Victor Vitoldovich Poboinev
@bsmu.by
General chemistry
Belarusian State Medical University
RESEARCH INTERESTS
Molecular biology, proteomics, bioinformatics, biophysics, biochemistry, pathological physiology
Scopus Publications
Scholar Citations
Scholar h-index
Scholar i10-index
Scopus Publications
Vladislav Victorovich Khrustalev, Aleksander Nicolaevich Stojarov, Anastasia Aleksandrovna Akunevich, Oleg Evgenyevich Baranov, Anna Vladimirovna Popinako, Elena Olegovna Samoilovich, Marina Anatolyevna Yermalovich, Galina Valeryevna Semeiko, Egor Gennadyevich Sapon, Victoria Igorevna Cheprasova,et al.
Bentham Science Publishers Ltd.
Background:: Binding appropriate cellular receptors is a crucial step of a lifecycle for any virus. Structure of receptor-binding domain for a viral surface protein has to be determined before the start of future drug design projects. Objective:: Investigation of pH-induced changes in the secondary structure for a capsid peptide with loss of function mutation can shed some light on the mechanism of entrance. Methods:: Spectroscopic methods were accompanied by electrophoresis, ultrafiltration, and computational biochemistry. Results:: In this study, we showed that a peptide from the receptor-binding domain of Parvovirus B19 VP1 capsid (residues 13-31) is beta-structural at pH=7.4 in 0.01 M phosphate buffer, but alpha- helical at pH=5.0, according to the circular dichroism (CD) spectroscopy results. Results of infra- red (IR) spectroscopy showed that the same peptide exists in both alpha-helical and beta-structural conformations in partial dehydration conditions both at pH=7.4 and pH=5.0. In contrast, the peptide with Y20W mutation, which is known to block the internalization of the virus, forms mostly alpha-helical conformation in partial dehydration conditions at pH=7.4. According to our hypothesis, an intermolecular antiparallel beta structure formed by the wild-type peptide in its tetramers at pH=7.4 is the prototype of the similar intermolecular antiparallel beta structure formed by the corresponding part of Parvovirus B19 receptor-binding domain with its cellular receptor (AXL). Conclusion:: Loss of function Y20W substitution in VP1 capsid protein prevents the shift into the beta-structural state by way of alpha helix stabilization and the decrease of its ability to turn into the disordered state.
Victor Vitoldovich Poboinev, Vladislav Victorovich Khrustalev, Anastasia Aleksandrovna Akunevich, Nikolai Vladimirovich Shalygo, Aleksander Nikolaevich Stojarov, Tatyana Aleksandrovna Khrustaleva, and Larisa Valentinovna Kordyukova
Springer Science and Business Media LLC
Victor Vitoldovich Poboinev, Vladislav Victorovich Khrustalev, Tatyana Aleksandrovna Khrustaleva, Tihon Evgenyevich Kasko, and Vadim Dmitrievich Popkov
Springer Science and Business Media LLC
Anastasia Aleksandrovna Akunevich, Vladislav Victorovich Khrustalev, Tatyana Aleksandrovna Khrustaleva, Victor Vitoldovich Poboinev, Nikolai Vladimirovich Shalygo, Aleksander Nicolaevich Stojarov, Alexander Migranovich Arutyunyan, Larisa Valentinovna Kordyukova, and Yehor Gennadyevich Sapon
Springer Science and Business Media LLC
An interplay between monomeric and dimeric forms of human epidermal growth factor (EGF) affecting its interaction with EGF receptor (EGFR) is poorly understood. While EGF dimeric structure was resolved at pH 8.1, the possibility of EGF dimerization under physiological conditions is still unclear. This study aimed to describe the oligomeric state of EGF in a solution at physiological pH value. With centrifugal ultrafiltration followed by blue native gel electrophoresis, we showed that synthetic human EGF in a solution at a concentration of 0.1 mg/ml exists mainly in the dimeric form at pH 7.4 and temperature of 37 °C, although a small fraction of its monomers was also observed. Based on bioinformatics predictions, we introduced the D46G substitution to examine if EGF C-terminal part is directly involved in the intermolecular interface formation of the observed dimers. We found a reduced ability of the resulting EGF D46G dimers to dissociate at temperatures up to 50 °C. The D46G substitution also increased the intermolecular antiparallel β-structure content within the EGF peptide in a solution according to the CD spectra analysis that was confirmed by HATR-FTIR results. Additionally, the energy transfer between Tyr and Trp residues was detected by fluorescence spectroscopy for the EGF D46G mutant, but not for the native EGF. This allowed us to suggest the elongation and rearrangement of the intermolecular β-structure that leads to the observed stabilization of EGF D46G dimers. The results imply EGF dimerization under physiological pH value and temperature and the involvement of EGF C-terminal part in this process.
