<?xml version="1.0" encoding="UTF-8"?>
<!DOCTYPE article PUBLIC "-//NLM//DTD JATS (Z39.96) Journal Publishing DTD v1.3 20210610//EN" "JATS-journalpublishing1-3.dtd">
<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">bloodjour</journal-id><journal-title-group><journal-title xml:lang="ru">Гематология и трансфузиология</journal-title><trans-title-group xml:lang="en"><trans-title>Russian journal of hematology and transfusiology</trans-title></trans-title-group></journal-title-group><issn pub-type="ppub">0234-5730</issn><issn pub-type="epub">2411-3042</issn><publisher><publisher-name>ООО Издательский дом «Практика»</publisher-name></publisher></journal-meta><article-meta><article-id pub-id-type="doi">10.18821/0234-5730-2017-62-4-223-229</article-id><article-id custom-type="elpub" pub-id-type="custom">bloodjour-676</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>ОБЗОРЫ ЛИТЕРАТУРЫ</subject></subj-group><subj-group subj-group-type="section-heading" xml:lang="en"><subject>REVIEWS OF LITERATURE</subject></subj-group></article-categories><title-group><article-title>Морфофункциональная характеристика защитных механизмов  нейтрофилов при бактериальных инфекциях и их вклад в патогенез провоспалительных реакций</article-title><trans-title-group xml:lang="en"><trans-title>Morphofunctional characteristics of protective mechanisms of neutrophils against bacterial infections and their contribution in pathogenesis of pro-inflammatory responses</trans-title></trans-title-group></title-group><contrib-group><contrib contrib-type="author" corresp="yes"><contrib-id contrib-id-type="orcid">https://orcid.org/0000-0001-9968-3347</contrib-id><name-alternatives><name name-style="eastern" xml:lang="ru"><surname>Матосова</surname><given-names>Е. В.</given-names></name><name name-style="western" xml:lang="en"><surname>Matosova</surname><given-names>E. V.</given-names></name></name-alternatives><bio xml:lang="ru"><p>Матосова Екатерина Владимировна, младший научный сотрудник лаборатории молекулярной эпидемиологии и микробиологии</p><p>690087, г. Владивосток</p></bio><bio xml:lang="en"><p>Matosova Ekaterina V., MD, junior researcher of the Laboratory of Molecular Epidemiology and Microbiology</p><p>Vladivostok, 690087</p></bio><email xlink:type="simple">e_matosova@mail.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/0000-0003-4456-808X</contrib-id><name-alternatives><name name-style="eastern" xml:lang="ru"><surname>Андрюков</surname><given-names>Б. Г.</given-names></name><name name-style="western" xml:lang="en"><surname>Andryukov</surname><given-names>B. G.</given-names></name></name-alternatives><bio xml:lang="ru"><p>690087, г. Владивосток</p></bio><bio xml:lang="en"><p>Vladivostok, 690087</p></bio><xref ref-type="aff" rid="aff-1"/></contrib></contrib-group><aff-alternatives id="aff-1"><aff xml:lang="ru"><institution>ФГБНУ «Научно-исследовательский институт эпидемиологии и микробиологии им. Г.П. Сомова»</institution><country>Россия</country></aff><aff xml:lang="en"><institution>Somov Institute of Epidemiology and Microbiology</institution><country>Russian Federation</country></aff></aff-alternatives><pub-date pub-type="collection"><year>2017</year></pub-date><pub-date pub-type="epub"><day>17</day><month>10</month><year>2025</year></pub-date><volume>62</volume><issue>4</issue><fpage>223</fpage><lpage>229</lpage><permissions><copyright-statement>Copyright &amp;#x00A9; Матосова Е.В., Андрюков Б.Г., 2025</copyright-statement><copyright-year>2025</copyright-year><copyright-holder xml:lang="ru">Матосова Е.В., Андрюков Б.Г.</copyright-holder><copyright-holder xml:lang="en">Matosova E.V., Andryukov B.G.</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://www.htjournal.ru/jour/article/view/676">https://www.htjournal.ru/jour/article/view/676</self-uri><abstract><p>Инфекции – одна из основных причин смертности и заболеваемости в мире. Нейтрофилы являются активным и многочисленным эффекторным звеном врождённой иммунной системы, которое защищает организм от инфицирования патогенными микроорганизмами. Однако вклад нейтрофилов в развитие инфекционного процесса был недооценён, несмотря на то, что функции этого подкласса лейкоцитов давно известны в качестве патогенетического элемента воспаления. В дополнение к фагоцитозу эти клетки могут опосредовать менее изученную в качестве антибактериальной стратегии внеклеточную дегрануляцию, а также, высвобождая внеклеточный хроматин, ядерный белок и сериновые протеазы, образовывать сетчатые волоконные структуры, называемые нейтрофильными внеклеточными ловушками (Neutrophil Extracellular Traps – NETs). NETs могут захватывать патогены, вызывать эндотелиальную дисфункцию и провоспалительные иммунные реакции. Феномен NETs – это сравнительно новая форма программируемой клеточной смерти (нетоз), значение которой в развитии инфекционного процесса и развитии воспаления до конца не изучено. Нетоз имеет высокий потенциал для дальнейшего изучения патогенеза воспаления и поиска эффективных методов лечения инфекций. В этом обзоре основное внимание уделяется современным данным об основных защитных стратегиях нейтрофилов при бактериальных инфекциях и их вкладу в патогенез провоспалительных реакций. Обсуждаются современные подходы к фармакологической модуляции различных вариантов антимикробных механизмов нейтрофилов, что перспективно в случаях комплексного лечения инфекций, ассоциированных с антибиотикорезистентными штаммами бактерий.