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<article article-type="research-article" dtd-version="1.3" xmlns:mml="http://www.w3.org/1998/Math/MathML" xmlns:xlink="http://www.w3.org/1999/xlink" xmlns:xsi="http://www.w3.org/2001/XMLSchema-instance" xml:lang="ru"><front><journal-meta><journal-id journal-id-type="publisher-id">microbe</journal-id><journal-title-group><journal-title xml:lang="ru">Проблемы особо опасных инфекций</journal-title><trans-title-group xml:lang="en"><trans-title>Problems of Particularly Dangerous Infections</trans-title></trans-title-group></journal-title-group><issn pub-type="ppub">0370-1069</issn><issn pub-type="epub">2658-719X</issn><publisher><publisher-name>Russian Research Anti-Plague Institute “Microbe”</publisher-name></publisher></journal-meta><article-meta><article-id pub-id-type="doi">10.21055/0370-1069-2026-1-123-128</article-id><article-id custom-type="elpub" pub-id-type="custom">microbe-2291</article-id><article-categories><subj-group subj-group-type="heading"><subject>Research Article</subject></subj-group><subj-group subj-group-type="section-heading" xml:lang="ru"><subject>ОРИГИНАЛЬНЫЕ СТАТЬИ</subject></subj-group><subj-group subj-group-type="section-heading" xml:lang="en"><subject>ORIGINAL ARTICLES</subject></subj-group></article-categories><title-group><article-title>Оценка значимости коллагена и фибронектина позвоночных в адгезии Yersinia pseudotuberculosis и Yersinia pestis с использованием оптической ловушки</article-title><trans-title-group xml:lang="en"><trans-title>Assessing the Siginificance of Vertebrate Collagen and Fibronectin in Adhesion of Yersinia pseudotuberculosis and Yersinia pestis Using an Optical Trap</trans-title></trans-title-group></title-group><contrib-group><contrib contrib-type="author" corresp="yes"><contrib-id contrib-id-type="orcid">https://orcid.org/0000-0001-6575-9630</contrib-id><name-alternatives><name name-style="eastern" xml:lang="ru"><surname>Конышев</surname><given-names>И. В.</given-names></name><name name-style="western" xml:lang="en"><surname>Konyshev</surname><given-names>I. V.</given-names></name></name-alternatives><bio xml:lang="ru"><p>167982, Республика Коми, Сыктывкар, ГСП-2, ул. Коммунистическая, 24; 610000, Киров, ул. Московская, 36</p></bio><bio xml:lang="en"><p>24, Kommunisticheskaya St., Syktyvkar, Komi Republic, 167982; 36, Moskovskaya St., Kirov, 610000</p></bio><email xlink:type="simple">info@vyatsu.ru</email><xref ref-type="aff" rid="aff-1"/></contrib><contrib contrib-type="author" corresp="yes"><contrib-id contrib-id-type="orcid">https://orcid.org/0000-0002-2172-9015</contrib-id><name-alternatives><name name-style="eastern" xml:lang="ru"><surname>Дудина</surname><given-names>Л. Г.</given-names></name><name name-style="western" xml:lang="en"><surname>Dudina</surname><given-names>L. G.</given-names></name></name-alternatives><bio xml:lang="ru"><p>167982, Республика Коми, Сыктывкар, ГСП-2, ул. Коммунистическая, 24; 610000, Киров, ул. Московская, 36</p></bio><bio xml:lang="en"><p>24, Kommunisticheskaya St., Syktyvkar, Komi Republic, 167982; 36, Moskovskaya St., Kirov, 610000</p></bio><email xlink:type="simple">info@vyatsu.ru</email><xref ref-type="aff" rid="aff-1"/></contrib><contrib contrib-type="author" corresp="yes"><contrib-id contrib-id-type="orcid">https://orcid.org/0000-0003-1117-5896</contrib-id><name-alternatives><name name-style="eastern" xml:lang="ru"><surname>Бывалов</surname><given-names>А. А.</given-names></name><name name-style="western" xml:lang="en"><surname>Byvalov</surname><given-names>A. A.