{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,4]],"date-time":"2026-09-04T02:33:26Z","timestamp":1788489206179,"version":"build-2803163510"},"reference-count":22,"publisher":"American Society of Tropical Medicine and Hygiene","issue":"1","license":[{"start":{"date-parts":[[2023,7,5]],"date-time":"2023-07-05T00:00:00Z","timestamp":1688515200000},"content-version":"unspecified","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2023,7,5]]},"abstract":"<jats:title>ABSTRACT.<\/jats:title>\n<jats:p>Paragonimiasis is an important but neglected foodborne trematodiasis caused by <jats:italic>Paragonimus mexicanus<\/jats:italic> in Costa Rica. Immunological techniques for diagnosing this parasitosis in humans do not exist in Central America. The objective of the present study was to use recombinant <jats:italic>Paragonimus westermani<\/jats:italic> cysteine protease 7 to standardize an ELISA for the detection of antibodies against <jats:italic>Paragonimus<\/jats:italic> spp. Human sera positive for <jats:italic>P. westermani<\/jats:italic>,<jats:italic> P. mexicanus<\/jats:italic>, or <jats:italic>Paragonimus<\/jats:italic> spp., human sera infected with other helminths, as well as sera of healthy humans without parasitic infections, were analyzed. The sensitivity of the ELISA was 92.9%, and the specificity was 91.9%. This report is the first to describe the development of an ELISA for the diagnosis of <jats:italic>Paragonimus<\/jats:italic> spp. in Costa Rica and Central America. Using this ELISA in the health system of Costa Rica is recommended to detect infections.<\/jats:p>","DOI":"10.4269\/ajtmh.22-0452","type":"journal-article","created":{"date-parts":[[2023,5,30]],"date-time":"2023-05-30T15:13:56Z","timestamp":1685459636000},"page":"166-169","source":"Crossref","is-referenced-by-count":3,"title":["Detection of Human Paragonimiasis by ELISA Using Recombinant Paragonimus westermani Cysteine Protease 7"],"prefix":"10.4269","volume":"109","author":[{"given":"Luana Gabriele","family":"Andrade-Gomes","sequence":"first","affiliation":[{"name":"Maestr\u00eda en Enfermedades Tropicales, Posgrado Regional en Ciencias Veterinarias Tropicales, Universidad Nacional, Heredia, Costa Rica;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mar\u00eda J.","family":"Zuniga","sequence":"additional","affiliation":[{"name":"Maestr\u00eda en Enfermedades Tropicales, Posgrado Regional en Ciencias Veterinarias Tropicales, Universidad Nacional, Heredia, Costa Rica;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Gaby","family":"Dolz","sequence":"additional","affiliation":[{"name":"Maestr\u00eda en Enfermedades Tropicales, Posgrado Regional en Ciencias Veterinarias Tropicales, Universidad Nacional, Heredia, Costa Rica;"},{"name":"Laboratorio de Zoonosis y Entomolog\u00eda, Programa de Medicina Poblacional, Escuela de Medicina Veterinaria, Universidad Nacional, Heredia, Costa Rica;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Frank","family":"Solano-Campos","sequence":"additional","affiliation":[{"name":"Escuela de Ciencias Biol\u00f3gicas, Universidad Nacional, Heredia, Costa Rica"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"2795","reference":[{"key":"b1","series-title":"Oxf Med Case Rep","first-page":"218","article-title":"Case series of paragonimiasis from Nepal","volume":"11","author":"Sah","year":"2017"},{"key":"b2","series-title":"BMC Res 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recombinant PsCP for detection of Paragonimus skrjabini infection in human","volume":"116","author":"Yu","year":"2017"},{"key":"b12","series-title":"J Infect Dis","first-page":"1373","article-title":"Recombinant Paragonimus westermani yolk ferritin is a useful serodiagnostic antigen","volume":"185","author":"Kim","year":"2002"},{"key":"b13","series-title":"Clin Diagn Lab Immunol","first-page":"932","article-title":"Structural and immunological characteristics of a 28-kilodalton cruzipain-like cysteine protease of Paragonimus westermani expressed in the definitive host stage","volume":"7","author":"Yun","year":"2000"},{"key":"b14","series-title":"Parasitol Res","first-page":"4457","article-title":"Molecular and immunological characterization of cathepsin L-like cysteine protease of Paragonimus pseudoheterotremus.","volume":"115","author":"Yoonuan","year":"2016"},{"key":"b15","series-title":"Parasitol Int","first-page":"37","article-title":"Expression characteristics and specific antibody reactivity of diverse cathepsin F members of Paragonimus westermani.","volume":"64","author":"Ahn","year":"2015"},{"key":"b16","series-title":"Parasitol Res","first-page":"535","article-title":"Characterization and localization of antigens for serodiagnosis of human paragonimiasis","volume":"120","author":"Curtis","year":"2021"},{"key":"b17","author":"Hern\u00e1ndez-Chea","year":"2016"},{"key":"b18","series-title":"Cienc Vet (Heredia)","first-page":"44","article-title":"Evaluaci\u00f3n de prote\u00ednas recombinantes PwCP4, PwCP7 y PwCP9 usando sueros de ratas Wistar infectadas experimentalmente con Paragonimus mexicanus.","volume":"36","author":"Andrade-Gomes","year":"2017"},{"key":"b19","series-title":"Curr Protoc Protein Sci","article-title":"Preparation and extraction of insoluble (inclusion\u2010body) proteins from Escherichia coli.","author":"Palmer","year":"2012"},{"key":"b20","series-title":"Immunochemistry","first-page":"289","article-title":"The effect of urea of antibody-antigen reactions","volume":"1","author":"Bata","year":"1964"},{"key":"b21","series-title":"Int J Mol Sci","first-page":"1395","article-title":"Rational design of recombinant papain-like cysteine protease: Optimal domain structure and expression conditions for wheat-derived enzyme triticain-\u03b1","volume":"18","author":"Gorokhovets","year":"2017"},{"key":"b22","series-title":"Appl Microbiol Biotechnol","first-page":"837","article-title":"A simple and effective strategy for solving the problem of inclusion bodies in recombinant protein technology: His-tag deletions enhance soluble expression","volume":"97","author":"Zhu","year":"2013"}],"container-title":["The American Journal of Tropical Medicine and 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