Electron microscopy of a typical aggregate formed in the mixture of peptides PB1 (6-13) and PB1 (6-25). The length of the black rectangle is 500 nm.

**Figure 6**
Docking model of the mirror-symmetric motif PB1 (6-25) interacting with PB1 (6-13). Beta-strands are represented as arrows. Numbers of residues begin from 1. Visualization using the ICM Molsoft software.

**Figure 7**
PB1 (6-13) influence on the secondary structure of PB1 (6-25). Results of the differential spectrum analysis with CDNN software.

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References

1. Vlieghe P, Lisowski V, Martinez J, Khrestchatisky M. Synthetic therapeutic peptides: science and market. Drug Discovery Today. 2010;15(1-2):40–56. - PubMed
1. Torreira E, Schoehn G, Fernández Y, et al. Three-dimensional model for the isolated recombinant influenza virus polymerase heterotrimer. Nucleic Acids Research. 2007;35(11):3774–3783. - PMC - PubMed
1. Perez DR, Donis RO. Functional analysis of PA binding by influenza A virus PB1: effects on polymerase activity and viral infectivity. Journal of Virology. 2001;75(17):8127–8136. - PMC - PubMed
1. Wunderlich K, Juozapaitis M, Ranadheera C, et al. Identification of high-affinity PB1-derived peptides with enhanced affinity to the PA protein of influenza A virus polymerase. Antimicrobial Agents and Chemotherapy. 2011;55(2):696–702. - PMC - PubMed
1. He X, Zhou J, Bartlam M, et al. Crystal structure of the polymerase PAC-PB1N complex from an avian influenza H5N1 virus. Nature. 2008;454(7208):1123–1126. - PubMed

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[1] Vlieghe P, Lisowski V, Martinez J, Khrestchatisky M. Synthetic therapeutic peptides: science and market. Drug Discovery Today. 2010;15(1-2):40–56. - PubMed

[2] Vlieghe P, Lisowski V, Martinez J, Khrestchatisky M. Synthetic therapeutic peptides: science and market. Drug Discovery Today. 2010;15(1-2):40–56. - PubMed

[3] Torreira E, Schoehn G, Fernández Y, et al. Three-dimensional model for the isolated recombinant influenza virus polymerase heterotrimer. Nucleic Acids Research. 2007;35(11):3774–3783. - PMC - PubMed

[4] Torreira E, Schoehn G, Fernández Y, et al. Three-dimensional model for the isolated recombinant influenza virus polymerase heterotrimer. Nucleic Acids Research. 2007;35(11):3774–3783. - PMC - PubMed

[5] Perez DR, Donis RO. Functional analysis of PA binding by influenza A virus PB1: effects on polymerase activity and viral infectivity. Journal of Virology. 2001;75(17):8127–8136. - PMC - PubMed

[6] Perez DR, Donis RO. Functional analysis of PA binding by influenza A virus PB1: effects on polymerase activity and viral infectivity. Journal of Virology. 2001;75(17):8127–8136. - PMC - PubMed

[7] Wunderlich K, Juozapaitis M, Ranadheera C, et al. Identification of high-affinity PB1-derived peptides with enhanced affinity to the PA protein of influenza A virus polymerase. Antimicrobial Agents and Chemotherapy. 2011;55(2):696–702. - PMC - PubMed

[8] Wunderlich K, Juozapaitis M, Ranadheera C, et al. Identification of high-affinity PB1-derived peptides with enhanced affinity to the PA protein of influenza A virus polymerase. Antimicrobial Agents and Chemotherapy. 2011;55(2):696–702. - PMC - PubMed

[9] He X, Zhou J, Bartlam M, et al. Crystal structure of the polymerase PAC-PB1N complex from an avian influenza H5N1 virus. Nature. 2008;454(7208):1123–1126. - PubMed

[10] He X, Zhou J, Bartlam M, et al. Crystal structure of the polymerase PAC-PB1N complex from an avian influenza H5N1 virus. Nature. 2008;454(7208):1123–1126. - PubMed

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Structural Features of the Peptide Homologous to 6-25 Fragment of Influenza A PB1 Protein

Affiliations

Structural Features of the Peptide Homologous to 6-25 Fragment of Influenza A PB1 Protein

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