</p></abstract><trans-abstract xml:lang="en"><p>Infection is one of the leading causes of the mortality and morbidity. Neutrophils protect the body against pathogenic microorganisms. However, the contribution of neutrophils in the development of the infectious process was underestimated. In addition to phagocytosis, neutrophils can mediate extracellular degranulation, release of  extracellular chromatin, nuclear protein and serine proteases and form neutrophil extracellular traps NETs. NETs can capture pathogens, cause endothelial dysfunction and pro-inflammatory immune responses. The phenomenon of NETs is a relatively new form of programmed cell death (NETosis). NETosis has a high potential for the further study of the pathogenesis of inflammation and the search for effective methods of treating infections. This review focuses on modern data on the basic protective strategies of neutrophils against bacterial infections and their contribution to the pathogenesis of proinflammatory responses. Approaches to pharmacological modulation of different antimicrobial mechanisms of neutrophils are discussed.</p></trans-abstract><kwd-group xml:lang="ru"><kwd>инфекционные болезни</kwd><kwd>нейтрофилы</kwd><kwd>воспаление</kwd><kwd>антибиотикорезистентность</kwd><kwd>фагоцитоз</kwd><kwd>дегрануляция</kwd><kwd>нейтрофильные внеклеточные ловушки (NETs)</kwd><kwd>обзор</kwd></kwd-group><kwd-group xml:lang="en"><kwd>infectious diseases</kwd><kwd>neutrophils</kwd><kwd>inflammation</kwd><kwd>antibiotic resistance</kwd><kwd>phagocytosis</kwd><kwd>degra- nulation</kwd><kwd>neutrophilic extracellular traps (NETs)</kwd><kwd>review</kwd></kwd-group><funding-group><funding-statement xml:lang="en">This work was supported by the Comprehensive Program of Basic Research of the Far East Branch of the Russian Academy of Sciences “Far East”, project No. 18-5-099. Acknowledgments. The authors express their gratitude to Bynina Marina Pavlovna, the junior researcher of the Laboratory of Molecular Epidemiology and Microbiology of Somov Institute of Epidemiology and Microbiology for her help in the preparation of materials</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">Borregaard N. Neutrophils, from marrow to microbes. Immunity. 2010; 33(5): 657–70. doi: 10.1016/j.immuni.2010.11.011.</mixed-citation><mixed-citation xml:lang="en">Borregaard N. Neutrophils, from marrow to microbes. Immunity. 2010; 33(5): 657–70. doi: 10.1016/j.immuni.2010.11.011.</mixed-citation></citation-alternatives></ref><ref id="cit2"><label>2</label><citation-alternatives><mixed-citation xml:lang="ru">Leliefeld P.H., Wessels C.M., Leenen L.P., Koenderman L., Pillay J. The role of neutrophils in immune dysfunction during severe inflammation. Crit. Care. 2016; 20: 73. doi: 10.1186/s13054-016-1250-4.</mixed-citation><mixed-citation xml:lang="en">Leliefeld P.H., Wessels C.M., Leenen L.P., Koenderman L., Pillay J. The role of neutrophils in immune dysfunction during severe inflammation. Crit. Care. 2016; 20: 73. doi: 10.1186/s13054-016-1250-4.</mixed-citation></citation-alternatives></ref><ref id="cit3"><label>3</label><citation-alternatives><mixed-citation xml:lang="ru">Nathan C. Neutrophils and immunity: challenges and opportunities. Nat. Rev. Immunol. 2006; 6(3): 173–82. doi: 10.1038/nri1785.</mixed-citation><mixed-citation xml:lang="en">Nathan C. Neutrophils and immunity: challenges and opportunities. Nat. Rev. Immunol. 2006; 6(3): 173–82. doi: 10.1038/nri1785.</mixed-citation></citation-alternatives></ref><ref id="cit4"><label>4</label><citation-alternatives><mixed-citation xml:lang="ru">Mayadas T.N., Cullere X., Lowell C.A. The multifaceted functions of neutrophils. Annu. Rev. Pathol. 2014; 9: 181–218. doi: 10.1146/annurevpathol-020712-164023.</mixed-citation><mixed-citation xml:lang="en">Mayadas T.N., Cullere X., Lowell C.A. The multifaceted functions of neutrophils. Annu. Rev. Pathol. 2014; 9: 181–218. doi: 10.1146/annurevpathol-020712-164023.</mixed-citation></citation-alternatives></ref><ref id="cit5"><label>5</label><citation-alternatives><mixed-citation xml:lang="ru">Segal A.W. How neutrophils kill microbes. Annu. Rev. Immunol. 2005; 23: 197– 223. doi:10.1146/annurev.immunol.23.021704.115653. Available at: https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2092448/(accessed 11 Sept 2017).</mixed-citation><mixed-citation xml:lang="en">Segal A.W. How neutrophils kill microbes. Annu. Rev. Immunol. 2005; 23: 197– 223. doi:10.1146/annurev.immunol.23.021704.115653. Available at: https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2092448/(accessed 11 Sept 2017).</mixed-citation></citation-alternatives></ref><ref id="cit6"><label>6</label><citation-alternatives><mixed-citation xml:lang="ru">Urban C.F., Lourido S., Zychlinsky A. How do microbes evade neutrophil killing? Cell Microbiol. 2006; 8(11): 1687–96. doi: 10.1111/j.14625822.2006.00792.x.</mixed-citation><mixed-citation xml:lang="en">Urban C.F., Lourido S., Zychlinsky A. How do microbes evade neutrophil killing? Cell Microbiol. 2006; 8(11): 1687–96. doi: 10.1111/j.14625822.2006.00792.x.</mixed-citation></citation-alternatives></ref><ref id="cit7"><label>7</label><citation-alternatives><mixed-citation xml:lang="ru">Döhrmann S., Cole J.N., Nizet V. Conquering neutrophils. PLoS Pathog. 