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Article ; Online: Quadrivalent adjuvanted haemagglutinin nanoparticle influenza vaccine: a step towards better protection of older adults from the constantly mutating H3N2 influenza viruses.

Isakova-Sivak, Irina / Matyushenko, Victoria

2021 Volume 22, Issue 1, Page(s) 7–8

MeSH term(s)	Adjuvants, Immunologic/administration & dosage ; Age Factors ; Aged ; Antibodies, Viral/blood ; Humans ; Influenza A Virus, H3N2 Subtype/genetics ; Influenza A Virus, H3N2 Subtype/immunology ; Influenza A Virus, H3N2 Subtype/pathogenicity ; Influenza Vaccines/administration & dosage ; Influenza Vaccines/immunology ; Influenza, Human/immunology ; Influenza, Human/prevention & control ; Mutation ; Nanoparticles/administration & dosage ; Nanoparticles/chemistry ; Vaccine Potency
Chemical Substances	Adjuvants, Immunologic ; Antibodies, Viral ; Influenza Vaccines
Language	English
Publishing date	2021-09-23
Publishing country	United States
Document type	Journal Article
ZDB-ID	2061641-7
ISSN	1474-4457 ; 1473-3099
ISSN (online)	1474-4457
ISSN	1473-3099
DOI	10.1016/S1473-3099(21)00209-7
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Article ; Online: Neurofilament Light Protein Rod Domain Exhibits Structural Heterogeneity.

Nefedova, Victoria V / Kleymenov, Sergey Y / Safenkova, Irina V / Levitsky, Dmitrii I / Matyushenko, Alexander M

Biomolecules

2024 Volume 14, Issue 1

Abstract: Neurofilaments are neuron-specific proteins that belong to the intermediate filament (IFs) protein family, with the neurofilament light chain protein (NFL) being the most abundant. The IFs structure typically includes a central coiled-coil rod domain ... ...

Abstract	Neurofilaments are neuron-specific proteins that belong to the intermediate filament (IFs) protein family, with the neurofilament light chain protein (NFL) being the most abundant. The IFs structure typically includes a central coiled-coil rod domain comprised of coils 1A, 1B, and 2, separated by linker regions. The thermal stability of the IF molecule plays a crucial role in its ability for self-association. In the current study, we investigated the thermal stability of NFL coiled-coil domains by analyzing a set of recombinant domains and their fusions (NFL
MeSH term(s)	Intermediate Filaments ; Tumor Necrosis Factor Ligand Superfamily Member 14 ; Calorimetry, Differential Scanning ; Neurons ; Protein Domains
Chemical Substances	Tumor Necrosis Factor Ligand Superfamily Member 14
Language	English
Publishing date	2024-01-09
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2701262-1
ISSN	2218-273X ; 2218-273X
ISSN (online)	2218-273X
ISSN	2218-273X
DOI	10.3390/biom14010085
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Article ; Online: Myopathy-causing mutation R91P in the TPM3 gene drastically impairs structural and functional properties of slow skeletal muscle tropomyosin γβ-heterodimer.

Gonchar, Anastasiia D / Koubassova, Natalia A / Kopylova, Galina V / Kochurova, Anastasia M / Nefedova, Victoria V / Yampolskaya, Daria S / Shchepkin, Daniil V / Bershitsky, Sergey Y / Tsaturyan, Andrey K / Matyushenko, Alexander M / Levitsky, Dmitrii I

Archives of biochemistry and biophysics

2024 Volume 752, Page(s) 109881

Abstract: Tropomyosin (Tpm) is a regulatory actin-binding protein involved in ... ...

Abstract	Tropomyosin (Tpm) is a regulatory actin-binding protein involved in Ca
MeSH term(s)	Humans ; Tropomyosin/chemistry ; Muscle, Skeletal/metabolism ; Muscular Diseases/genetics ; Mutation ; Muscle Weakness/metabolism ; Actins/genetics ; Actins/metabolism
Chemical Substances	Tropomyosin ; Actins ; TPM3 protein, human
Language	English
Publishing date	2024-01-06
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	523-x
ISSN	1096-0384 ; 0003-9861
ISSN (online)	1096-0384
ISSN	0003-9861
DOI	10.1016/j.abb.2023.109881
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Article ; Online: Effect of Neurodegenerative Mutations in the NEFL Gene on Thermal Denaturation of the Neurofilament Light Chain Protein.

Nefedova, Victoria V / Yampolskaya, Daria S / Kleymenov, Sergey Y / Chebotareva, Natalia A / Matyushenko, Alexander M / Levitsky, Dmitrii I

Biochemistry. Biokhimiia

2023 Volume 88, Issue 5, Page(s) 610–620

Abstract: Effects of E90K, N98S, and A149V mutations in the light chain of neurofilaments (NFL) on the structure and thermal denaturation of the NFL molecule were investigated. By using circular dichroism spectroscopy, it was shown that these mutations did not ... ...

