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On the other hand, tissue invasion by many pathogens has often been associated with increased matrix metalloprotease (MMP) activity in the invaded tissues. By employing cell biology and reverse genetics, we studied the expression and explored putative functions of one of the three MMPs encoded in the genome of the malaria vector\n            <jats:named-content content-type=\"genus-species\">Anopheles gambiae<\/jats:named-content>\n            , namely, the\n            <jats:named-content content-type=\"genus-species\">Anopheles gambiae<\/jats:named-content>\n            <jats:italic>MMP1<\/jats:italic>\n            (\n            <jats:italic>AgMMP1<\/jats:italic>\n            ) gene, during the processes of blood digestion, midgut epithelium invasion by\n            <jats:named-content content-type=\"genus-species\">Plasmodium<\/jats:named-content>\n            ookinetes, and oocyst development. We show that AgMMP1 exists in two alternative isoforms resulting from alternative splicing; one secreted (S-MMP1) and associated with hemocytes, and one membrane type (MT-MMP1) enriched in the cell attachment sites of the midgut epithelium. MT-MMP1 showed a remarkable response to ookinete midgut invasion manifested by increased expression, enhanced zymogen maturation, and subcellular redistribution, all indicative of an implication in the midgut epithelial healing that accompanies ookinete invasion. Importantly, RNA interference (RNAi)-mediated silencing of the\n            <jats:italic>AgMMP1<\/jats:italic>\n            gene revealed a postinvasion protective function of AgMMP1 during oocyst development. The combined results link for the first time an MMP with vector competence and mosquito-\n            <jats:named-content content-type=\"genus-species\">Plasmodium<\/jats:named-content>\n            interactions.\n          <\/jats:p>","DOI":"10.1128\/iai.02080-14","type":"journal-article","created":{"date-parts":[[2014,9,3]],"date-time":"2014-09-03T12:51:37Z","timestamp":1409748697000},"page":"4865-4877","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":22,"title":["Functional Characterization of Anopheles Matrix Metalloprotease 1 Reveals Its Agonistic Role during Sporogonic Development of Malaria Parasites"],"prefix":"10.1128","volume":"82","author":[{"given":"Evi","family":"Goulielmaki","sequence":"first","affiliation":[{"name":"Institute of Molecular Biology and Biotechnology, Foundation of Research and Technology-Hellas, Heraklion, Crete, Greece"},{"name":"Biology Department, University of Crete, Heraklion, Crete, 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