Peptide-Mediated Interference with Influenza A Virus Polymerase-Reference-Cited by-同舟云学术

Peptide-Mediated Interference with Influenza A Virus Polymerase

Published:2007-07-15 Issue:14 Volume:81 Page:7801-7804
ISSN:0022-538X
Container-title:Journal of Virology
language:en
Short-container-title:J Virol

Author:

Ghanem Alexander¹,Mayer Daniel¹,Chase Geoffrey¹,Tegge Werner²,Frank Ronald²,Kochs Georg¹,García-Sastre Adolfo³⁴,Schwemmle Martin¹

Affiliation:

1. Department of Virology, Institute for Medical Microbiology and Hygiene, University of Freiburg, Freiburg

2. Department of Chemical Biology, Helmholtz Centre for Infection Research, Braunschweig, Germany

3. Department of Microbiology

4. Emerging Pathogens Institute, Box 1124, Mount Sinai School of Medicine, 1 Gustave L. Levy Place, New York, New York 10029

Abstract

ABSTRACT The assembly of the polymerase complex of influenza A virus from the three viral polymerase subunits PB1, PB2, and PA is required for viral RNA synthesis. We show that peptides which specifically bind to the protein-protein interaction domains in the subunits responsible for complex formation interfere with polymerase complex assembly and inhibit viral replication. Specifically, we provide evidence that a 25-amino-acid peptide corresponding to the PA-binding domain of PB1 blocks the polymerase activity of influenza A virus and inhibits viral spread. Targeting polymerase subunit interactions therefore provides a novel strategy to develop antiviral compounds against influenza A virus or other viruses.

Publisher

American Society for Microbiology

Subject

Virology,Insect Science,Immunology,Microbiology

Link

https://journals.asm.org/doi/pdf/10.1128/JVI.00724-07

Reference21 articles.

1. Influenza virus polymerase basic protein 1 interacts with influenza virus polymerase basic protein 2 at multiple sites

2. Crescenzo-Chaigne, B., N. Naffakh, and S. van der Werf. 1999. Comparative analysis of the ability of the polymerase complexes of influenza viruses type A, B and C to assemble into functional RNPs that allow expression and replication of heterotypic model RNA templates in vivo. Virology265:342-353.

3. De Clercq, E. 2004. Antivirals and antiviral strategies. Nat Rev. Microbiol.2:704-720.

4. Dostmann, W. R., C. Nickl, S. Thiel, I. Tsigelny, R. Frank, and W. J. Tegge. 1999. Delineation of selective cyclic GMP-dependent protein kinase Ialpha substrate and inhibitor peptides based on combinatorial peptide libraries on paper. Pharmacol. Ther.82:373-387.

5. Fawell, S., J. Seery, Y. Daikh, C. Moore, L. L. Chen, B. Pepinsky, and J. Barsoum. 1994. Tat-mediated delivery of heterologous proteins into cells. Proc. Natl. Acad. Sci. USA91:664-668.

Cited by 118 articles. 订阅此论文施引文献订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献

1. Optimization of potent, broad-spectrum, and specific anti-influenza compounds targeting RNA polymerase PA-PB1 heterodimerization;European Journal of Medicinal Chemistry;2024-11

2. The PB2 I714S mutation influenced mammalian adaptation of the H3N2 canine influenza virus by interfering with nuclear import efficiency and RNP complex assembly;Emerging Microbes & Infections;2024-08-14

3. Novel Acyl Thiourea-Based Hydrophobic Tagging Degraders Exert Potent Anti-Influenza Activity through Two Distinct Endonuclease Polymerase Acidic-Targeted Degradation Pathways;Journal of Medicinal Chemistry;2024-05-22

4. Cryptic proteins translated from deletion-containing viral genomes dramatically expand the influenza virus proteome;Nucleic Acids Research;2024-02-26

5. Cryptic proteins translated from deletion-containing viral genomes dramatically expand the influenza virus proteome;2023-12-12