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

Егоров, Владимир В.; Matusevich, Oleg V.; Shaldzhyan, Aram A.; Skvortsov, A. N.; Zabrodskaya, Yana A.; Garmay, Yuri; Landa, Sergey; Лебедев, Д. В.; Zarubayev, Vladimir V.; Сироткин, А. К.; Васин, А. В.; Киселев, О. И.

doi:10.1155/2013/370832

Cited by 10 publications

(14 citation statements)

References 9 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Peptides used as a model for the influenza A virus polymerase complex PB1 subunit N-terminal region: MDVNPTLLFLKVPAQNAISTTFPYT (PB1 ) and TLLFLKVPAQNAISTTFPYT (PB1 (6)(7)(8)(9)(10)(11)(12)(13)(14)(15)(16)(17)(18)(19)(20)(21)(22)(23)(24)(25)). The peptides tested were: TLLFLKVP (PB1 (6)(7)(8)(9)(10)(11)(12)(13)); TLLFLKVPA (PB1(6-13)-Ala); and FITClabeled TLLFLKVPA (FITC-PB1(6-13)-Ala).…”

Section: Peptidesmentioning

confidence: 99%

“…At the first stage, the interaction between the PB1(6-13) peptide fibrils and the PB1 subunit N-terminal region was studied by the SANS method ( Figure 5). (6)(7)(8)(9)(10)(11)(12)(13) in fibrillar form (black dots); and the normalized mathematical sum of the individual scattering curves for PB1 (6)(7)(8)(9)(10)(11)(12)(13)(14)(15)(16)(17)(18)(19)(20)(21)(22)(23)(24)(25) and PB1(6-13) (red curve)…”

Section: The Pb1(6-13) Peptide Fibril's Ability To Interact With the mentioning

confidence: 99%

“…Analogous calculations were made in the study of the PB1(6-13) and PB1 (6)(7)(8)(9)(10)(11)(12)(13)(14)(15)(16)(17)(18)(19)(20)(21)(22)(23)(24)(25) peptides' SAXS spectra in the q interval from 0.01 to 0.2 nm -1 . The changes in the singular decomposition zero and first components are shown in Figure 7(A) and 7(B), respectively.…”

Section: Timing Of the Interaction Between The Pb1(6-13) Peptide And mentioning

confidence: 99%

See 2 more Smart Citations

The amyloidogenicity of the influenza virus PB1-derived peptide sheds light on its antiviral activity

Zabrodskaya

Лебедев

Egorova

et al. 2017

Preprint

Self Cite

View full text Add to dashboard Cite

The influenza virus polymerase complex is a promising target for new antiviral drug development. It is known that, within the influenza virus polymerase complex, the PB1 subunit region from the 1 st to the 25 th amino acid residues has to be is in an alpha-helical conformation for proper interaction with the PA subunit. We have previously shown that PB1(6-13) peptide at low concentrations is able to interact with the PB1 subunit N-terminal region in a peptide model which shows aggregate formation and antiviral activity in cell cultures. In this paper, it was shown that PB1(6-13) peptide is prone to form the amyloid-like fibrillar aggregates. The peptide homo-oligomerization kinetics were examined, and the affinity and characteristic interaction time of PB1(6-13) peptide monomers and the influenza virus polymerase complex PB1 subunit N-terminal region were evaluated by the SPR and TR-SAXS methods. Based on the data obtained, a hypothesis about the PB1(6-13) peptide mechanism of action was proposed: the peptide in its monomeric form is capable of altering the conformation of the PB1 subunit N-terminal region, causing a change from an alpha helix to a beta structure. This conformational change disrupts PB1 and PA subunit interaction and, by that mechanism, the peptide displays antiviral activity.

show abstract

Section: Peptidesmentioning

confidence: 99%

Section: The Pb1(6-13) Peptide Fibril's Ability To Interact With the mentioning

confidence: 99%

Section: Timing Of the Interaction Between The Pb1(6-13) Peptide And mentioning

confidence: 99%

See 1 more Smart Citation

The amyloidogenicity of the influenza virus PB1-derived peptide sheds light on its antiviral activity