2016; 12(7): e1005682. doi: 10.1371/journal.ppat.1005682. Available at: http://journals.plos.org/plospathogens/article?id=10.1371/journal.ppat.1005682 (accessed 11 Sept 2017)</mixed-citation><mixed-citation xml:lang="en">Döhrmann S., Cole J.N., Nizet V. Conquering neutrophils. PLoS Pathog. 2016; 12(7): e1005682. doi: 10.1371/journal.ppat.1005682. Available at: http://journals.plos.org/plospathogens/article?id=10.1371/journal.ppat.1005682 (accessed 11 Sept 2017)</mixed-citation></citation-alternatives></ref><ref id="cit8"><label>8</label><citation-alternatives><mixed-citation xml:lang="ru">Nauseef W.M. Neutrophils, from cradle to grave and beyond. Immunol. Rev. 2016; 273(1): 5–10. doi: 10.1111/imr.12463.</mixed-citation><mixed-citation xml:lang="en">Nauseef W.M. Neutrophils, from cradle to grave and beyond. Immunol. Rev. 2016; 273(1): 5–10. doi: 10.1111/imr.12463.</mixed-citation></citation-alternatives></ref><ref id="cit9"><label>9</label><citation-alternatives><mixed-citation xml:lang="ru">Dunkelberger J.R., Song W.C. Complement and its role in innate and adaptive immune responses. Cell Res. 2010; 20(1): 34–50. doi: 10.1038/cr.2009.139. Available at: https://www.nature.com/cr/journal/v20/n1/full/cr2009139a.html (accessed 11 Sept 2017)</mixed-citation><mixed-citation xml:lang="en">Dunkelberger J.R., Song W.C. Complement and its role in innate and adaptive immune responses. Cell Res. 2010; 20(1): 34–50. doi: 10.1038/cr.2009.139. Available at: https://www.nature.com/cr/journal/v20/n1/full/cr2009139a.html (accessed 11 Sept 2017)</mixed-citation></citation-alternatives></ref><ref id="cit10"><label>10</label><citation-alternatives><mixed-citation xml:lang="ru">van Kessel K.P., Bestebroer J., van Strijp J.A. Neutrophil-mediated phagocytosis of Staphylococcus aureus. Front. Immunol. 2014; 5: 467. doi: 10.3389/fimmu.2014.00467. Available at: http://journal.frontiersin.org/article/10.3389/fimmu.2014.00467/full (accessed 11 Sept 2017)</mixed-citation><mixed-citation xml:lang="en">van Kessel K.P., Bestebroer J., van Strijp J.A. Neutrophil-mediated phagocytosis of Staphylococcus aureus. Front. Immunol. 2014; 5: 467. doi: 10.3389/fimmu.2014.00467. Available at: http://journal.frontiersin.org/article/10.3389/fimmu.2014.00467/full (accessed 11 Sept 2017)</mixed-citation></citation-alternatives></ref><ref id="cit11"><label>11</label><citation-alternatives><mixed-citation xml:lang="ru">Amulic B., Cazalet C., Hayes G.L., Metzler K.D., Zychlinsky A. Neutrophil function: from mechanisms to disease. Annu. Rev. Immunol. 2012; 30: 459– 89. doi: 10.1146/annurev-immunol-020711-074942.</mixed-citation><mixed-citation xml:lang="en">Amulic B., Cazalet C., Hayes G.L., Metzler K.D., Zychlinsky A. Neutrophil function: from mechanisms to disease. Annu. Rev. Immunol. 2012; 30: 459– 89. doi: 10.1146/annurev-immunol-020711-074942.</mixed-citation></citation-alternatives></ref><ref id="cit12"><label>12</label><citation-alternatives><mixed-citation xml:lang="ru">Rigby K.M., DeLeo F.R. Neutrophils in innate host defense against Staphylococcus aureus infections. Semin Immunopathol. 2012; 34(2): 237– 59. doi: 10.1007/s00281-011-0295-3. Available at:: https://link.springer.com/article/10.1007/s00281-011-0295-3 (accessed 11 Sept 2017)</mixed-citation><mixed-citation xml:lang="en">Rigby K.M., DeLeo F.R. Neutrophils in innate host defense against Staphylococcus aureus infections. Semin Immunopathol. 2012; 34(2): 237– 59. doi: 10.1007/s00281-011-0295-3. Available at:: https://link.springer.com/article/10.1007/s00281-011-0295-3 (accessed 11 Sept 2017)</mixed-citation></citation-alternatives></ref><ref id="cit13"><label>13</label><citation-alternatives><mixed-citation xml:lang="ru">Ford J.W., McVicar D.W. TREM and TREM-like receptors in inflammation and disease. Curr. Opin. Immunol. 2009; 21(1): 38–46. doi: 10.1016/j.coi.2009.01.009.</mixed-citation><mixed-citation xml:lang="en">Ford J.W., McVicar D.W. TREM and TREM-like receptors in inflammation and disease. Curr. Opin. Immunol. 2009; 21(1): 38–46. doi: 10.1016/j.coi.2009.01.009.</mixed-citation></citation-alternatives></ref><ref id="cit14"><label>14</label><citation-alternatives><mixed-citation xml:lang="ru">Mщcsai A. Diverse novel functions of neutrophils in immunity, inflammation, and beyond. J. Exp. Med. 2013; 210(7): 1283–99. doi: 10.1084/jem.20122220. Available at (accessed 11 Sept 2017): http://jem.rupress.org/content/210/7/1283.long</mixed-citation><mixed-citation xml:lang="en">Mщcsai A. Diverse novel functions of neutrophils in immunity, inflammation, and beyond. J. Exp. Med. 2013; 210(7): 1283–99. doi: 10.1084/jem.20122220. Available at (accessed 11 Sept 2017): http://jem.rupress.org/content/210/7/1283.long</mixed-citation></citation-alternatives></ref><ref id="cit15"><label>15</label><citation-alternatives><mixed-citation xml:lang="ru">Roos D., van Bruggen R., Meischl C. Oxidative killing of microbes by neutrophils. Microbes Infect. 2003; 5(14): 1307–15. doi: 10.1016/j.micinf.2003.09.009.</mixed-citation><mixed-citation xml:lang="en">Roos D., van Bruggen R., Meischl C. Oxidative killing of microbes by neutrophils. Microbes Infect. 2003; 5(14): 1307–15. doi: 10.1016/j.micinf.2003.09.009.</mixed-citation></citation-alternatives></ref><ref id="cit16"><label>16</label><citation-alternatives><mixed-citation xml:lang="ru">Greenlee-Wacker M., DeLeo F.R., Nauseef W.M. How methicillin-resistant Staphylococcus aureus evade neutrophil killing. Curr. Opin. Hematol. 