</given-names></name></name-alternatives><bio xml:lang="ru"><p>Бывалов Андрей Анатольевич</p><p>167982, Республика Коми, Сыктывкар, ГСП-2, ул. Коммунистическая, 24; 610000, Киров, ул. Московская, 36</p></bio><bio xml:lang="en"><p>Andrey A. Byvalov</p><p>24, Kommunisticheskaya St., Syktyvkar, Komi Republic, 167982; 36, Moskovskaya St., Kirov, 610000</p></bio><email xlink:type="simple">byvalov@nextmail.ru</email><xref ref-type="aff" rid="aff-1"/></contrib></contrib-group><aff-alternatives id="aff-1"><aff xml:lang="ru"><institution>Институт физиологии Коми научного центра Уральского отделения Российской академии наук; Вятский государственный университет</institution><country>Россия</country></aff><aff xml:lang="en"><institution>Institute of Physiology, Komi Scientific Center of the Ural Branch of the Russian Academy of Sciences; Vyatka State University</institution><country>Russian Federation</country></aff></aff-alternatives><pub-date pub-type="collection"><year>2026</year></pub-date><pub-date pub-type="epub"><day>30</day><month>03</month><year>2026</year></pub-date><volume>0</volume><issue>1</issue><fpage>123</fpage><lpage>128</lpage><permissions><copyright-statement>Copyright &amp;#x00A9; Конышев И.В., Дудина Л.Г., Бывалов А.А., 2026</copyright-statement><copyright-year>2026</copyright-year><copyright-holder xml:lang="ru">Конышев И.В., Дудина Л.Г., Бывалов А.А.</copyright-holder><copyright-holder xml:lang="en">Konyshev I.V., Dudina L.G., Byvalov A.A.</copyright-holder><license xml:lang="ru" license-type="creative-commons-attribution" xlink:href="https://creativecommons.org/licenses/by/4.0/" xlink:type="simple"><license-p>Данная работа распространяется под лицензией Creative Commons Attribution 4.0.</license-p></license><license xml:lang="en" license-type="creative-commons-attribution" xlink:href="https://creativecommons.org/licenses/by/4.0/" xlink:type="simple"><license-p>This work is licensed under a Creative Commons Attribution 4.0 License.</license-p></license></permissions><self-uri xlink:href="https://journal.microbe.ru/jour/article/view/2291">https://journal.microbe.ru/jour/article/view/2291</self-uri><abstract><p>В настоящее время большое внимание уделяется изучению механизмов адгезии патогенов к клеткам и тканям человека. Наряду со стандартными микробиологическими техниками с этой целью широко применяются современные биофизические методы, среди которых особое место занимает оптическая ловушка, позволяющая захватывать и перемещать отдельные бактериальные клетки с измерением силы связи между ними и целевыми молекулами. Цель работы состояла в оценке значимости коллагена и фибронектина в адгезии клеток Yersinia pseudotuberculosis O1b и вакцинного штамма Yersinia pestis EV НИИЭГ, выращенных при разной температуре, с использованием оптической ловушки. Материалы и методы. Бактерии, выращенные при двух температурах (+10 и +37 °С для клеток Y. pseudotuberculosis и +27 и +37 °С для клеток Y. pestis), захватывали лазерным лучом и пошагово подводили к стеклянным подложкам, обработанным целевыми белками. Спустя одну секунду после контакта клетку отводили в полуавтоматическом режиме с постоянной скоростью до наблюдения резкого скачка на хронограмме сигнала, величину которого пересчитывали в единицы силы. Различия между массивами данных определялись по средним и медианным силам, а также по результатам построения гистограмм распределения сил взаимодействия. Результаты и обсуждение. Показана значимость коллагена в адгезии бактерий Y. pseudotuberculosis, выращенных при +37 °С, но не при +10 °С. При работе с фибронектином не выявлено выраженных отличий между бактериями двух видов иерсиний при всех использованных температурных режимах их выращивания. Во всех случаях взаимодействие клеток иерсиний с коллагеном и фибронектином оказалось более прочным по сравнению с контролем (бычьим сывороточным альбумином): соответствующие значения силы связи составили 7,2, 8,1 и 2,0 пН для клеток 1b-10; 12,4, 7,6 и 4,7 пН для клеток 1b-37; 6,1, 6,6 и 4,4 пН для клеток EV-27; 7,4, 7,3 и 4,3 пН для клеток EV-37. Взаимодействие клеток иерсиний с обоими белками, вероятно, обусловлено физико-химическими свойствами поверхностных структур бактерий и компонентов соединительной ткани, а также условиями проведения экспериментов. Выявление механизмов таких взаимодействий требует постановки дополнительных опытов с использованием индивидуальных антигенов иерсиний, нанесенных на полистирольные микросферы. Использованные методические подходы могут быть востребованы при работе с другими патогенами.