{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,22]],"date-time":"2026-09-22T14:35:16Z","timestamp":1790087716705,"version":"4.0.1"},"reference-count":71,"publisher":"American Society for Microbiology","issue":"6","license":[{"start":{"date-parts":[[2015,6,1]],"date-time":"2015-06-01T00:00:00Z","timestamp":1433116800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/journals.asm.org\/non-commercial-tdm-license"}],"content-domain":{"domain":["journals.asm.org"],"crossmark-restriction":true},"short-container-title":["Infect Immun"],"published-print":{"date-parts":[[2015,6]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n          <jats:p>\n            We have previously shown that secreted phospholipases A\n            <jats:sub>2<\/jats:sub>\n            (sPLA\n            <jats:sub>2<\/jats:sub>\n            s) from animal venoms inhibit the\n            <jats:italic>in vitro<\/jats:italic>\n            development of\n            <jats:named-content content-type=\"genus-species\">Plasmodium falciparum<\/jats:named-content>\n            , the agent of malaria. In addition, the inflammatory-type human group IIA (hGIIA) sPLA\n            <jats:sub>2<\/jats:sub>\n            circulates at high levels in the serum of malaria patients. However, the role of the different human sPLA\n            <jats:sub>2<\/jats:sub>\n            s in host defense against\n            <jats:named-content content-type=\"genus-species\">P. falciparum<\/jats:named-content>\n            has not been investigated. We show here that 4 out of 10 human sPLA\n            <jats:sub>2<\/jats:sub>\n            s, namely, hGX, hGIIF, hGIII, and hGV, exhibit potent\n            <jats:italic>in vitro<\/jats:italic>\n            anti-\n            <jats:named-content content-type=\"genus-species\">Plasmodium<\/jats:named-content>\n            properties with half-maximal inhibitory concentrations (IC\n            <jats:sub>50<\/jats:sub>\n            s) of 2.9 \u00b1 2.4, 10.7 \u00b1 2.1, 16.5 \u00b1 9.7, and 94.2 \u00b1 41.9 nM, respectively. Other human sPLA2s, including hGIIA, are inactive. The inhibition is dependent on sPLA\n            <jats:sub>2<\/jats:sub>\n            catalytic activity and primarily due to hydrolysis of plasma lipoproteins from the parasite culture. Accordingly, purified lipoproteins that have been prehydrolyzed by hGX, hGIIF, hGIII, and hGV are more toxic to\n            <jats:named-content content-type=\"genus-species\">P. falciparum<\/jats:named-content>\n            than native lipoproteins. However, the total enzymatic activities of human sPLA\n            <jats:sub>2<\/jats:sub>\n            s on purified lipoproteins or plasma did not reflect their inhibitory activities on\n            <jats:named-content content-type=\"genus-species\">P. falciparum<\/jats:named-content>\n            . For instance, hGIIF is 9-fold more toxic than hGV but releases a lower quantity of nonesterified fatty acids (NEFAs). Lipidomic analyses of released NEFAs from lipoproteins demonstrate that sPLA\n            <jats:sub>2<\/jats:sub>\n            s with anti-\n            <jats:named-content content-type=\"genus-species\">Plasmodium<\/jats:named-content>\n            properties are those that release polyunsaturated fatty acids (PUFAs), with hGIIF being the most selective enzyme. NEFAs purified from lipoproteins hydrolyzed by hGIIF were more potent at inhibiting\n            <jats:named-content content-type=\"genus-species\">P. falciparum<\/jats:named-content>\n            than those from hGV, and PUFA-enriched liposomes hydrolyzed by sPLA\n            <jats:sub>2<\/jats:sub>\n            s were highly toxic, demonstrating the critical role of PUFAs. The selectivity of sPLA\n            <jats:sub>2<\/jats:sub>\n            s toward low- and high-density (LDL and HDL, respectively) lipoproteins and their ability to directly attack parasitized erythrocytes further explain their anti-\n            <jats:named-content content-type=\"genus-species\">Plasmodium<\/jats:named-content>\n            activity. Together, our findings indicate that 4 human sPLA\n            <jats:sub>2<\/jats:sub>\n            s are active against\n            <jats:named-content content-type=\"genus-species\">P. falciparum<\/jats:named-content>\n            <jats:italic>in vitro<\/jats:italic>\n            and pave the way to future investigations on their\n            <jats:italic>in vivo<\/jats:italic>\n            contribution in malaria pathophysiology.\n          <\/jats:p>","DOI":"10.1128\/iai.02474-14","type":"journal-article","created":{"date-parts":[[2015,4,1]],"date-time":"2015-04-01T09:46:18Z","timestamp":1427881578000},"page":"2453-2465","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":15,"title":["<i>In Vitro<\/i>\n            Anti-Plasmodium falciparum Properties of the Full Set of Human Secreted Phospholipases A\n            <sub>2<\/sub>"],"prefix":"10.1128","volume":"83","author":[{"given":"Carole","family":"Guillaume","sequence":"first","affiliation":[{"name":"Mus\u00e9um National d'Histoire Naturelle, UMR 7245 CNRS\/MNHN, MCAM \u00e9quipe BAMEE, Paris, France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Christine","family":"Payr\u00e9","sequence":"additional","affiliation":[{"name":"Institut de Pharmacologie Mol\u00e9culaire et Cellulaire, CNRS et Universit\u00e9 de Nice Sophia Antipolis, UMR 7275, Sophia Antipolis, Valbonne, France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ikram","family":"Jemel","sequence":"additional","affiliation":[{"name":"Institut de Pharmacologie Mol\u00e9culaire et Cellulaire, CNRS et Universit\u00e9 de Nice Sophia Antipolis, UMR 7275, Sophia Antipolis, Valbonne, France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Louise","family":"Jeammet","sequence":"additional","affiliation":[{"name":"Institut de Pharmacologie 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