Abstract	Effects of E90K, N98S, and A149V mutations in the light chain of neurofilaments (NFL) on the structure and thermal denaturation of the NFL molecule were investigated. By using circular dichroism spectroscopy, it was shown that these mutations did not lead to the changes in α-helical structure of NFL, but they caused noticeable effects on the stability of the molecule. We also identified calorimetric domains in the NFL structure by using differential scanning calorimetry. It was shown that the E90K replacement leads to the disappearance of the low-temperature thermal transition (domain 1). The mutations cause changes in the enthalpy of NFL domains melting, as well as lead to the significant changes in the melting temperatures (T
MeSH term(s)	Intermediate Filaments/metabolism ; Proteins/metabolism ; Mutation ; Protein Denaturation ; Calorimetry, Differential Scanning ; Circular Dichroism
Chemical Substances	Proteins
Language	English
Publishing date	2023-06-16
Publishing country	United States
Document type	Journal Article
ZDB-ID	1109-5
ISSN	1608-3040 ; 0006-2979 ; 0320-9717
ISSN (online)	1608-3040
ISSN	0006-2979 ; 0320-9717
DOI	10.1134/S0006297923050048
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Article: In Vitro Stimulation with Live SARS-CoV-2 Suggests Th17 Dominance In Virus-Specific CD4+ T Cell Response after COVID-19.

Kudryavtsev, Igor / Matyushenko, Victoria / Stepanova, Ekaterina / Vasilyev, Kirill / Rudenko, Larisa / Isakova-Sivak, Irina

Vaccines

2022 Volume 10, Issue 9

Abstract: The SARS-CoV-2 and influenza viruses are the main causes of human respiratory tract infections with similar disease manifestation but distinct mechanisms of immunopathology and host response to the infection. In this study, we investigated the SARS-CoV-2- ...

Abstract	The SARS-CoV-2 and influenza viruses are the main causes of human respiratory tract infections with similar disease manifestation but distinct mechanisms of immunopathology and host response to the infection. In this study, we investigated the SARS-CoV-2-specific CD4+ T cell phenotype in comparison with H1N1 influenza-specific CD4+ T cells. We determined the levels of SARS-CoV-2- and H1N1-specific CD4+ T cell responses in subjects recovered from COVID-19 one to 15 months ago by stimulating PBMCs with live SARS-CoV-2 or H1N1 influenza viruses. We investigated phenotypes and frequencies of main CD4+ T cell subsets specific for SARS-CoV-2 using an activation induced cell marker assay and multicolor flow cytometry, and compared the magnitude of SARS-CoV-2- and H1N1-specific CD4+ T cells. SARS-CoV-2-specific CD4+ T cells were detected 1-15 months post infection and the frequency of SARS-CoV-2-specific central memory CD4+ T cells was increased with the time post-symptom onset. Next, SARS-CoV-2-specific CD4+ T cells predominantly expressed the Th17 phenotype, but the level of Th17 cells in this group was lower than in H1N1-specific CD4+ T cells. Finally, we found that the lower level of total Th17 subset within total SARS-CoV-2-specific CD4+ T cells was linked with the low level of CCR4+CXCR3- 'classical' Th17 cells if compared with H1N1-specific Th17 cells. Taken together, our data suggest the involvement of Th17 cells and their separate subsets in the pathogenesis of SARS-CoV-2- and influenza-induced pneumonia; and a better understanding of Th17 mediated antiviral immune responses may lead to the development of new therapeutic strategies.
Language	English
Publishing date	2022-09-16
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2703319-3
ISSN	2076-393X
ISSN	2076-393X
DOI	10.3390/vaccines10091544
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Article: Truncation of NS1 Protein Enhances T Cell-Mediated Cross-Protection of a Live Attenuated Influenza Vaccine Virus Expressing Wild-Type Nucleoprotein.

Prokopenko, Polina / Matyushenko, Victoria / Rak, Alexandra / Stepanova, Ekaterina / Chistyakova, Anna / Goshina, Arina / Kudryavtsev, Igor / Rudenko, Larisa / Isakova-Sivak, Irina

Vaccines

2023 Volume 11, Issue 3

Abstract: Current seasonal influenza vaccines have suboptimal effectiveness, especially in seasons dominated by viruses that do not match the vaccine. Therefore, finding new approaches to improve the immunogenicity and efficacy of traditional influenza vaccines is ...