</p></abstract><trans-abstract xml:lang="en"><p>Currently, much attention is paid to the study of mechanisms of pathogen adhesion to human cells and tissues. Along with standard microbiological techniques, advanced biophysical methods are widely used for this purpose, among which a special place is occupied by optical trapping, which allows catching and moving individual bacterial cells with measurement of the interaction force between them and target molecules. The aim of this work was to evaluate the significance of collagen and fibronectin in adhesion of Yersinia pseudotuberculosis O1b and the vaccine strain Yersinia pestis EV NIIEG, cultivated at different temperatures, applying optical trap. Materials and methods. Bacteria grown at two temperatures (+10 and +37 °C for Y. pseudotuberculosis or +27 and +37 °C for Y. pestis) were caught by a laser beam and stepwise brought to the protein-coated glass. One second after the contact, the cell was retracted in semi-automatic mode at a constant speed until a spike was observed on the signal chronogram, and its voltage then was converted into force units. Differences between data sets were determined by the mean and median forces, as well as by the results of constructing histograms of the distribution of interaction forces. Results and discussion. The significance of collagen in the adhesion of Y. pseudotuberculosis grown at +37 °C but not at +10 °C was shown. Fibronectin demonstrated no pronounced differences between the bacteria of the two Yersinia species at all the cultivation temperature modes. In all cases, affinity of Yersinia cells with collagen and fibronectin was higher compared to the control, bovine serum albumin: 7.2, 8.1, and 2.0 pN for 1b-10 cells; 12.4, 7.6, and 4.7 pN for 1b-37 cells; 6.1, 6.6, and 4.4 pN for EV-27 cells; 7.4, 7.3, and 4.3 pN for EV-37 cells, respectively. The binding of Yersinia to collagen and fibronectin is probably due to the physicochemical properties of the bacterial surface structures and components of connective tissue, as well as experimental conditions. Revealing the mechanisms of such interactions requires additional investigations of individual Yersinia antigens applied onto polystyrene beads. The method may be introduced when working with other pathogens too.</p></trans-abstract><kwd-group xml:lang="ru"><kwd>адгезия</kwd><kwd>Yersinia</kwd><kwd>лазерная ловушка</kwd><kwd>коллаген</kwd><kwd>фибронектин</kwd><kwd>сила взаимодействия</kwd></kwd-group><kwd-group xml:lang="en"><kwd>adhesion</kwd><kwd>Yersinia</kwd><kwd>laser trap</kwd><kwd>collagen</kwd><kwd>fibronectin</kwd><kwd>interaction force</kwd></kwd-group><funding-group><funding-statement xml:lang="ru">Авторы заявляют об отсутствии дополнительного финансирования при проведении данного исследования</funding-statement><funding-statement xml:lang="en">The authors declare no additional financial support for this study</funding-statement></funding-group></article-meta></front><back><ref-list><title>References</title><ref id="cit1"><label>1</label><citation-alternatives><mixed-citation xml:lang="ru">Zhao A., Sun J., Liu Y. Understanding bacterial biofilms: From definition to treatment strategies. Front. Cell. Infect. Microbiol. 2023; 13:1137947. DOI: 10.3389/fcimb.2023.1137947.