Vladislav V. Khrustalev, Larisa V. Kordyukova, Alexander M. Arutyunyan, Victor V. Poboinev, Tatyana A. Khrustaleva, Aleksander N. Stojarov, Lyudmila A. Baratova, Alena S. Sapon, and Valery G. Lugin
Informa UK Limited
Influenza A/H1N1 virus hemagglutinin (HA) is an integral type I glycoprotein that contains a large glycosylated ectodomain, a transmembrane domain, and a cytoplasmic tail (CT) of 10-14 amino acid residues. There are absolutely no data on the secondary or tertiary structure of the HA CT, which is important for virus pathogenesis. Three highly conserved cysteines are post-translationally modified by the attachment of fatty acid residues that pin the CT to the lipid membrane inside the virion. We applied circular dichroism (CD) and fluorescence spectroscopy analysis to examine four synthetic peptides corresponding to 14-15 C-terminal residues of H1 subtype HA (NH2-WMCSNGSLQCRICI-COOH; NH2-FWMCSNGSLQCRICI-COOH), with free or acetaminomethylated cysteines, in the reduced or non-reduced state, at various pH values and temperatures. The CD analysis detected the formation of a β-structure (30-65% according to the new BeStSel algorithm), in addition to an unstructured random coil, in every peptide in various conditions. It was completely or partially recognized as an antiparallel β-structure that was also confirmed by the multi-bounce Horizontal Attenuated Total Reflectance Fourier Transformed Infrared (HATR-FTIR) spectroscopy analysis. According to the experimental data, as well as 3 D modeling, we assume that the amino acid sequence corresponding to the HA CT may form a short antiparallel β-structure under the lipid membrane within a virion. Communicated by Ramaswamy H. Sarma.
Khrustalev Vladislav Victorovich, Khrustaleva Tatyana Aleksandrovna, Poboinev Victor Vitoldovich, Stojarov Aleksander Nicolaevich, Kordyukova Larisa Valentinovna, and Akunevich Anastasia Aleksandrovna
Elsevier BV
Fluorescence spectra of proteins and peptides are traditionally used to get an information on self-association of proteins and peptides, on their tertiary and quaternary structure. In this study it was shown that there are just three peaks of tryptophan fluorescence (at ∼308, at ∼330, and at ∼360 nm) in rough unsmoothed spectra of fluorescence of pure tryptophan in different solvents that change their heights depending on the polarity of a solvent. Two separate peaks at ∼330 nm and ∼360 nm are especially prominent in the spectrum of human epidermal growth factor. In contrast, in smoothed (either mathematically, or physically) spectra of Trp-containing proteins a single maximum of fluorescence varies between 330 and 360 nm. The theory of tryptophan fluorescence is discussed in light of three discrete peaks existence. A stabilizing hydrogen bond with aromatic system of benzene ring in the excited state is proposed as the cause of emission at ∼360 nm bringing Trp to the destabilized ground state. Emission from the destabilized excited state has a maximum at ∼330 nm if the ground state is destabilized, as well as if both states are stabilized. If the excited state is destabilized, while the ground state is stabilized by purely hydrophobic interactions, emitted light should have a maximum at ∼308 nm. The degree of hydrophilicity of tryptophan microenvironment is proposed to be measured as the ratio between the peak at 360 nm and the peak at 330 nm if the observed shifts are not "horizontal", but "vertical". The process of dissociation of hemagglutinin trimers from pandemic Influenza A(H1N1) virus is described as an example of the advantages of the proposed method.
V. V. Poboinev, V. V. Khrustalev, A. N. Stojarov, and T. A. Khrustaleva
Publishing House Belorusskaya Nauka
In this article we analyze the bilirubin binding sites of human serum albumin from the point of view of the secondary structure instability, as well as the effect of amino acid substitutions caused by radiation exposure on the ability of albumin to bind bilirubin-IX-alpha. Based on calculations of binding energy and inhibition constants of bilirubin-albumin complexes before and after the amino acid substitutions, it was found that amino acid substitutions have different effects on the ability of human serum albumin to bind bilirubin. Amino acid substitutions Asp269-Gly269 (Nagasaki-1), Glu354-Lys354 (Hiroshima-1), Asp375-Asn375 (Nagasaki-2) reduce the binding free energy of bilirubin with human serum albumin, and the amino acid substitutions His3-Gln3 (Nagasaki-3) and Glu382-Lys382 (Hiroshima-2) increase it during molecular docking with the corresponding areas of the protein surface. The inhibition constants are significantly higher than with known binding sites. In general, mutations caused by radiation exposure cannot effect on bilirubin binding sites of human serum albumin, since the amino acid residues that are replaced do not interact with the amino acid residues from the binding sites (Leu115, Arg117, Phe134, Tyr138, Ile142, Phe149, Phe157, Tyr161, Arg186, Lys190, Lys240, Arg222). All amino acid residues from known binding sites are located in stable elements of the secondary structure of human serum albumin.The data obtained are important for understanding the impact of radiation exposure on the development of bilirubin encephalopathy in the population of the Chernobyl region and Japan.