Abstract	Current seasonal influenza vaccines have suboptimal effectiveness, especially in seasons dominated by viruses that do not match the vaccine. Therefore, finding new approaches to improve the immunogenicity and efficacy of traditional influenza vaccines is of high priority for public health. Licensed live attenuated influenza vaccine (LAIV) is a promising platform for designing broadly protective vaccines due to its ability to induce cross-reactive T-cell immunity. In this study, we tested the hypothesis that truncation of the nonstructural protein 1 (NS1) and the replacement of the nucleoprotein (NP) of the A/Leningrad/17 master donor virus with a recent NP, i.e., switching to 5:3 genome composition, could improve the cross-protective potential of the LAIV virus. We generated a panel of LAIV candidates differing from the classical vaccine by the source of NP gene and/or by the length of NS1 protein. We showed that NS1-modified LAIV viruses had reduced viral replication in the respiratory tract of mice, indicating a more attenuated phenotype compared to the LAIVs with full-length NS1. Most importantly, the LAIV candidate with both NP and NS genes modified induced a robust systemic and lung-localized memory CD8 T-cell response targeting more recent viruses, and better protected immunized mice against lethal challenge with a heterosubtypic influenza virus than the control LAIV variant. Overall, these data indicate that the 5:3 LAIVs with truncated NS1 may be beneficial for protection against heterologous influenza viruses and warrant further preclinical and clinical development.
Language	English
Publishing date	2023-02-21
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2703319-3
ISSN	2076-393X
ISSN	2076-393X
DOI	10.3390/vaccines11030501
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Article ; Online: Structural and Functional Properties of Tropomyosin Isoforms Tpm4.1 and Tpm2.1.

Logvinov, Andrey S / Nefedova, Victoria V / Yampolskaya, Daria S / Kleymenov, Sergey Y / Levitsky, Dmitrii I / Matyushenko, Alexander M

Biochemistry. Biokhimiia

2023 Volume 88, Issue 6, Page(s) 801–809

Abstract: Tropomyosin (Tpm) is one of the most important partners of actin filament that largely determines its properties. In animal organisms, there are different isoforms of Tpm, which are believed to be involved in the regulation of various cellular functions. ...

Abstract	Tropomyosin (Tpm) is one of the most important partners of actin filament that largely determines its properties. In animal organisms, there are different isoforms of Tpm, which are believed to be involved in the regulation of various cellular functions. However, molecular mechanisms by which various Tpm cytoplasmic regulate of the functioning of actin filaments are still poorly understood. Here, we investigated the properties of Tpm2.1 and Tpm4.1 isoforms and compared them to each other and to more extensively studied Tpm isoforms. Tpm2.1 and Tpm4.1 were very similar in their affinity to F-actin, thermal stability, and resistance to limited proteolysis by trypsin, but differed markedly in the viscosity of their solutions and thermal stability of their complexes with F-actin. The main difference of Tpm2.1 and Tpm4.1 from other Tpm isoforms (e.g., Tpm1.6 and Tpm1.7) was their extremely low thermal stability as measured by the CD and DSC methods. We suggested the possible causes of this instability based on comparing the amino acid sequences of Tpm4.1 and Tpm2.1 with the sequences of Tpm1.6 and Tpm1.7 isoforms, respectively, that have similar exon structure.
MeSH term(s)	Animals ; Actins ; Tropomyosin ; Cytoskeletal Proteins ; Protein Isoforms ; Amino Acid Sequence
Chemical Substances	Actins ; Tropomyosin ; Cytoskeletal Proteins ; Protein Isoforms
Language	English
Publishing date	2023-09-25
Publishing country	United States
Document type	Journal Article
ZDB-ID	1109-5
ISSN	1608-3040 ; 0006-2979 ; 0320-9717
ISSN (online)	1608-3040
ISSN	0006-2979 ; 0320-9717
DOI	10.1134/S0006297923060081
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Article ; Online: RDE Treatment Prevents Non-Specific Detection of SARS-CoV-2- and Influenza-Specific IgG Antibodies in Heat-Inactivated Serum Samples.

Goshina, Arina / Matyushenko, Victoria / Mezhenskaya, Daria / Rak, Alexandra / Katelnikova, Anastasia / Gusev, Denis / Rudenko, Larisa / Isakova-Sivak, Irina

Antibodies (Basel, Switzerland)

2023 Volume 12, Issue 2

Abstract: Assessing the levels of serum IgG antibodies is widely used to measure immunity to influenza and the new severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) after natural infection or vaccination with specific vaccines, as well as to study ... ...

