{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,10,6]],"date-time":"2025-10-06T05:59:24Z","timestamp":1759730364749,"version":"3.40.5"},"reference-count":37,"publisher":"Bentham Science Publishers Ltd.","issue":"4","content-domain":{"domain":["eurekaselect.com"],"crossmark-restriction":true},"short-container-title":["PPL"],"published-print":{"date-parts":[[2021,5,19]]},"abstract":"<jats:sec>\n<jats:title>Background:<\/jats:title>\n<jats:p>The O. tesota lectin PF2 is a tetrameric protein with subunits of 33 kDa\nthat recognizes only complex carbohydrates, resistant to proteolytic enzymes and has insecticidal\nactivity against Phaseolus beans pest.<\/jats:p>\n<\/jats:sec>\n<jats:sec>\n<jats:title>Objective:<\/jats:title>\n<jats:p>To explore PF2 lectin features at different protein structural levels and to evaluate the effect\nof temperature and pH on its functionality and conformational stability.<\/jats:p>\n<\/jats:sec>\n<jats:sec>\n<jats:title>Methods:<\/jats:title>\n<jats:p>PF2 lectin was purified by affinity chromatography. Its primary structure was resolved\nby mass spectrometry and analyzed by bioinformatic tools, including its tertiary structure homology\nmodeling. The effect of temperature and pH on its conformational traits and stability was addressed\nby dynamic light scattering, circular dichroism, and intrinsic fluorescence. The hemagglutinating\nactivity was evaluated using a suspension of peripheral blood erythrocytes.<\/jats:p>\n<\/jats:sec>\n<jats:sec>\n<jats:title>Results:<\/jats:title>\n<jats:p>The proposed PF2 folding comprises a high content of beta sheets. At pH 7 and 25\u00b0C, the\nhydrodynamic diameter (Dh) was found to be 12.3 nm which corresponds to the oligomeric native\nstate of PF2 lectin. Dh increased under the other evaluated pH and temperature conditions, suggesting\nprotein aggregation. At basic pH, PF2 exhibited low conformational stability. The native PF2\n(pH 7) retained its full hemagglutinating activity up to 45\u00b0C and exhibited one transition state with\na melting temperature of 76.8\u00b0C.<\/jats:p>\n<\/jats:sec>\n<jats:sec>\n<jats:title>Conclusion:<\/jats:title>\n<jats:p>PF2 showed distinctive characteristics found in legume lectins. The pH influences the\nfunctionality and conformational stability of the protein. PF2 lectin displayed a relatively narrow\nthermostability to the loss of secondary structure and hemagglutinating activity.<\/jats:p>\n<\/jats:sec>","DOI":"10.2174\/0929866527666200813204303","type":"journal-article","created":{"date-parts":[[2020,8,16]],"date-time":"2020-08-16T05:51:26Z","timestamp":1597557086000},"page":"403-413","update-policy":"https:\/\/doi.org\/10.2174\/bsp_crossmark_policy","source":"Crossref","is-referenced-by-count":1,"title":["Insights into the Structural Features, Conformational Stability and Functional Activity of the Olneya tesota PF2 Lectin"],"prefix":"10.2174","volume":"28","author":[{"ORCID":"https:\/\/orcid.org\/0000-0003-1568-0638","authenticated-orcid":true,"given":"Edgar","family":"Acedo-Espinoza","sequence":"first","affiliation":[{"name":"Departamento de Investigaciones Cient\u00edficas y Tecnol\u00f3gicas, Universidad de Sonora, Hermosillo, Sonora 83000, Mexico"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-4057-1778","authenticated-orcid":true,"given":"Irlanda","family":"Lagarda-Diaz","sequence":"additional","affiliation":[{"name":"CONACyT -Universidad de Sonora, Sonora, Mexico"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-9653-9806","authenticated-orcid":true,"given":"Rosina","family":"Cabrera","sequence":"additional","affiliation":[{"name":"Centro de Investigaci\u00f3n y Desarrollo en Agrobiotecnolog\u00eda Alimentaria (Consortium between Centro de Investigaci\u00f3n en Alimentaci\u00f3n y Desarrollo and Centro de Investigaci\u00f3n y Asistencia en Tecnolog\u00eda y Dise\u00f1o del Estado de Jalisco), Pachuca Ciudad del Conocimiento y la Cultura, San Agust\u00edn Tlaxiaca, Hidalgo 42163, Mexico"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-0481-8689","authenticated-orcid":true,"given":"Ana M.","family":"Guzman-Partida","sequence":"additional","affiliation":[{"name":"CONACyT- Centro de Investigaci\u00f3n en Alimentaci\u00f3n y Desarrollo, A.C., Hermosillo, Sonora 83304, Mexico"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-5631-9358","authenticated-orcid":true,"given":"Amir","family":"Maldonado-Arce","sequence":"additional","affiliation":[{"name":"Departamento de F\u00edsica, Universidad de Sonora, Hermosillo, Sonora 83000, Mexico"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-3517-0336","authenticated-orcid":true,"given":"Mar\u00eda M.","family":"Ortega-Nieblas","sequence":"additional","affiliation":[{"name":"Departamento de Investigaciones Cient\u00edficas y Tecnol\u00f3gicas, Universidad de Sonora, Hermosillo, Sonora 83000, Mexico"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-3614-1772","authenticated-orcid":true,"given":"Lerma","family":"Chan-Chan","sequence":"additional","affiliation":[{"name":"CONACyT -Universidad de Sonora, Sonora, Mexico"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-8953-3756","authenticated-orcid":true,"given":"Luz","family":"V\u00e1zquez-Moreno","sequence":"additional","affiliation":[{"name":"CONACyT- Centro de Investigaci\u00f3n en Alimentaci\u00f3n y Desarrollo, A.C., Hermosillo, Sonora 83304, Mexico"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"965","reference":[{"key":"ref=1","doi-asserted-by":"publisher","first-page":"637","DOI":"10.1021\/cr940413g","volume":"98","author":"Lis H.","year":"1998","unstructured":"Lis H.; Sharon N.; Lectins: Carbohydrate-specific proteins that mediate cellular recognition. 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