GeneralMABHeader.jpg
Amoeboid Tvag on VEC.jpg
Biofilm Tvag on VEC.jpg
Cross Sectioin EM_Dark Tvag on VEC.jpg
Illustration of the Vaginal Epithelium.jpg
Illustration showing T vaginalis adherent to vaginal epithelial cells.jpg
Pathology PAPsmear of T. vaginalis on VECs of patient.jpg
Purified Squamous Vaginal Epithelial Cells with normal flora.jpg
Trichomonas vaginalis adherence to HeLa epithelial cells.jpg
GeneralMABHeader.jpg
Amoeboid Tvag on VEC.jpg
Biofilm Tvag on VEC.jpg
Cross Sectioin EM_Dark Tvag on VEC.jpg
Illustration of the Vaginal Epithelium.jpg
Illustration showing T vaginalis adherent to vaginal epithelial cells.jpg
Pathology PAPsmear of T. vaginalis on VECs of patient.jpg
Purified Squamous Vaginal Epithelial Cells with normal flora.jpg
Trichomonas vaginalis adherence to HeLa epithelial cells.jpg

α-Enolase (51.3 kDA)

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References

  • The discovery that the enzyme α-enolase is on the surface of T. vaginalis and is a plasminogen- binding protein.

ALD13, ALD55, ALD97, ALD11, ALD25

  • The discovery that a novel, chimeric protein derived from epitopes of 3 metabolic enzymes (AEG::SOE2) is a perfect serodiagnostic target equal to α-actinin.

  • Recombinant Protein of Immunogenic Metabolic Enzyme Epitopes of Trichomonas vaginalis are Common to Humans and Microorganisms