2015; 22(1): 30–5. doi: 10.1097/MOH.0000000000000096.</mixed-citation><mixed-citation xml:lang="en">Greenlee-Wacker M., DeLeo F.R., Nauseef W.M. How methicillin-resistant Staphylococcus aureus evade neutrophil killing. Curr. Opin. Hematol. 2015; 22(1): 30–5. doi: 10.1097/MOH.0000000000000096.</mixed-citation></citation-alternatives></ref><ref id="cit17"><label>17</label><citation-alternatives><mixed-citation xml:lang="ru">Odobasic D., Kitching A.R., Holdsworth S.R. Neutrophil-mediated regulation of innate and adaptive immunity: the role of myeloperoxidase. J. Immunol. Res. 2016; 2016: 11. doi: 10.1155/2016/2349817.2349817. Available at: http://dx.doi.org/10.1155/2016/2349817(accessed 11 Sept 2017)</mixed-citation><mixed-citation xml:lang="en">Odobasic D., Kitching A.R., Holdsworth S.R. Neutrophil-mediated regulation of innate and adaptive immunity: the role of myeloperoxidase. J. Immunol. Res. 2016; 2016: 11. doi: 10.1155/2016/2349817.2349817. Available at: http://dx.doi.org/10.1155/2016/2349817(accessed 11 Sept 2017)</mixed-citation></citation-alternatives></ref><ref id="cit18"><label>18</label><citation-alternatives><mixed-citation xml:lang="ru">Bardoel B.W., Kenny E.F., Sollberger G., Zychlinsky A. The balancing act of neutrophils cell host and microbe. Cell Host. Microbe. 2014; 15(5): 526–36. doi: 10.1016/j.chom.2014.04.011. Available at: http://www.cell.com/action/showImagesData?pii=S1931-3128%2814%2900145-0 (accessed 11 Sept 2017)</mixed-citation><mixed-citation xml:lang="en">Bardoel B.W., Kenny E.F., Sollberger G., Zychlinsky A. The balancing act of neutrophils cell host and microbe. Cell Host. Microbe. 2014; 15(5): 526–36. doi: 10.1016/j.chom.2014.04.011. Available at: http://www.cell.com/action/showImagesData?pii=S1931-3128%2814%2900145-0 (accessed 11 Sept 2017)</mixed-citation></citation-alternatives></ref><ref id="cit19"><label>19</label><citation-alternatives><mixed-citation xml:lang="ru">Klebanoff S.J. Myeloperoxidase: friend and foe. J. Leukoc. Biol. 2005; 77(5): 598–625.</mixed-citation><mixed-citation xml:lang="en">Klebanoff S.J. Myeloperoxidase: friend and foe. J. Leukoc. Biol. 2005; 77(5): 598–625.</mixed-citation></citation-alternatives></ref><ref id="cit20"><label>20</label><citation-alternatives><mixed-citation xml:lang="ru">Dapunt U., Hansch G.M., Arciola C.R. Innate Immune Response in ImplantAssociated Infections: Neutrophils against Biofilms. Materials. 2016; 9(5): 387. Available at: http://www.mdpi.com/1996-1944/9/5/387/htm (accessed 11 Sept 2017)</mixed-citation><mixed-citation xml:lang="en">Dapunt U., Hansch G.M., Arciola C.R. Innate Immune Response in ImplantAssociated Infections: Neutrophils against Biofilms. Materials. 2016; 9(5): 387. Available at: http://www.mdpi.com/1996-1944/9/5/387/htm (accessed 11 Sept 2017)</mixed-citation></citation-alternatives></ref><ref id="cit21"><label>21</label><citation-alternatives><mixed-citation xml:lang="ru">Morozov V.I., Pryatkin S.A., Kalinski M.I., Rogozkin V.A. Effect of exercise to exhaustion on myeloperoxidase and lysozyme release from blood neutrophils. Eur. J. Appl. Physiol. 2003; 89(3–4): 257–62. doi: 10.1007/s00421-002-0755-5.</mixed-citation><mixed-citation xml:lang="en">Morozov V.I., Pryatkin S.A., Kalinski M.I., Rogozkin V.A. Effect of exercise to exhaustion on myeloperoxidase and lysozyme release from blood neutrophils. Eur. J. Appl. Physiol. 2003; 89(3–4): 257–62. doi: 10.1007/s00421-002-0755-5.</mixed-citation></citation-alternatives></ref><ref id="cit22"><label>22</label><citation-alternatives><mixed-citation xml:lang="ru">Winterbourn C.C., Kettle A.J., Hampton M.B. Reactive oxygen species and neutrophil function. Annu. Rev. Biochem. 2016; 85: 765–92. doi: 10.1146/annurev-biochem-060815-014442.</mixed-citation><mixed-citation xml:lang="en">Winterbourn C.C., Kettle A.J., Hampton M.B. Reactive oxygen species and neutrophil function. Annu. Rev. Biochem. 2016; 85: 765–92. doi: 10.1146/annurev-biochem-060815-014442.</mixed-citation></citation-alternatives></ref><ref id="cit23"><label>23</label><citation-alternatives><mixed-citation xml:lang="ru">Cardot-Martin E., Casalegno J.S., Badiou C., Dauwalder O., Keller D., Prévost G., et al. α-defensins partially protect human neutrophils against Panton-Valentine leukocidin produced by Staphylococcus aureus. Lett. Appl. Microbiol. 2015; 61(2): 158–64. doi: 10.1111/lam.12438.</mixed-citation><mixed-citation xml:lang="en">Cardot-Martin E., Casalegno J.S., Badiou C., Dauwalder O., Keller D., Prévost G., et al. α-defensins partially protect human neutrophils against Panton-Valentine leukocidin produced by Staphylococcus aureus. Lett. Appl. Microbiol. 2015; 61(2): 158–64. doi: 10.1111/lam.12438.</mixed-citation></citation-alternatives></ref><ref id="cit24"><label>24</label><citation-alternatives><mixed-citation xml:lang="ru">Frasca L., Lande R. Role of defensins and cathelicidin LL37 in auto-immune and auto-inflammatory diseases. Curr. Pharm .Biotechnol. 2012; 13(10): 1882–97. doi: 10.2174/138920112802273155.</mixed-citation><mixed-citation xml:lang="en">Frasca L., Lande R. Role of defensins and cathelicidin LL37 in auto-immune and auto-inflammatory diseases. Curr. Pharm .Biotechnol. 2012; 13(10): 1882–97. doi: 10.2174/138920112802273155.