A5021986271- Influenza Virus Research Studies
- Protein Structure and Dynamics
- Monoclonal and Polyclonal Antibodies Research
- Respiratory viral infections research
- RNA and protein synthesis mechanisms
- Enzyme Structure and Function
- Viral gastroenteritis research and epidemiology
- Advanced Proteomics Techniques and Applications
- Bacteriophages and microbial interactions
- Mass Spectrometry Techniques and Applications
- Virology and Viral Diseases
- Biochemical and Structural Characterization
- Neuroscience and Neuropharmacology Research
- Virus-based gene therapy research
- Lipid Membrane Structure and Behavior
- Protein purification and stability
- Glycosylation and Glycoproteins Research
- interferon and immune responses
- Metabolomics and Mass Spectrometry Studies
- HER2/EGFR in Cancer Research
- SARS-CoV-2 and COVID-19 Research
- vaccines and immunoinformatics approaches
- Peptidase Inhibition and Analysis
- Analytical Chemistry and Chromatography
- Immune Response and Inflammation
Lomonosov Moscow State University
2015-2024
Moscow State University
2008-2023
S acylation of cysteines located in the transmembrane and/or cytoplasmic region influenza virus hemagglutinins (HA) contributes to membrane fusion and assembly virions. Our results from using mass spectrometry (MS) show that B HA possessing two contains palmitate, whereas HA-esterase-fusion glycoprotein C having one cysteine is stearoylated. HAs A contain both palmitate stearate. MS analysis recombinant viruses with deletions individual cysteines, as well tandem-MS sequencing, revealed...
Covalent attachment of C16:0 to proteins (palmitoylation) regulates protein function. Proteins are also S-acylated by other fatty acids including C18:0. Whether acylation with different has functional outcomes is not well studied. We show here that C18:0 (stearate) and C18:1 (oleate) compete S-acylate Cys3 GNAI proteins. becomes desaturated so both cause S-oleoylation GNAI. Exposure cells or shifts towards palmitoylation oleoylation, respectively. Oleoylation causes shift out cell membrane...
Inactivated vaccines are promising tools for tackling the COVID-19 pandemic. We applied several protocols SARS-CoV-2 inactivation (by β-propiolactone, formaldehyde, and UV radiation) examined morphology of viral spikes, protein composition preparations, their immunoreactivity in ELISA using two panels sera collected from convalescents people vaccinated by Sputnik V. Transmission electron microscopy (TEM) allowed us to distinguish wider flail-like spikes (supposedly S-protein’s pre-fusion...
Hemagglutinin (HA), the trimeric spike of influenza virus, catalyzes fusion viral and cellular membranes. We have synthesized anchoring peptide including linker, transmembrane region cytoplasmic tail (HA-TMR-CT) in a cell-free system. Furthermore, to mimic palmitoylation three conserved cysteines within CT, we chemically alkylated HA-TMR-CT using hexadecyl-methanethiosulfonate. While nuclear magnetic resonance spectroscopy showed pure refolded peptides, formation multiple oligomers higher...
Influenza A virus hemagglutinin (HA) is a major envelope glycoprotein mediating viral and cell membrane fusion. HA anchored in the by light HA(2) chain containing one transmembrane domain cytoplasmic tail. Three cysteine residues C-terminal region, two tail, are highly conserved potentially palmitoylated all subtypes. The C- terminal anchoring segments were extracted to organic phase from bromelain-digested viruses (subviral particles) of three strains: A/X-31 (H3 subtype), A/Puerto...
Recruitment of the matrix protein M1 to assembly site influenza virus is thought be mediated by interactions with cytoplasmic tail hemagglutinin (HA). Based on a comprehensive sequence comparison all sequences present in database, we analyzed effect mutating conserved residues cytosol-facing part transmembrane region and HA (A/WSN/33 (H1N1) strain) replication morphology virions. Removal two acylation sites substitution neighboring isoleucine glutamine prevented rescue infectious In...
The first attempt has been made to suggest a model of influenza A virus matrix M1 protein spatial structure and molecule orientation within virion on the basis tritium planigraphy data theoretical prediction results. Limited in situ proteolysis intact virions with bromelain surface plasmon resonance spectroscopy study interaction lipid coated surfaces were used for independent confirmation proposed model.
Influenza A virus envelope contains lipid molecules of the host cell and three integral viral proteins: major hemagglutinin, neuraminidase, minor M2 protein. Membrane-associated M1 matrix protein is thought to interact with bilayer cytoplasmic domains proteins form infectious progeny. We used small-angle X-ray scattering (SAXS) complementary techniques analyze interactions different components Small unilamellar liposomes composed various mixtures synthetic or “native” lipids extracted from...
Interactions between integral membrane proteins hemagglutinin (HA), neuraminidase (NA), M2 and membrane-associated matrix protein M1 of influenza A virus are thought to be crucial for assembly functionally competent virions. We hypothesized that the amino acid residues located at interface two different under physical constraints thus probably co-evolve. To predict co-evolving residue pairs, EvFold ( http://evfold.org ) program searching (nontransitive) Direct Information scores was applied...
The structural study of plant viruses is great importance to reduce the damage caused by these agricultural pathogens and support their biotechnological applications. Nowadays, X-ray crystallography, NMR spectroscopy cryo-electron microscopy are well accepted methods obtain 3D protein structure with best resolution. However, for large complex supramolecular structures such as viruses, especially flexible filamentous ones, there a number technical limitations resolving native in solution. In...
Influenza A virus matrix M1 protein is membrane associated and plays a crucial role in assembly budding. The N-terminal two thirds of was resolved by X-ray crystallography. overall 3D structure as well arrangement the molecule relation to viral remains obscure. Now proteolytic digestion virions with bromelain used an instrument for situ assessment structure. lipid bilayer around subviral particles lacking glycoprotein spikes partially disrupted shown transmission electron microscopy....
MALDI-TOF MS and N-terminal amino acid sequencing allowed us to identify several fragments of the C-terminal peptide Influenza A hemagglutinin (HA) containing transmembrane domains (TMD). These were detected in organic phase chloroform-methanol extracts from bromelain-treated virus particles. Heterogeneous fatty acylation C-terminus was revealed. Tritium bombardment technique might open an opportunity for 3D structural investigation HA TMD situ.