{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,4]],"date-time":"2026-08-04T05:52:13Z","timestamp":1785822733228,"version":"3.56.0"},"update-to":[{"DOI":"10.1371\/journal.pntd.0012069","type":"new_version","label":"New version","source":"publisher","updated":{"date-parts":[[2024,9,12]],"date-time":"2024-09-12T00:00:00Z","timestamp":1726099200000}}],"reference-count":73,"publisher":"Public Library of Science (PLoS)","issue":"8","license":[{"start":{"date-parts":[[2024,8,30]],"date-time":"2024-08-30T00:00:00Z","timestamp":1724976000000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100004837","name":"Ministerio de Ciencia e Innovaci\u00f3n","doi-asserted-by":"publisher","award":["RTI2018-093463-J-100"],"award-info":[{"award-number":["RTI2018-093463-J-100"]}],"id":[{"id":"10.13039\/501100004837","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100004837","name":"Ministerio de Ciencia e Innovaci\u00f3n","doi-asserted-by":"publisher","award":["CNS2022-135561"],"award-info":[{"award-number":["CNS2022-135561"]}],"id":[{"id":"10.13039\/501100004837","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100014180","name":"Junta de Castilla y Le\u00f3n","doi-asserted-by":"publisher","award":["CLU-2019-05"],"award-info":[{"award-number":["CLU-2019-05"]}],"id":[{"id":"10.13039\/501100014180","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001602","name":"Science Foundation Ireland","doi-asserted-by":"publisher","award":["17\/RP\/5368"],"award-info":[{"award-number":["17\/RP\/5368"]}],"id":[{"id":"10.13039\/501100001602","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100002081","name":"Irish Research Council","doi-asserted-by":"publisher","award":["RCS1904"],"award-info":[{"award-number":["RCS1904"]}],"id":[{"id":"10.13039\/501100002081","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["www.plosntds.org"],"crossmark-restriction":false},"short-container-title":["PLoS Negl Trop Dis"],"abstract":"<jats:p>Enolase is a 47 kDa enzyme that functions within the glycolysis and gluconeogenesis pathways involved in the reversible conversion of D-2-phosphoglycerate (2PGA) to phosphoenolpyruvate (PEP). However, in the context of host-pathogen interactions, enolase from different species of parasites, fungi and bacteria have been shown to contribute to adhesion processes by binding to proteins of the host extracellular matrix (ECM), such as fibronectin (FN) or laminin (LM). In addition, enolase is a plasminogen (PLG)-binding protein and induces its activation to plasmin, the main protease of the host fibrinolytic system. These secondary \u2018moonlighting\u2019 functions of enolase are suggested to facilitate pathogen migration through host tissues. This study aims to uncover the moonlighting role of enolase from the parasite <jats:italic>Fasciola hepatica<\/jats:italic>, shedding light on its relevance to host-parasite interactions in fasciolosis, a global zoonotic disease of increasing concern. A purified recombinant form of <jats:italic>F<\/jats:italic>. <jats:italic>hepatica<\/jats:italic> enolase (rFhENO), functioning as an active homodimeric glycolytic enzyme of ~94 kDa, was successfully obtained, fulfilling its canonical role. Immunoblotting studies on adult worm extracts showed that the enzyme is present in the tegument and the excretory\/secretory products of the parasite, which supports its key role at the host-parasite interface. Confocal immunolocalisation studies of the protein in newly excysted juveniles and adult worms also localised its expression within the parasite tegument. Finally, we showed by ELISA that rFhENO can act as a parasitic adhesin by binding host LM, but not FN. rFhENO also binds PLG and enhances its conversion to plasmin in the presence of the tissue-type and urokinase-type PLG activators (t-PA and u-PA). This moonlighting adhesion-like function of the glycolytic protein enolase could contribute to the mechanisms by which <jats:italic>F<\/jats:italic>. <jats:italic>hepatica<\/jats:italic> efficiently invades and migrates within its host and encourages further research efforts that are designed to impede this function by vaccination or drug design.<\/jats:p>","DOI":"10.1371\/journal.pntd.0012069","type":"journal-article","created":{"date-parts":[[2024,8,30]],"date-time":"2024-08-30T19:37:55Z","timestamp":1725046675000},"page":"e0012069","update-policy":"https:\/\/doi.org\/10.1371\/journal.pntd.corrections_policy","source":"Crossref","is-referenced-by-count":9,"title":["Moonlighting on the Fasciola hepatica tegument: Enolase, a glycolytic enzyme, interacts with the extracellular matrix and fibrinolytic system of the host"],"prefix":"10.1371","volume":"18","author":[{"given":"Eve","family":"O\u2019Kelly","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Krystyna","family":"Cwiklinski","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Carolina","family":"De Marco Verissimo","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Nichola Eliza Davies","family":"Calvani","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jes\u00fas","family":"L\u00f3pez Corrales","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Heather","family":"Jewhurst","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Andrew","family":"Flaus","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Richard","family":"Lalor","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Judit","family":"Serrat","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"John P.","family":"Dalton","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-4279-4761","authenticated-orcid":true,"given":"Javier","family":"Gonz\u00e1lez-Miguel","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"340","published-online":{"date-parts":[[2024,8,30]]},"reference":[{"issue":"Pt 3","key":"pntd.0012069.ref001","doi-asserted-by":"crossref","first-page":"359","DOI":"10.1017\/S0031182000081919","article-title":"The evolution of tissue migration by parasitic nematode larvae","volume":"111","author":"AF Read","year":"1995","journal-title":"Parasitology"},{"issue":"6","key":"pntd.0012069.ref002","doi-asserted-by":"crossref","first-page":"273","DOI":"10.1016\/j.pt.2005.04.003","article-title":"Tissue migration by parasitic helminths\u2014an immunoevasive strategy?","volume":"21","author":"Mulcahy G","year":"2005","journal-title":"Trends Parasitol"},{"key":"pntd.0012069.ref003","volume-title":"Streptococcus pyogenes: Basic Biology to Clinical Manifestations.","author":"M Rohde","year":"2022"},{"issue":"3","key":"pntd.0012069.ref004","doi-asserted-by":"crossref","first-page":"277","DOI":"10.1007\/s00430-019-00644-3","article-title":"Interaction with the host: the role of fibronectin and extracellular matrix proteins in the adhesion of Gram-negative bacteria","volume":"209","author":"DJ Vaca","year":"2020","journal-title":"Med Microbiol Immunol"},{"key":"pntd.0012069.ref005","doi-asserted-by":"crossref","first-page":"610189","DOI":"10.3389\/fmed.2021.610189","article-title":"The Charming World of the Extracellular Matrix: A Dynamic and Protective Network of the Intestinal Wall.","volume":"8","author":"S Pompili","year":"2021","journal-title":"Front Med (Lausanne)."},{"key":"pntd.0012069.ref006","doi-asserted-by":"crossref","first-page":"205","DOI":"10.1016\/S0065-308X(09)69004-7","article-title":"Chapter 4. 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