</mixed-citation></citation-alternatives></ref><ref id="cit25"><label>25</label><citation-alternatives><mixed-citation xml:lang="ru">Nordenfelt P., Tapper H.J. Phagosome dynamics during phagocytosis by neutrophils. J. Leukoc. Biol. 2011; 90(2): 271–84. doi: 10.1189/jlb.0810457.</mixed-citation><mixed-citation xml:lang="en">Nordenfelt P., Tapper H.J. Phagosome dynamics during phagocytosis by neutrophils. J. Leukoc. Biol. 2011; 90(2): 271–84. doi: 10.1189/jlb.0810457.</mixed-citation></citation-alternatives></ref><ref id="cit26"><label>26</label><citation-alternatives><mixed-citation xml:lang="ru">Chebotar I.V. Mechanisms of antibiofilm immunity. Annals of the Russian Academy of Medical Sciences. 2012; 67(12): 22–9. doi:10.15690/vramn. v67i12.477. (in Russian)</mixed-citation><mixed-citation xml:lang="en">Chebotar I.V. Mechanisms of antibiofilm immunity. Annals of the Russian Academy of Medical Sciences. 2012; 67(12): 22–9. doi:10.15690/vramn. v67i12.477. (in Russian)</mixed-citation></citation-alternatives></ref><ref id="cit27"><label>27</label><citation-alternatives><mixed-citation xml:lang="ru">Schuerholz T., Brandenburg K., Marx G. Antimicrobial peptides and their potential application in inflammation and sepsis. Crit. Care. 2012; 16(2): 207. doi: 10.1186/cc11220. Available at: https://doi.org/10.1186/cc11220 (accessed 11 Sept 2017)</mixed-citation><mixed-citation xml:lang="en">Schuerholz T., Brandenburg K., Marx G. Antimicrobial peptides and their potential application in inflammation and sepsis. Crit. Care. 2012; 16(2): 207. doi: 10.1186/cc11220. Available at: https://doi.org/10.1186/cc11220 (accessed 11 Sept 2017)</mixed-citation></citation-alternatives></ref><ref id="cit28"><label>28</label><citation-alternatives><mixed-citation xml:lang="ru">Cojocaru I.M., Cojocaru M., Burcin C. Evaluation of granulocyte elastase as a sensitive diagnostic parameter of inflammation in first ischemic stroke. Rom. J. Intern. Med. 2006; 44(3): 317–21. Available at: https://www.ncbi.nlm.nih.gov/pubmed/18386609 (accessed 11 Sept 2017)</mixed-citation><mixed-citation xml:lang="en">Cojocaru I.M., Cojocaru M., Burcin C. Evaluation of granulocyte elastase as a sensitive diagnostic parameter of inflammation in first ischemic stroke. Rom. J. Intern. Med. 2006; 44(3): 317–21. Available at: https://www.ncbi.nlm.nih.gov/pubmed/18386609 (accessed 11 Sept 2017)</mixed-citation></citation-alternatives></ref><ref id="cit29"><label>29</label><citation-alternatives><mixed-citation xml:lang="ru">Naegelen I., Beaume N., Plançon S., Schenten V., Tschirhart E.J., Bréchard S. Regulation of Neutrophil Degranulation and Cytokine Secretion: A Novel Model Approach Based on Linear Fitting. J. Immunol. Res. 2015; 2015: 817038.. Available at: https://www.hindawi.com/journals/jir/2015/817038/ (accessed 11 Sept 2017)</mixed-citation><mixed-citation xml:lang="en">Naegelen I., Beaume N., Plançon S., Schenten V., Tschirhart E.J., Bréchard S. Regulation of Neutrophil Degranulation and Cytokine Secretion: A Novel Model Approach Based on Linear Fitting. J. Immunol. Res. 2015; 2015: 817038.. Available at: https://www.hindawi.com/journals/jir/2015/817038/ (accessed 11 Sept 2017)</mixed-citation></citation-alternatives></ref><ref id="cit30"><label>30</label><citation-alternatives><mixed-citation xml:lang="ru">Park C.B., Yi K.S., Matsuzaki K., Kim M.S., Kim S.C. Structure-activity analysis of buforin II, a histone H2A-derived antimicrobial peptide: the proline hinge is responsible for the cell-penetrating ability of buforin II. Proc. Natl. Acad. Sci. U.S.A. 2000; 97(15): 8245–50. Available at: http://www.pnas.org/content/97/15/8245.long (accessed 11 Sept 2017)</mixed-citation><mixed-citation xml:lang="en">Park C.B., Yi K.S., Matsuzaki K., Kim M.S., Kim S.C. Structure-activity analysis of buforin II, a histone H2A-derived antimicrobial peptide: the proline hinge is responsible for the cell-penetrating ability of buforin II. Proc. Natl. Acad. Sci. U.S.A. 2000; 97(15): 8245–50. Available at: http://www.pnas.org/content/97/15/8245.long (accessed 11 Sept 2017)</mixed-citation></citation-alternatives></ref><ref id="cit31"><label>31</label><citation-alternatives><mixed-citation xml:lang="ru">Malcolm K.C., Worthen G.S. Lipopolysaccharide stimulates p38-dependent induction of antiviral genes in neutrophils independently of paracrine factors. J. Biol. Chem. 2003; 278(18): 15693-701. Available at: http://www.jbc.org/content/278/18/15693.long (accessed 11 Sept 2017)</mixed-citation><mixed-citation xml:lang="en">Malcolm K.C., Worthen G.S. Lipopolysaccharide stimulates p38-dependent induction of antiviral genes in neutrophils independently of paracrine factors. J. Biol. Chem. 2003; 278(18): 15693-701. Available at: http://www.jbc.org/content/278/18/15693.long (accessed 11 Sept 2017)</mixed-citation></citation-alternatives></ref><ref id="cit32"><label>32</label><citation-alternatives><mixed-citation xml:lang="ru">Brinkmann V., Reichard U., Goosmann C., Fauler B., Uhlemann Y., Weiss D.S., et al. Neutrophil extracellular traps kill bacteria. Science. 2004; 303(5663): 1532–5.</mixed-citation><mixed-citation xml:lang="en">Brinkmann V., Reichard U., Goosmann C., Fauler B., Uhlemann Y., Weiss D.S., et al. Neutrophil extracellular traps kill bacteria. Science. 2004; 303(5663): 1532–5.