</mixed-citation><mixed-citation xml:lang="en">Zhao A., Sun J., Liu Y. Understanding bacterial biofilms: From definition to treatment strategies. Front. Cell. Infect. Microbiol. 2023; 13:1137947. DOI: 10.3389/fcimb.2023.1137947.</mixed-citation></citation-alternatives></ref><ref id="cit2"><label>2</label><citation-alternatives><mixed-citation xml:lang="ru">Osei-Owusu P., Charlton T.M., Kim H.K., Missiakas D., Schneewind O. FPR1 is the plague receptor on host immune cells. Nature. 2019; 574:57–62. DOI: 10.1038/s41586-019-1570-z.</mixed-citation><mixed-citation xml:lang="en">Osei-Owusu P., Charlton T.M., Kim H.K., Missiakas D., Schneewind O. FPR1 is the plague receptor on host immune cells. Nature. 2019; 574:57–62. DOI: 10.1038/s41586-019-1570-z.</mixed-citation></citation-alternatives></ref><ref id="cit3"><label>3</label><citation-alternatives><mixed-citation xml:lang="ru">LaFoya B., Munroe J.A., Miyamoto A., Detweiler M.A., Crow J.J., Gazdik T., Albig A.R. Beyond the matrix: the many non-ECM ligands for integrins. Int. J. Mol. Sci. 2018; 19(2):449. DOI: 10.3390/ijms19020449.</mixed-citation><mixed-citation xml:lang="en">LaFoya B., Munroe J.A., Miyamoto A., Detweiler M.A., Crow J.J., Gazdik T., Albig A.R. Beyond the matrix: the many non-ECM ligands for integrins. Int. J. Mol. Sci. 2018; 19(2):449. DOI: 10.3390/ijms19020449.</mixed-citation></citation-alternatives></ref><ref id="cit4"><label>4</label><citation-alternatives><mixed-citation xml:lang="ru">Santos A.L., Preta G. Lipids in the cell: organization regulates function. Cell. Mol. Life Sci. 2018; 75(11):1909–27. DOI: 10.1007/s00018-018-2765-4.</mixed-citation><mixed-citation xml:lang="en">Santos A.L., Preta G. Lipids in the cell: organization regulates function. Cell. Mol. Life Sci. 2018; 75(11):1909–27. DOI: 10.1007/s00018-018-2765-4.</mixed-citation></citation-alternatives></ref><ref id="cit5"><label>5</label><citation-alternatives><mixed-citation xml:lang="ru">Dzobo K., Dandara C. The extracellular matrix: its composition, function, remodeling, and role in tumorigenesis. Biomimetics (Basel). 2023; 8(2):146. DOI: 10.3390/biomimetics8020146.</mixed-citation><mixed-citation xml:lang="en">Dzobo K., Dandara C. The extracellular matrix: its composition, function, remodeling, and role in tumorigenesis. Biomimetics (Basel). 2023; 8(2):146. DOI: 10.3390/biomimetics8020146.</mixed-citation></citation-alternatives></ref><ref id="cit6"><label>6</label><citation-alternatives><mixed-citation xml:lang="ru">Sekiguchi R., Yamada K.M. Basement membranes in development and disease. Curr. Top. Dev. Biol. 2018; 130:143–91. DOI: 10.1016/bs.ctdb.2018.02.005.</mixed-citation><mixed-citation xml:lang="en">Sekiguchi R., Yamada K.M. Basement membranes in development and disease. Curr. Top. Dev. Biol. 2018; 130:143–91. DOI: 10.1016/bs.ctdb.2018.02.005.</mixed-citation></citation-alternatives></ref><ref id="cit7"><label>7</label><citation-alternatives><mixed-citation xml:lang="ru">Tvaroška I. Glycosylation modulates the structure and functions of collagen: a review. Molecules. 2024; 29(7):1417. DOI: 10.3390/molecules29071417.</mixed-citation><mixed-citation xml:lang="en">Tvaroška I. Glycosylation modulates the structure and functions of collagen: a review. Molecules. 2024; 29(7):1417. DOI: 10.3390/molecules29071417.</mixed-citation></citation-alternatives></ref><ref id="cit8"><label>8</label><citation-alternatives><mixed-citation xml:lang="ru">Singh B., Fleury C., Jalalvand F., Riesbeck K. Human pathogens utilize host extracellular matrix proteins laminin and collagen for adhesion and invasion of the host. FEMS Microbiol. Rev. 2012; 36(6):1122–80. DOI: 10.1111/j.1574-6976.2012.00340.x.