Zabrodskaya

Лебедев

Egorova

et al. 2017

Preprint

Self Cite

View full text Add to dashboard Cite

show abstract

“…In some cases, short peptides are capable of not only facilitating the adoption of an amyloidogenic protein conformation in its parent protein, but also causing changes in the parent protein's functional secondary structures. For example, it has been shown that the antiviral activity of the PB1 (6-13) peptide of influenza virus PB1 protein affects the secondary structure of the N-terminal domain of the PB1 protein itself [ 32 , 33 ].…”

Section: Induction Of Conformational Transitionsmentioning

confidence: 99%

“…It is interesting to note that those peptides for the prion protein PrP [ 27 ], alpha-lactalbumin [ 28 , 29 ], and PB1 [ 32 ], all of which are capable of inducing a parent protein conformational transition, contain mirror-symmetrical motifs (MSMs) within their primary structures ( Figure 6 ) [ 34 ]. Mirror-symmetrical motif formation can arise due to amplification of repeats in DNA and have a role in the formation of the tertiary structure in proteins [ 35 ].…”

Section: Induction Of Conformational Transitionsmentioning

confidence: 99%

Peptide-Induced Amyloid-Like Conformational Transitions in Proteins

Егоров

Грудинина

Васин

et al. 2015

International Journal of Peptides

View full text Add to dashboard Cite

Changes in protein conformation can occur both as part of normal protein functioning and during disease pathogenesis. The most common conformational diseases are amyloidoses. Sometimes the development of a number of diseases which are not traditionally related to amyloidoses is associated with amyloid-like conformational transitions of proteins. Also, amyloid-like aggregates take part in normal physiological processes such as memorization and cell signaling. Several primary structural features of a protein are involved in conformational transitions. Also the protein proteolytic fragments can cause the conformational transitions in the protein. Short peptides which could be produced during the protein life cycle or which are encoded by short open reading frames can affect the protein conformation and function.

show abstract

Amyloid peptides with antimicrobial and/or microbial agglutination activity

Chen

Liu

Chen

et al. 2022

Appl Microbiol Biotechnol

View full text Add to dashboard Cite

Microbe (including bacteria, fungi, and virus) infection in brains is associated with amyloid fibril deposit and neurodegeneration. Increasing findings suggest that amyloid proteins, like Abeta (Aβ), are important innate immune effectors in preventing infections. In some previous studies, amyloid peptides have been linked to antimicrobial peptides due to their common mechanisms in membrane-disruption ability, while the other mechanisms of bactericidal protein aggregation and protein function knockdown are less discussed. Besides, another important function of amyloid peptides in pathogen agglutination is rarely illustrated. In this review, we summarized and divided the different roles and mechanisms of amyloid peptides against microbes in antimicrobial activity and microbe agglutination activity. Besides, the range of amyloids’ antimicrobial spectrum, the effectiveness of amyloid peptide states (monomers, oligomers, and fibrils), and cytotoxicity are discussed. The good properties of amyloid peptides against microbes might provide implications for the development of novel antimicrobial drug. Key points • Antimicrobial and/or microbial agglutination is a characteristic of amyloid peptides. • Various mechanisms of amyloid peptides against microbes are discovered recently . • Amyloid peptides might be developed into novel antimicrobial drugs . Supplementary information The online version contains supplementary material available at 10.1007/s00253-022-12246-w.

show abstract

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

Cited by 10 publications

References 9 publications

The amyloidogenicity of the influenza virus PB1-derived peptide sheds light on its antiviral activity

The amyloidogenicity of the influenza virus PB1-derived peptide sheds light on its antiviral activity

Peptide-Induced Amyloid-Like Conformational Transitions in Proteins

Amyloid peptides with antimicrobial and/or microbial agglutination activity

Contact Info

Product

Resources

About