</mixed-citation></citation-alternatives></ref><ref id="cit33"><label>33</label><citation-alternatives><mixed-citation xml:lang="ru">Brinkmann V., Zychlinsky A. Neutrophil extracellular traps: is immunity the second function of chromatin? J. Cell Biol. 2012; 198(5): 773–83. doi Available at: http://jcb.rupress.org/content/198/5/773.long(accessed 11 Sept 2017)</mixed-citation><mixed-citation xml:lang="en">Brinkmann V., Zychlinsky A. Neutrophil extracellular traps: is immunity the second function of chromatin? J. Cell Biol. 2012; 198(5): 773–83. doi Available at: http://jcb.rupress.org/content/198/5/773.long(accessed 11 Sept 2017)</mixed-citation></citation-alternatives></ref><ref id="cit34"><label>34</label><citation-alternatives><mixed-citation xml:lang="ru">Klebanoff S.J., Kettle A.J., Rosen H., Winterbourn C.C., Nauseef W.M. Myeloperoxidase: a front-line defeder against phagocytosed microorganisms. J. Leukoc. Biol. 2013; 93(2): 185–98. doi: 10.1189/jlb.0712349.</mixed-citation><mixed-citation xml:lang="en">Klebanoff S.J., Kettle A.J., Rosen H., Winterbourn C.C., Nauseef W.M. Myeloperoxidase: a front-line defeder against phagocytosed microorganisms. J. Leukoc. Biol. 2013; 93(2): 185–98. doi: 10.1189/jlb.0712349.</mixed-citation></citation-alternatives></ref><ref id="cit35"><label>35</label><citation-alternatives><mixed-citation xml:lang="ru">Theeß W., Sellau J., Steeg C., Klinke A., Baldus S., Cramer J.P., et al. Myeloperoxidase attenuates pathogen clearance during Plasmodium yoelii nonlethal infection. Infect. Immun. 2016; 85(1): e00475–16. Available at: http://iai.asm.org/content/85/1/e00475-16.long (accessed 11 Sept 2017)</mixed-citation><mixed-citation xml:lang="en">Theeß W., Sellau J., Steeg C., Klinke A., Baldus S., Cramer J.P., et al. Myeloperoxidase attenuates pathogen clearance during Plasmodium yoelii nonlethal infection. Infect. Immun. 2016; 85(1): e00475–16. Available at: http://iai.asm.org/content/85/1/e00475-16.long (accessed 11 Sept 2017)</mixed-citation></citation-alternatives></ref><ref id="cit36"><label>36</label><citation-alternatives><mixed-citation xml:lang="ru">Delgado-Rizo V., Martinez-Guzman M.A., Iniguez-Gutierrez L., GarciaOrozco A., Alvarado-Navarro A., Fafutis-Morris M. Neutrophil extracellular traps and its implications in inflammation: an overview. Front. Immunol. 2017; 8: 81. doi: 10.3389/fimmu.2017.00081. Available at: http://journal.frontiersin.org/article/10.3389/fimmu.2017.00081/full (accessed 11 Sept 2017)</mixed-citation><mixed-citation xml:lang="en">Delgado-Rizo V., Martinez-Guzman M.A., Iniguez-Gutierrez L., GarciaOrozco A., Alvarado-Navarro A., Fafutis-Morris M. Neutrophil extracellular traps and its implications in inflammation: an overview. Front. Immunol. 2017; 8: 81. doi: 10.3389/fimmu.2017.00081. Available at: http://journal.frontiersin.org/article/10.3389/fimmu.2017.00081/full (accessed 11 Sept 2017)</mixed-citation></citation-alternatives></ref><ref id="cit37"><label>37</label><citation-alternatives><mixed-citation xml:lang="ru">Yang H., Biermann M.H., Brauner J.M., Liu Y., Zhao Y., Herrmann M. New insights into neutrophil extracellular traps: mechanisms of formation and role in inflammation. Front. Immunol. 2016; 7: 302. Available at: http://journal.frontiersin.org/article/10.3389/fimmu.2016.00302/full (accessed 11 Sept 2017)</mixed-citation><mixed-citation xml:lang="en">Yang H., Biermann M.H., Brauner J.M., Liu Y., Zhao Y., Herrmann M. New insights into neutrophil extracellular traps: mechanisms of formation and role in inflammation. Front. Immunol. 2016; 7: 302. Available at: http://journal.frontiersin.org/article/10.3389/fimmu.2016.00302/full (accessed 11 Sept 2017)</mixed-citation></citation-alternatives></ref><ref id="cit38"><label>38</label><citation-alternatives><mixed-citation xml:lang="ru">Chakraborty S., Kaur S., Guha S., Batra S.K. The multifaceted roles of neutrophil gelatinase associated lipocalin (NGAL) in inflammation and cancer. Biochim. Biophys. Acta. 2012; 1826(1): 129–69. doi: 10.1016/j.bbcan.2012.03.008.</mixed-citation><mixed-citation xml:lang="en">Chakraborty S., Kaur S., Guha S., Batra S.K. The multifaceted roles of neutrophil gelatinase associated lipocalin (NGAL) in inflammation and cancer. Biochim. Biophys. Acta. 2012; 1826(1): 129–69. doi: 10.1016/j.bbcan.2012.03.008.</mixed-citation></citation-alternatives></ref><ref id="cit39"><label>39</label><citation-alternatives><mixed-citation xml:lang="ru">Koymans K.J., Feitsma L.J., Brondijk T.H., Aerts P.C., Lukkien E., Lössl P., et al. Structural basis for inhibition of TLR2 by staphylococcal superantigen-like protein 3 (SSL3). Proc. Natl. Acad. Sci. U.S.A. 2015; 112(35): 11018–23.</mixed-citation><mixed-citation xml:lang="en">Koymans K.J., Feitsma L.J., Brondijk T.H., Aerts P.C., Lukkien E., Lössl P., et al. Structural basis for inhibition of TLR2 by staphylococcal superantigen-like protein 3 (SSL3). Proc. Natl. Acad. Sci. U.S.A. 2015; 112(35): 11018–23.</mixed-citation></citation-alternatives></ref><ref id="cit40"><label>40</label><citation-alternatives><mixed-citation xml:lang="ru">Amulic B., Hayes G. Neutrophil extracellular traps. Curr. Biol. 2011; 21(9): R297-8.:</mixed-citation><mixed-citation xml:lang="en">Amulic B., Hayes G. Neutrophil extracellular traps. Curr. Biol. 2011; 21(9): R297-8.:</mixed-citation></citation-alternatives></ref><ref id="cit41"><label>41</label><citation-alternatives><mixed-citation xml:lang="ru">Pang Y.Y., Schwartz J., Bloomberg S., Boyd J.M., Horswill A.R., Nauseef W.M. Methionine sulfoxide reductases protect against oxidative stress in staphylococcus aureus encountering exogenous oxidants and human neutrophils. J. Innate. Immun. 