</mixed-citation><mixed-citation xml:lang="en">Singh B., Fleury C., Jalalvand F., Riesbeck K. Human pathogens utilize host extracellular matrix proteins laminin and collagen for adhesion and invasion of the host. FEMS Microbiol. Rev. 2012; 36(6):1122–80. DOI: 10.1111/j.1574-6976.2012.00340.x.</mixed-citation></citation-alternatives></ref><ref id="cit9"><label>9</label><citation-alternatives><mixed-citation xml:lang="ru">Bachman H., Nicosia J., Dysart M., Barker T.H. Utilizing fibronectin integrin-binding specificity to control cellular responses. Adv. Wound Care (New Rochelle). 2015; 4(8):501–11. DOI: 10.1089/wound.2014.0621.</mixed-citation><mixed-citation xml:lang="en">Bachman H., Nicosia J., Dysart M., Barker T.H. Utilizing fibronectin integrin-binding specificity to control cellular responses. Adv. Wound Care (New Rochelle). 2015; 4(8):501–11. DOI: 10.1089/wound.2014.0621.</mixed-citation></citation-alternatives></ref><ref id="cit10"><label>10</label><citation-alternatives><mixed-citation xml:lang="ru">Vaca D.J., Thibau A., Schütz M., Kraiczy P., Happonen L., Malmström J., Kempf V.A.J. Interaction with the host: the role of fibronectin and extracellular matrix proteins in the adhesion of Gramnegative bacteria. Med. Microbiol. Immunol. 2020; 209(3):277–99. DOI: 10.1007/s00430-019-00644-3.</mixed-citation><mixed-citation xml:lang="en">Vaca D.J., Thibau A., Schütz M., Kraiczy P., Happonen L., Malmström J., Kempf V.A.J. Interaction with the host: the role of fibronectin and extracellular matrix proteins in the adhesion of Gramnegative bacteria. Med. Microbiol. Immunol. 2020; 209(3):277–99. DOI: 10.1007/s00430-019-00644-3.</mixed-citation></citation-alternatives></ref><ref id="cit11"><label>11</label><citation-alternatives><mixed-citation xml:lang="ru">Chen H.D., Ge K.K., Li Y.M., Wu J.G., Gu Y.Q., Wei H.M., Tian Z.G. Application of optical tweezers in the research of molecular interaction between lymphocyte function associated antigen-1 and its monoclonal antibody. Cell. Mol. Immunol. 2007; 4(3):221–5.</mixed-citation><mixed-citation xml:lang="en">Chen H.D., Ge K.K., Li Y.M., Wu J.G., Gu Y.Q., Wei H.M., Tian Z.G. Application of optical tweezers in the research of molecular interaction between lymphocyte function associated antigen-1 and its monoclonal antibody. Cell. Mol. Immunol. 2007; 4(3):221–5.</mixed-citation></citation-alternatives></ref><ref id="cit12"><label>12</label><citation-alternatives><mixed-citation xml:lang="ru">Bustamante C.J., Chemla Y.R., Liu S., Wang M.D. Optical tweezers in single-molecule biophysics. Nat. Rev. Methods Primers. 2021; 1:25. DOI: 10.1038/s43586-021-00021-6.</mixed-citation><mixed-citation xml:lang="en">Bustamante C.J., Chemla Y.R., Liu S., Wang M.D. Optical tweezers in single-molecule biophysics. Nat. Rev. Methods Primers. 2021; 1:25. DOI: 10.1038/s43586-021-00021-6.</mixed-citation></citation-alternatives></ref><ref id="cit13"><label>13</label><citation-alternatives><mixed-citation xml:lang="ru">Al Azzam O., Watts J.C., Reynolds J.E., Davis J.E., Reinemann D.N. Probing myosin ensemble mechanics in actin filament bundles using optical tweezers. J. Vis. Exp. 2022; (183):e63672. DOI: 10.3791/63672.</mixed-citation><mixed-citation xml:lang="en">Al Azzam O., Watts J.C., Reynolds J.E., Davis J.E., Reinemann D.N. Probing myosin ensemble mechanics in actin filament bundles using optical tweezers. J. Vis. Exp. 2022; (183):e63672. DOI: 10.3791/63672.</mixed-citation></citation-alternatives></ref><ref id="cit14"><label>14</label><citation-alternatives><mixed-citation xml:lang="ru">Gudimchuk N.B., Alexandrova V.V. Measuring and modeling forces generated by microtubules. Biophys. Rev. 2023; 15(5):1095–110. DOI: 10.1007/s12551-023-01161-7.</mixed-citation><mixed-citation xml:lang="en">Gudimchuk N.B., Alexandrova V.V. Measuring and modeling forces generated by microtubules. Biophys. Rev. 2023; 15(5):1095–110. DOI: 10.1007/s12551-023-01161-7.