Publication: Pyruvate : Ferredoxin oxidoreductase from Entamoeba histolytica recognized by a monoclonal antibody
Issued Date
1996-03-01
Resource Type
ISSN
01251562
Other identifier(s)
2-s2.0-0030090247
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Mahidol University
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SCOPUS
Bibliographic Citation
Southeast Asian Journal of Tropical Medicine and Public Health. Vol.27, No.1 (1996), 63-70
Suggested Citation
Nitaya Thammapalerd, Daroon Kotimanusvanij, Michael Duchêne, Jacqueline A. Upcroft, Roger Mitchell, Andrew Healey, Nirma Samarawickrema, Savanat Tharavanij, Gerhard Wiedermann, Peter Upcroft Pyruvate : Ferredoxin oxidoreductase from Entamoeba histolytica recognized by a monoclonal antibody. Southeast Asian Journal of Tropical Medicine and Public Health. Vol.27, No.1 (1996), 63-70. Retrieved from: https://repository.li.mahidol.ac.th/handle/123456789/17758
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Title
Pyruvate : Ferredoxin oxidoreductase from Entamoeba histolytica recognized by a monoclonal antibody
Abstract
A mouse monoclonal antibody, Eh208C2-2 MAb, raised against whole cell antigens of Entamoeba histolytica trophozoites of the pathogenic strain HM-1 : IMSS and polyclonal antisera (PAb) against membrane antigens of E. histolytica trophozoites of strain HTH-56 : MUTM were screened against a cDNA library of the pathogenic strain, SFL3. The monoconal antibody detected many phage plaques expressing an E. histolytica protein. The DNA sequence encoding the protein was approximately 55% identical, over 1.100bp, to Trichomonas vaginalis pyruvate : ferredoxin oxidoreductase (PFOR) and pyruvate : flavodoxin oxidoreductase from Klebsiella pneumoniae, Anabaena variabilis and Enterobacter agglomerans. Two of seven clones detected by mouse polyclonal antisera also encoded this protein. Two others encoded Entamoeba Hsp70, another encoded Entamoeba alkyl-hydroperoxide reductase and the remaining two were unidentified sequences. Entamoeba PFOR is an abundant, antigenic protein which may be a useful target for the development of protective host immune responses against invasive amebiasis.