2014; 6(3): 353–64.</mixed-citation><mixed-citation xml:lang="en">Pang Y.Y., Schwartz J., Bloomberg S., Boyd J.M., Horswill A.R., Nauseef W.M. Methionine sulfoxide reductases protect against oxidative stress in staphylococcus aureus encountering exogenous oxidants and human neutrophils. J. Innate. Immun. 2014; 6(3): 353–64.</mixed-citation></citation-alternatives></ref><ref id="cit42"><label>42</label><citation-alternatives><mixed-citation xml:lang="ru">Nishimura Y., Lee H., Hafenstein S., Kataoka C., Wakita T., Bergelson J.M., et al. Enterovirus 71 binding to PSGL-1 on leukocytes: VP1-145 acts as a molecular switch to control receptor interaction. PLoS Pathog. 2013; 9(7): e1003511.. Available at: http://journals.plos.org/plospathogens/article?id=10.1371/journal.ppat.1003511 (accessed 11 Sept 2017)</mixed-citation><mixed-citation xml:lang="en">Nishimura Y., Lee H., Hafenstein S., Kataoka C., Wakita T., Bergelson J.M., et al. Enterovirus 71 binding to PSGL-1 on leukocytes: VP1-145 acts as a molecular switch to control receptor interaction. PLoS Pathog. 2013; 9(7): e1003511.. Available at: http://journals.plos.org/plospathogens/article?id=10.1371/journal.ppat.1003511 (accessed 11 Sept 2017)</mixed-citation></citation-alternatives></ref><ref id="cit43"><label>43</label><citation-alternatives><mixed-citation xml:lang="ru">Lee L.Y., Höök M., Haviland D., Wetsel R.A., Yonter E.O., Syribeys P., et al. Inhibition of complement activation by a secreted Staphylococcus aureus protein. J. Infect. Dis. 2004; 190(3): 571–9.</mixed-citation><mixed-citation xml:lang="en">Lee L.Y., Höök M., Haviland D., Wetsel R.A., Yonter E.O., Syribeys P., et al. Inhibition of complement activation by a secreted Staphylococcus aureus protein. J. Infect. Dis. 2004; 190(3): 571–9.</mixed-citation></citation-alternatives></ref><ref id="cit44"><label>44</label><citation-alternatives><mixed-citation xml:lang="ru">Higgins J., Loughman A., Van Kessel K.P., Van Strijp J.A., Foster T.J. Clumping factor A of Staphylococcus aureus inhibits phagocytosis by human polymorphonuclear leucocytes. FEMS Microb. Let. 2006; 258(2): 290–6.</mixed-citation><mixed-citation xml:lang="en">Higgins J., Loughman A., Van Kessel K.P., Van Strijp J.A., Foster T.J. Clumping factor A of Staphylococcus aureus inhibits phagocytosis by human polymorphonuclear leucocytes. FEMS Microb. Let. 2006; 258(2): 290–6.</mixed-citation></citation-alternatives></ref><ref id="cit45"><label>45</label><citation-alternatives><mixed-citation xml:lang="ru">Postma B., Poppelier M.J., van Galen J.C., Prossnitz E.R., van Strijp J.A., de Haas C.J., et al. Chemotaxis inhibitory protein of Staphylococcus aureus binds specifically to the C5a and formylated peptide receptor. J. Immunol. 2004; 172(11): 6994–7001.</mixed-citation><mixed-citation xml:lang="en">Postma B., Poppelier M.J., van Galen J.C., Prossnitz E.R., van Strijp J.A., de Haas C.J., et al. Chemotaxis inhibitory protein of Staphylococcus aureus binds specifically to the C5a and formylated peptide receptor. J. Immunol. 2004; 172(11): 6994–7001.</mixed-citation></citation-alternatives></ref><ref id="cit46"><label>46</label><citation-alternatives><mixed-citation xml:lang="ru">van Wamel W.J., Rooijakkers S.H., Ruyken M., van Kessel K.P., van Strijp J.A. The innate immune modulators staphylococcal complement inhibitor and chemotaxis inhibitory protein of Staphylococcus aureus are located on β-hemolysin-converting bacteriophages. J. Bacteriol. 2006; 188(4): 1310–5.</mixed-citation><mixed-citation xml:lang="en">van Wamel W.J., Rooijakkers S.H., Ruyken M., van Kessel K.P., van Strijp J.A. The innate immune modulators staphylococcal complement inhibitor and chemotaxis inhibitory protein of Staphylococcus aureus are located on β-hemolysin-converting bacteriophages. J. Bacteriol. 2006; 188(4): 1310–5.</mixed-citation></citation-alternatives></ref><ref id="cit47"><label>47</label><citation-alternatives><mixed-citation xml:lang="ru">Gustafsson E., Rosén A., Barchan K., van Kessel K.P., Haraldsson K., Lindman S., et al. Directed evolution of chemotaxis inhibitory protein of Staphylococcus aureus generates biologically functional variants with reduced interaction with human antibodies. Protein Eng. Des. Sel. 2010; 23(2): 91–101.</mixed-citation><mixed-citation xml:lang="en">Gustafsson E., Rosén A., Barchan K., van Kessel K.P., Haraldsson K., Lindman S., et al. Directed evolution of chemotaxis inhibitory protein of Staphylococcus aureus generates biologically functional variants with reduced interaction with human antibodies. Protein Eng. Des. Sel. 2010; 23(2): 91–101.</mixed-citation></citation-alternatives></ref><ref id="cit48"><label>48</label><citation-alternatives><mixed-citation xml:lang="ru">Thammavongsa V., Missiakas D.M., Schneewind O. Staphylococcus aureus degrades neutrophil extracellular traps to promote immune cell death. Science. 2013; 342(6160): 863–6. doi: 10.1126/science.1242255.</mixed-citation><mixed-citation xml:lang="en">Thammavongsa V., Missiakas D.M., Schneewind O. Staphylococcus aureus degrades neutrophil extracellular traps to promote immune cell death. Science. 