</mixed-citation></citation-alternatives></ref><ref id="cit15"><label>15</label><citation-alternatives><mixed-citation xml:lang="ru">Agrawal R., Smart T., Nobre-Cardoso J., Richards C., Bhatnagar R., Tufail A., Shima D., Jones P.H., Pavesio C. Assessment of red blood cell deformability in type 2 diabetes mellitus and diabetic retinopathy by dual optical tweezers stretching technique. Sci. Rep. 2023; 6:15873. DOI: 10.1038/srep15873.</mixed-citation><mixed-citation xml:lang="en">Agrawal R., Smart T., Nobre-Cardoso J., Richards C., Bhatnagar R., Tufail A., Shima D., Jones P.H., Pavesio C. Assessment of red blood cell deformability in type 2 diabetes mellitus and diabetic retinopathy by dual optical tweezers stretching technique. Sci. Rep. 2023; 6:15873. DOI: 10.1038/srep15873.</mixed-citation></citation-alternatives></ref><ref id="cit16"><label>16</label><citation-alternatives><mixed-citation xml:lang="ru">Altindal T., Chattopadhyay S., Wu X.L. Bacterial chemotaxis in an optical trap. PLoS One. 2011; 6(4):18231. DOI: 10.1371/journal.pone.0018231.</mixed-citation><mixed-citation xml:lang="en">Altindal T., Chattopadhyay S., Wu X.L. Bacterial chemotaxis in an optical trap. PLoS One. 2011; 6(4):18231. DOI: 10.1371/journal.pone.0018231.</mixed-citation></citation-alternatives></ref><ref id="cit17"><label>17</label><citation-alternatives><mixed-citation xml:lang="ru">Konyshev I., Byvalov A. Model systems for optical trapping: the physical basis and biological applications. Biophys. Rev. 2021; 13(4):515–29. DOI: 10.1007/s12551-021-00823-8.</mixed-citation><mixed-citation xml:lang="en">Konyshev I., Byvalov A. Model systems for optical trapping: the physical basis and biological applications. Biophys. Rev. 2021; 13(4):515–29. DOI: 10.1007/s12551-021-00823-8.</mixed-citation></citation-alternatives></ref><ref id="cit18"><label>18</label><citation-alternatives><mixed-citation xml:lang="ru">Munford R.S., Hall C.L., Rick P.D. Size heterogeneity of Salmonella typhimurium lipopolysaccharides in outer membranes and culture supernatant membrane fragments. J. Bacteriol. 1980; 144(2):630–40. DOI: 10.1128/jb.144.2.630-640.1980.</mixed-citation><mixed-citation xml:lang="en">Munford R.S., Hall C.L., Rick P.D. Size heterogeneity of Salmonella typhimurium lipopolysaccharides in outer membranes and culture supernatant membrane fragments. J. Bacteriol. 1980; 144(2):630–40. DOI: 10.1128/jb.144.2.630-640.1980.</mixed-citation></citation-alternatives></ref><ref id="cit19"><label>19</label><citation-alternatives><mixed-citation xml:lang="ru">Bramkamp M., Lopez D. Exploring the existence of lipid rafts in bacteria. Microbiol. Mol. Biol. Rev. 2015; 79(1):81–100. DOI: 10.1128/MMBR.00036-14.</mixed-citation><mixed-citation xml:lang="en">Bramkamp M., Lopez D. Exploring the existence of lipid rafts in bacteria. Microbiol. Mol. Biol. Rev. 2015; 79(1):81–100. DOI: 10.1128/MMBR.00036-14.</mixed-citation></citation-alternatives></ref><ref id="cit20"><label>20</label><citation-alternatives><mixed-citation xml:lang="ru">Dabirmanesh B., Khajeh K., Uversky V.N. Protein aggregation: an overview. Prog. Mol. Biol. Transl. Sci. 2024; 206:1–10. DOI: 10.1016/bs.pmbts.2024.03.007.</mixed-citation><mixed-citation xml:lang="en">Dabirmanesh B., Khajeh K., Uversky V.N. Protein aggregation: an overview. Prog. Mol. Biol. Transl. Sci. 2024; 206:1–10. DOI: 10.1016/bs.pmbts.2024.03.007.</mixed-citation></citation-alternatives></ref><ref id="cit21"><label>21</label><citation-alternatives><mixed-citation xml:lang="ru">Zhang P., Snyder S., Feng P., Azadi P., Zhang S., Bulgheresi S., Sanderson K.E., He J., Klena J., Chen T. Role of N-acetylglucosamine within core lipopolysaccharide of several species of gram-negative bacteria in targeting the DC-SIGN (CD209). J. Immunol. 