Abstract	Assessing the levels of serum IgG antibodies is widely used to measure immunity to influenza and the new severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) after natural infection or vaccination with specific vaccines, as well as to study immune responses to these viruses in animal models. For safety reasons, sometimes serum specimens collected from infected individuals are subjected to heat inactivation at 56 °C to reduce the risk of infecting personnel during serological studies. However, this procedure may affect the level of virus-specific antibodies, making the results of antibody immunoassays uninterpretable. Here, we evaluated the effect of the heat inactivation of human, ferret and hamster serum samples on the binding of IgG antibodies to the influenza and SARS-CoV-2 antigens. For this, serum samples of naive and immune hosts were analyzed in three variants: (i) untreated sera, (ii) heated at 56 °C for 1 h, and (iii) treated with receptor-destroying enzyme (RDE). The samples were studied through an in-house enzyme-linked immunosorbent assay (ELISA) using whole influenza virus or recombinant proteins corresponding to nucleocapsid (N) protein and the receptor-binding domain of SARS-CoV-2 Spike (RBD) as antigens. We demonstrated that the heat inactivation of the naive serum samples of various hosts can lead to false-positive results, while RDE treatment abolished the effect of the non-specific binding of IgG antibodies to the viral antigens. Furthermore, RDE also significantly decreased the level of virus-specific IgG antibodies in SARS-CoV-2 and influenza-immune sera of humans and animals, although it is unknown whether it actually removes true virus-specific IgG antibodies or only non-specifically binding artifacts. Nevertheless, we suggest that the RDE treatment of human and animal sera may be useful in preventing false-positive results in various immunoassays, while also neutralizing infectious virus, since the standard protocol for the use of RDE also includes heating the sample at 56 °C.
Language	English
Publishing date	2023-06-16
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2661514-9
ISSN	2073-4468 ; 2073-4468
ISSN (online)	2073-4468
ISSN	2073-4468
DOI	10.3390/antib12020039
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Article ; Online: Structural and Functional Peculiarities of Cytoplasmic Tropomyosin Isoforms, the Products of

Marchenko, Marina / Nefedova, Victoria / Artemova, Natalia / Kleymenov, Sergey / Levitsky, Dmitrii / Matyushenko, Alexander

International journal of molecular sciences

2021 Volume 22, Issue 10

Abstract: Tropomyosin (Tpm) is one of the major protein partners of actin. Tpm molecules ... ...

Abstract	Tropomyosin (Tpm) is one of the major protein partners of actin. Tpm molecules are
MeSH term(s)	Actin Cytoskeleton/metabolism ; Alternative Splicing ; Cytoplasm/metabolism ; Exons ; Humans ; Protein Isoforms ; Tropomyosin/chemistry ; Tropomyosin/genetics ; Tropomyosin/metabolism
Chemical Substances	Protein Isoforms ; TPM1 protein, human ; TPM4 protein, human ; Tropomyosin
Language	English
Publishing date	2021-05-13
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2019364-6
ISSN	1422-0067 ; 1422-0067 ; 1661-6596
ISSN (online)	1422-0067
ISSN	1422-0067 ; 1661-6596
DOI	10.3390/ijms22105141
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Article: Prospects of and Barriers to the Development of Epitope-Based Vaccines against Human Metapneumovirus.

Stepanova, Ekaterina / Matyushenko, Victoria / Rudenko, Larisa / Isakova-Sivak, Irina

Pathogens (Basel, Switzerland)

2020 Volume 9, Issue 6

Abstract: Human metapneumovirus (HMPV) is a major cause of respiratory illnesses in children, the elderly and immunocompromised patients. Although this pathogen was only discovered in 2001, an enormous amount of research has been conducted in order to develop safe ...

Abstract	Human metapneumovirus (HMPV) is a major cause of respiratory illnesses in children, the elderly and immunocompromised patients. Although this pathogen was only discovered in 2001, an enormous amount of research has been conducted in order to develop safe and effective vaccines to prevent people from contracting the disease. In this review, we summarize current knowledge about the most promising experimental B- and T-cell epitopes of human metapneumovirus for the rational design of HMPV vaccines using vector delivery systems, paying special attention to the conservation of these epitopes among different lineages/genotypes of HMPV. The prospects of the successful development of an epitope-based HMPV vaccine are discussed in the context of recent findings regarding HMPV's ability to modulate host immunity. In particular, we discuss the lack of data on experimental human CD4 T-cell epitopes for HMPV despite the role of CD4 lymphocytes in both the induction of higher neutralizing antibody titers and the establishment of CD8 memory T-cell responses. We conclude that current research should be focused on searching for human CD4 T-cell epitopes of HMPV that can help us to design a safe and cross-protective epitope-based HMPV vaccine.
Keywords	covid19
Language	English
Publishing date	2020-06-18
Publishing country	Switzerland
Document type	Journal Article ; Review
ZDB-ID	2695572-6
ISSN	2076-0817
ISSN	2076-0817
DOI	10.3390/pathogens9060481
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