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<article 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" xmlns:ali="http://www.niso.org/schemas/ali/1.0/" article-type="research-article" dtd-version="1.2" xml:lang="en"><front><journal-meta><journal-id journal-id-type="publisher-id">Current Protein &amp; Peptide Science</journal-id><journal-title-group><journal-title xml:lang="en">Current Protein &amp; Peptide Science</journal-title><trans-title-group xml:lang="ru"><trans-title>Current Protein &amp; Peptide Science</trans-title></trans-title-group></journal-title-group><issn publication-format="print">1389-2037</issn><issn publication-format="electronic">1875-5550</issn><publisher><publisher-name xml:lang="en">Bentham Science</publisher-name></publisher></journal-meta><article-meta><article-id pub-id-type="publisher-id">645643</article-id><article-id pub-id-type="doi">10.2174/0113892037275751231221053730</article-id><article-categories><subj-group subj-group-type="toc-heading"><subject>Life Sciences</subject></subj-group><subj-group subj-group-type="article-type"><subject>Research Article</subject></subj-group></article-categories><title-group><article-title xml:lang="en">A Review of the Leishmanicidal Properties of Lectins</article-title></title-group><contrib-group><contrib contrib-type="author"><name><surname>Grangeiro</surname><given-names>Yasmim</given-names></name><email>info@benthamscience.net</email><xref ref-type="aff" rid="aff1"/></contrib><contrib contrib-type="author"><name><surname>Santos</surname><given-names>Ana</given-names></name><email>info@benthamscience.net</email><xref ref-type="aff" rid="aff2"/></contrib><contrib contrib-type="author"><name><surname>Barbosa</surname><given-names>Flávia</given-names></name><email>info@benthamscience.net</email><xref ref-type="aff" rid="aff2"/></contrib><contrib contrib-type="author"><name><surname>Roma</surname><given-names>Renato</given-names></name><email>info@benthamscience.net</email><xref ref-type="aff" rid="aff1"/></contrib><contrib contrib-type="author"><name><surname>Souza</surname><given-names>Racquel</given-names></name><email>info@benthamscience.net</email><xref ref-type="aff" rid="aff2"/></contrib><contrib contrib-type="author"><name><surname>Silva</surname><given-names>Cláudio</given-names></name><email>info@benthamscience.net</email><xref ref-type="aff" rid="aff2"/></contrib><contrib contrib-type="author"><name><surname>Teixeira</surname><given-names>Claudener</given-names></name><email>info@benthamscience.net</email><xref ref-type="aff" rid="aff3"/></contrib></contrib-group><aff id="aff1"><institution>Departamento de Bioquímica, Universidade Federal do Ceará</institution></aff><aff id="aff2"><institution>Faculdade de Medicina, Universidade Federal do Cariri</institution></aff><aff id="aff3"><institution>Centro de Ciências Agrárias e da biodiversidade, Universidade Federal do Cariri</institution></aff><pub-date date-type="pub" iso-8601-date="2024-06-01" publication-format="electronic"><day>01</day><month>06</month><year>2024</year></pub-date><volume>25</volume><issue>6</issue><issue-title xml:lang="ru"/><fpage>443</fpage><lpage>453</lpage><history><date date-type="received" iso-8601-date="2025-01-11"><day>11</day><month>01</month><year>2025</year></date></history><permissions><copyright-statement xml:lang="en">Copyright ©; 2024, Bentham Science Publishers</copyright-statement><copyright-year>2024</copyright-year><copyright-holder xml:lang="en">Bentham Science Publishers</copyright-holder><ali:free_to_read xmlns:ali="http://www.niso.org/schemas/ali/1.0/"/></permissions><self-uri xlink:href="https://journals.eco-vector.com/1389-2037/article/view/645643">https://journals.eco-vector.com/1389-2037/article/view/645643</self-uri><abstract xml:lang="en"><p id="idm46466589530512">Lectins are proteins widely distributed among plants, animals and microorganisms that have the ability to recognize and interact with specific carbohydrates. They have varied biological activities, such as the inhibition of the progression of infections caused by fungi, bacteria, viruses and protozoa, which is related to the interaction of these proteins with the carbohydrates present in the cell walls of these microorganisms. Leishmaniasis are a group of endemic infectious diseases caused by protozoa of the genus Leishmania. In vitro and in vivo tests with promastigotes and amastigotes of Leishmania demonstrated that lectins have the ability to interact with glycoconjugates present on the cell surface of the parasite, it prevents their development through various mechanisms of action, such as the production of ROS and alteration of membrane integrity, and can also interact with defense cells present in the human body, thus showing that these molecules can be considered alternative pharmacological targets for the treatment of leishmaniasis. The objective of the present work is to carry out a bibliographic review on lectins with leishmanicidal activity, emphasizing the advances and perspectives of research in this theme. Through the analysis of the selected studies, we were able to conclude that lectins have great potential for inhibiting the development of leishmaniasis. However, there are still few studies on this subject.</p></abstract><kwd-group xml:lang="en"><kwd>Carbohydrate recognition domain</kwd><kwd>glycoconjugates</kwd><kwd>interaction</kwd><kwd>lectins</kwd><kwd>leishmaniasis</kwd><kwd>endemic infectious diseases.</kwd></kwd-group></article-meta></front><body></body><back><ref-list><ref id="B1"><label>1.</label><mixed-citation>Peumans, W.J.; Van Damme, E. Lectins as plant defense proteins. Plant Physiol., 1995, 109(2), 347-352. doi: 10.1104/pp.109.2.347 PMID: 7480335</mixed-citation></ref><ref id="B2"><label>2.</label><mixed-citation>Povineli, K.L.; Finardi Filho, F. The multiple functions of plant lectins. 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