Vladislav Victorovich Khrustalev, Rajanish Giri, Tatyana Aleksandrovna Khrustaleva, Shivani Krishna Kapuganti, Aleksander Nicolaevich Stojarov, and Victor Vitoldovich Poboinev
Frontiers Media SA
Larisa V. Kordyukova, Ramil R. Mintaev, Artyom A. Rtishchev, Marina S. Kunda, Natalia N. Ryzhova, Sergei S. Abramchuk, Marina V. Serebryakova, Vladislav V. Khrustalev, Tatyana A. Khrustaleva, Victor V. Poboinev,et al.
Cambridge University Press (CUP)
AbstractInfluenza A virus is a serious human pathogen that assembles enveloped virions on the plasma membrane of the host cell. The pleiomorphic morphology of influenza A virus, represented by spherical, elongated, or filamentous particles, is important for the spread of the virus in nature. Using fixative protocols for sample preparation and negative staining electron microscopy, we found that the recombinant A/WSN/33 (H1N1) (rWSN) virus, a strain considered to be strictly spherical, may produce filamentous particles when amplified in the allantoic cavity of chicken embryos. In contrast, the laboratory WSN strain and the rWSN virus amplified in Madin–Darby canine kidney cells exhibited a spherical morphology. Next-generation sequencing (NGS) suggested a rare Ser126Cys substitution in the M1 protein of rWSN, which was confirmed by the mass spectrometric analysis. No structurally relevant substitutions were found by NGS in other proteins of rWSN. Bioinformatics algorithms predicted a neutral structural effect of the Ser126Cys mutation. The mrWSN_M1_126S virus generated after the introduction of the reverse Cys126Ser substitution exhibited a similar host-dependent partially filamentous phenotype. We hypothesize that a shortage of some as-yet-undefined cellular components involved in virion budding and membrane scission may result in the appearance of filamentous particles in the case of usually “nonfilamentous” virus strains.
M. A. Yermalovich, V. V. Khrustalev, T. A. Khrustaleva, V. V. Poboinev, and E. O. Samoilovich
Publishing House Belorusskaya Nauka
Two genovariants (1a1 and 1a2) are distinguished among Human parvovirus B19 (B19P) of subgenotype 1a, of which 1a2 was predominantly distributed during the incidence rise in Belarus. The aim of this study was a comparative analysis of the amino acid variability and of the mutational pressure directions in different parts of the genome between genovariants 1a1 and 1a2.The analysis of the consensus amino acid sequences of two genovariants and the three-dimensional structure models of protein fragments was carried out. In total, two unique amino acid substitutions in the main non-structural protein NS1 of 1a2 were found (I181M and E114G), one of which E114G is close to the DNA-binding domain (OBD) responsible for attachment to the replication origin site and can affect the rate of virus replication and transcription. Three unique amino acid substitutions were found in the structural polypeptide VP of 1a2: V30L, S98N, and N533S. Two of them are located in the most immunogenic region VP1u and can contribute to the escape from immune response. The investigation of the mutational pressure direction revealed a decrease in the frequency of G to T transversions in the second reading frame of 1a2, which reflects a higher transcription rate as a result of amino acid substitution in the OBD protein.The differences revealed between the genetic variants of subgenotype 1a B19P both in the antigenic sites and in the replication and transcription system can provide an increased “fitness” for the genetic variant 1a2 and explain its predominant distribution during the incidence rise.
Vladislav Victorovich Khrustalev, Tatyana Aleksandrovna Khrustaleva, Victor Vitoldovich Poboinev, Carolina Igorevna Karchevskaya, Elizaveta Aleksandrovna Shablovskaya, and Tatyana Germanovna Terechova
Royal Society of Chemistry (RSC)
Herein, a set of non-homologous proteins (238) that could bind the cobalt(ii) cations was selected from all the available Protein Data Bank structures with Co2+ cations.
Vladislav Victorovich Khrustalev, Victor Vitoldovich Poboinev, Aleksander Nicolaevich Stojarov, and Tatyana Aleksandrovna Khrustaleva
Springer Science and Business Media LLC
Vladislav Victorovich Khrustalev, Tatyana Aleksandrovna Khrustaleva, Victor Vitoldovich Poboinev, and Konstantin Vyachislavovich Yurchenko
Elsevier BV
Vladislav Victorovich Khrustalev, Tatyana Aleksandrovna Khrustaleva, and Victor Vitoldovich Poboinev
Elsevier BV
Vladislav Victorovich Khrustalev, Tatyana Aleksandrovna Khrustaleva, Kamil Szpotkowski, Victor Vitoldovich Poboinev, and Katsiaryna Yurieuna Kakhanouskaya
Wiley