2006; 177(6):4002–11. DOI: 10.4049/jimmunol.177.6.4002.</mixed-citation><mixed-citation xml:lang="en">Zhang P., Snyder S., Feng P., Azadi P., Zhang S., Bulgheresi S., Sanderson K.E., He J., Klena J., Chen T. Role of N-acetylglucosamine within core lipopolysaccharide of several species of gram-negative bacteria in targeting the DC-SIGN (CD209). J. Immunol. 2006; 177(6):4002–11. DOI: 10.4049/jimmunol.177.6.4002.</mixed-citation></citation-alternatives></ref><ref id="cit22"><label>22</label><citation-alternatives><mixed-citation xml:lang="ru">Yang K., Park C.G., Cheong C., Bulgheresi S., Zhang S., Zhang P., He Y., Jiang L., Huang H., Ding H., Wu Y., Wang S., Zhang L., Li A., Xia L., Bartra S.S., Plano G.V., Skurnik M., Klena J.D., Chen T. Host Langerin (CD207) is a receptor for Yersinia pestis phagocytosis and promotes dissemination. Immunol. Cell. Biol. 2015; 93(9):815–24. DOI: 10.1038/icb.2015.46.</mixed-citation><mixed-citation xml:lang="en">Yang K., Park C.G., Cheong C., Bulgheresi S., Zhang S., Zhang P., He Y., Jiang L., Huang H., Ding H., Wu Y., Wang S., Zhang L., Li A., Xia L., Bartra S.S., Plano G.V., Skurnik M., Klena J.D., Chen T. Host Langerin (CD207) is a receptor for Yersinia pestis phagocytosis and promotes dissemination. Immunol. Cell. Biol. 2015; 93(9):815–24. DOI: 10.1038/icb.2015.46.</mixed-citation></citation-alternatives></ref><ref id="cit23"><label>23</label><citation-alternatives><mixed-citation xml:lang="ru">Zhang P., Skurnik M., Zhang S.S., Schwartz O., Kalyanasundaram R., Bulgheresi S., He J.J., Klena J.D., Hinnebusch B.J., Chen T. Human dendritic cell-specific intercellular adhesion molecule-grabbing nonintegrin (CD209) is a receptor for Yersinia pestis that promotes phagocytosis by dendritic cells. Infect. Immun. 2008; 76(5):2070–9. DOI: 10.1128/IAI.01246-07.</mixed-citation><mixed-citation xml:lang="en">Zhang P., Skurnik M., Zhang S.S., Schwartz O., Kalyanasundaram R., Bulgheresi S., He J.J., Klena J.D., Hinnebusch B.J., Chen T. Human dendritic cell-specific intercellular adhesion molecule-grabbing nonintegrin (CD209) is a receptor for Yersinia pestis that promotes phagocytosis by dendritic cells. Infect. Immun. 2008; 76(5):2070–9. DOI: 10.1128/IAI.01246-07.</mixed-citation></citation-alternatives></ref><ref id="cit24"><label>24</label><citation-alternatives><mixed-citation xml:lang="ru">Nair M.K., De Masi L., Yue M., Galván E.M., Chen H., Wang F., Schifferli D.M. Adhesive properties of YapV and paralogous autotransporter proteins of Yersinia pestis. Infect. Immun. 2015; 83(5):1809–19. DOI: 10.1128/IAI.00094-15.</mixed-citation><mixed-citation xml:lang="en">Nair M.K., De Masi L., Yue M., Galván E.M., Chen H., Wang F., Schifferli D.M. Adhesive properties of YapV and paralogous autotransporter proteins of Yersinia pestis. Infect. Immun. 2015; 83(5):1809–19. DOI: 10.1128/IAI.00094-15.</mixed-citation></citation-alternatives></ref><ref id="cit25"><label>25</label><citation-alternatives><mixed-citation xml:lang="ru">Yamashita S., Lukacik P., Barnard T.J., Noinaj N., Felek S., Tsang T.M., Krukonis E.S., Hinnebusch B.J., Buchanan S.K. Structural insights into Ail-mediated adhesion in Yersinia pestis. Structure. 2011; 19(11):1672–82. DOI: 10.1016/j.str.2011.08.010.</mixed-citation><mixed-citation xml:lang="en">Yamashita S., Lukacik P., Barnard T.J., Noinaj N., Felek S., Tsang T.M., Krukonis E.S., Hinnebusch B.J., Buchanan S.K. Structural insights into Ail-mediated adhesion in Yersinia pestis. Structure. 2011; 19(11):1672–82. DOI: 10.1016/j.str.2011.08.010.</mixed-citation></citation-alternatives></ref></ref-list><fn-group><fn fn-type="conflict"><p>The authors declare that there are no conflicts of interest present.</p></fn></fn-group></back></article>