2013; 342(6160): 863–6. doi: 10.1126/science.1242255.</mixed-citation></citation-alternatives></ref><ref id="cit49"><label>49</label><citation-alternatives><mixed-citation xml:lang="ru">Abate F., Malito E., Falugi F., Margarit Y Ros I., Bottomley M.J. Cloning, expression, purification, crystallization and preliminary X-ray diffraction analysis of SpyCEP, a candidate antigen for a vaccine against Streptococcus pyogenes. Acta Cryst. 2013; 69(Pt 10): 1103–6. doi: 10.1107/S1744309113024871. Available at: http://scripts.iucr.org/cgi-bin/paper?S1744309113024871(accessed 11 Sept 2017)</mixed-citation><mixed-citation xml:lang="en">Abate F., Malito E., Falugi F., Margarit Y Ros I., Bottomley M.J. Cloning, expression, purification, crystallization and preliminary X-ray diffraction analysis of SpyCEP, a candidate antigen for a vaccine against Streptococcus pyogenes. Acta Cryst. 2013; 69(Pt 10): 1103–6. doi: 10.1107/S1744309113024871. Available at: http://scripts.iucr.org/cgi-bin/paper?S1744309113024871(accessed 11 Sept 2017)</mixed-citation></citation-alternatives></ref><ref id="cit50"><label>50</label><citation-alternatives><mixed-citation xml:lang="ru">Lazaro-Diez M., Chapartegui-Gonzalez I., Redondo-Salvo S., Leigh C., Merino D., Segundo D., et al. Human neutrophils phagocytose and kill Acinetobacter baumannii and A. pittii. Sci. Rep. 2017; 7(1): 4571. doi: 10.1038/s41598-017-04870-8.</mixed-citation><mixed-citation xml:lang="en">Lazaro-Diez M., Chapartegui-Gonzalez I., Redondo-Salvo S., Leigh C., Merino D., Segundo D., et al. Human neutrophils phagocytose and kill Acinetobacter baumannii and A. pittii. Sci. Rep. 2017; 7(1): 4571. doi: 10.1038/s41598-017-04870-8.</mixed-citation></citation-alternatives></ref><ref id="cit51"><label>51</label><citation-alternatives><mixed-citation xml:lang="ru">Feng S., Bowden N., Fragiadaki M., Souilhol C., Hsiao S., Mahmoud M., et al. Mechanical activation of hypoxia-inducible factor 1α drives endothelial dysfunction at atheroprone sites. Arterioscler. Thromb. Vasc. Biol. 2017; 37(11): 2087–2101. doi: 10.1161/ATVBAHA.117.309249.</mixed-citation><mixed-citation xml:lang="en">Feng S., Bowden N., Fragiadaki M., Souilhol C., Hsiao S., Mahmoud M., et al. Mechanical activation of hypoxia-inducible factor 1α drives endothelial dysfunction at atheroprone sites. Arterioscler. Thromb. Vasc. Biol. 2017; 37(11): 2087–2101. doi: 10.1161/ATVBAHA.117.309249.</mixed-citation></citation-alternatives></ref><ref id="cit52"><label>52</label><citation-alternatives><mixed-citation xml:lang="ru">Guo X., Zhu Z., Zhang W., Meng X., Zhu Y., Han P., et al. Nuclear translocation of HIF-1α induced by influenza A (H1N1) infection is critical to the production of proinflammatory cytokines. Emerg. Microbes. Infect. 2017; 6(5): e39. doi: 10.1038/emi.2017.21. Available at: https://www.nature.com/emi/journal/v6/n5/full/emi201721a.html (accessed 11 Sept 2017)</mixed-citation><mixed-citation xml:lang="en">Guo X., Zhu Z., Zhang W., Meng X., Zhu Y., Han P., et al. Nuclear translocation of HIF-1α induced by influenza A (H1N1) infection is critical to the production of proinflammatory cytokines. Emerg. Microbes. Infect. 2017; 6(5): e39. doi: 10.1038/emi.2017.21. Available at: https://www.nature.com/emi/journal/v6/n5/full/emi201721a.html (accessed 11 Sept 2017)</mixed-citation></citation-alternatives></ref><ref id="cit53"><label>53</label><citation-alternatives><mixed-citation xml:lang="ru">Niyonsaba F., Madera L., Afacan N., Okumura K., Ogawa H., Hancock R.E. The innate defense regulator peptides IDR-HH2, IDR-1002, and IDR-1018 modulate human neutrophil functions. J. Leukoc. Biol. 2013; 94(1): 159–70. doi: 10.1189/jlb.1012497.</mixed-citation><mixed-citation xml:lang="en">Niyonsaba F., Madera L., Afacan N., Okumura K., Ogawa H., Hancock R.E. The innate defense regulator peptides IDR-HH2, IDR-1002, and IDR-1018 modulate human neutrophil functions. J. Leukoc. Biol. 2013; 94(1): 159–70. doi: 10.1189/jlb.1012497.</mixed-citation></citation-alternatives></ref><ref id="cit54"><label>54</label><citation-alternatives><mixed-citation xml:lang="ru">Corriden R., Hollands A., Olson J., Derieux J., Lopez J., Chang J.T., et al. Tamoxifen augments the innate immune function of neutrophils through modulation of intracellular ceramide. Nat. Commun. 2015; 6: 8369. doi: 10.1038/ncomms9369. Available at: https://www.nature.com/articles/ncomms9369 (accessed 11 Sept 2017) 55. Hollands A., Corriden R., Gysler G., Dahesh S., Olson J., Raza Ali S., et al. Natural product anacardic acid from cashew nut shells stimulates neutrophil extracellular trap production and bactericidal activity. J. Biol. Chem. 2016; 291(27): 13964–73.</mixed-citation><mixed-citation xml:lang="en">Corriden R., Hollands A., Olson J., Derieux J., Lopez J., Chang J.T., et al. Tamoxifen augments the innate immune function of neutrophils through modulation of intracellular ceramide. Nat. Commun. 2015; 6: 8369. doi: 10.1038/ncomms9369. Available at: https://www.nature.com/articles/ncomms9369 (accessed 11 Sept 2017) 55. Hollands A., Corriden R., Gysler G., Dahesh S., Olson J., Raza Ali S., et al. Natural product anacardic acid from cashew nut shells stimulates neutrophil extracellular trap production and bactericidal activity. J. Biol. Chem. 2016; 291(27): 13964–73.</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>
