Богданов Иван Владимирович
Кандидат химических наук
Научный сотрудник (Отдел «Учебно-научный центр»)
Эл. почта: email@example.com
Премии и заслуги
- Медаль лауреата конкурса молодых ученых Шестого Московского международного конгресса «Биотехнология: состояние и перспективы развития» за работу «Биотехнологический способ получения тотально меченного стабильными изотопами липид-транспортирующего белка чечевицы» в 2011 г.
- Медаль лауреата конкурса молодых ученых международной научно-практической конференции «Фармацевтические и медицинские биотехнологии» за работу «Получение и характеристика рекомбинантных изоформ липид-транспортирующего белка чечевицы» в 2012 г.
- Победитель конкурса (II место) молодых ученых Седьмого Московского международного конгресса «Биотехнология: состояние и перспективы развития» с работой: «Выделение и структурная характеристика новых растительных аллергенов класса LTP» в 2013 г.
- Победитель конкурса (III место) молодых ученых Международной конференции по биоорганической химии, биотехнологии и бионанотехнологии с работой: «Новый липид-транспортирующий белок из гороха Pisum sativum» в 2014 г.
- Победитель осеннего финала программы «У.М.Н.И.К.» РАН с работой: «Конструирование панели рекомбинантных аналогов клинически значимых растительных аллергенов с целью создания биочипа для компонентной аллергодиагностики и аллерговакцин для аллерген-специфической иммунотерапии» в 2015 г.
Членство в научных обществах
Член Совета молодых Ученых ИБХ РАН второго созыва с 2014 г. и третьего созыва с 2016 г.
- (2016). Plant pathogenesis-related proteins PR-10 and PR-14 as components of innate immunity system and ubiquitous allergens. Curr. Med. Chem. , [+]
Pathogenesis-related (PR) proteins are components of innate immunity system in plants. They play an important role in plant defense against pathogens. Lipid transfer proteins (LTPs) and Bet v 1 homologues comprise two separate families of PR-proteins. Both LTPs (PR-14) and Bet v 1 homologues (PR-10) are multifunctional small proteins involving in plant response to abiotic and biotic stress conditions. The representatives of these PR-protein families do not show any sequence similarity but have other common biochemical features such as low molecular masses, the presence of hydrophobic cavities, ligand binding properties, and antimicrobial activities. Besides, many members of PR-10 and PR-14 families are ubiquitous plant panallergens which are able to cause sensitization of human immune system and cross-reactive allergic reactions to plant food and pollen. This review is aimed at comparative analysis of structure-functional and allergenic properties of the PR-10 and PR-14 families, as well as prospects for their medicinal application.ID:1660
- (2016). A novel lipid transfer protein from the pea Pisum sativum: isolation, recombinant expression, solution structure, antifungal activity, lipid binding, and allergenic properties. BMC Plant Biol. 16 (1), 107 [+]
Plant lipid transfer proteins (LTPs) assemble a family of small (7-9 kDa) ubiquitous cationic proteins with an ability to bind and transport lipids as well as participate in various physiological processes including defense against phytopathogens. They also form one of the most clinically relevant classes of plant allergens. Nothing is known to date about correlation between lipid-binding and IgE-binding properties of LTPs. The garden pea Pisum sativum is widely consumed crop and important allergenic specie of the legume family. This work is aimed at isolation of a novel LTP from pea seeds and characterization of its structural, functional, and allergenic properties.ID:1507
- (2016). Lipid Transfer Proteins As Components of the Plant Innate Immune System: Structure, Functions, and Applications. Acta Naturae 8 (2), 47–61 [+]
Among a variety of molecular factors of the plant innate immune system, small proteins that transfer lipids and exhibit a broad spectrum of biological activities are of particular interest. These are lipid transfer proteins (LTPs). LTPs are interesting to researchers for three main features. The first feature is the ability of plant LTPs to bind and transfer lipids, whereby these proteins got their name and were combined into one class. The second feature is that LTPs are defense proteins that are components of plant innate immunity. The third feature is that LTPs constitute one of the most clinically important classes of plant allergens. In this review, we summarize the available data on the plant LTP structure, biological properties, diversity of functions, mechanisms of action, and practical applications, emphasizing their role in plant physiology and their significance in human life.ID:1536
- (2015). Structural and Functional Characterization of Recombinant Isoforms of the Lentil Lipid Transfer Protein. Acta Naturae 7 (3), 65–73 [+]
The recombinant isoforms Lc-LTP1 and Lc-LTP3 of the lentil lipid transfer protein were overexpressed in E. coli cells. It was confirmed that both proteins are stabilized by four disulfide bonds and characterized by a high proportion of the α-helical structure. It was found that Lc-LTP1 and Lc-LTP3 possess antimicrobial activity and can bind fatty acids. Both isoforms have the ability to bind specific IgE from sera of patients with food allergies, which recognize similar epitopes of the major peach allergen Pru p 3. Both isoforms were shown to have immunological properties similar to those of other plant allergenic LTPs, but Lc-LTP3 displayed a less pronounced immunoreactivity.ID:1315
- (2013). Recombinant production and solution structure of lipid transfer protein from lentil Lens culinaris. Biochem. Biophys. Res. Commun. 439 (4), 427–32 [+]
Lipid transfer protein, designated as Lc-LTP2, was isolated from seeds of the lentil Lens culinaris. The protein has molecular mass 9282.7Da, consists of 93 amino acid residues including 8 cysteines forming 4 disulfide bonds. Lc-LTP2 and its stable isotope labeled analogues were overexpressed in Escherichia coli and purified. Antimicrobial activity of the recombinant protein was examined, and its spatial structure was studied by NMR spectroscopy. The polypeptide chain of Lc-LTP2 forms four α-helices (Cys4-Leu18, Pro26-Ala37, Thr42-Ala56, Thr64-Lys73) and a long C-terminal tail without regular secondary structure. Side chains of the hydrophobic residues form a relatively large internal tunnel-like lipid-binding cavity (van der Waals volume comes up to ∼600Å(3)). The side-chains of Arg45, Pro79, and Tyr80 are located near an assumed mouth of the cavity. Titration with dimyristoyl phosphatidylglycerol (DMPG) revealed formation of the Lc-LTP2/lipid non-covalent complex accompanied by rearrangements in the protein spatial structure and expansion of the internal cavity. The resultant Lc-LTP2/DMPG complex demonstrates limited lifetime and dissociates within tens of hours.ID:979