November 1991
Volume 32, Issue 12
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Articles  |   November 1991
Neuraminidase activity in acanthamoeba species trophozoites and cysts.
Author Affiliations
  • J L Pellegrin
    Division of Geographic Medicine and Infectious Diseases, New England Medical Center Hospitals, Tufts University School of Medicine, Boston, Massachusetts.
  • E Ortega-Barria
    Division of Geographic Medicine and Infectious Diseases, New England Medical Center Hospitals, Tufts University School of Medicine, Boston, Massachusetts.
  • M Barza
    Division of Geographic Medicine and Infectious Diseases, New England Medical Center Hospitals, Tufts University School of Medicine, Boston, Massachusetts.
  • J Baum
    Division of Geographic Medicine and Infectious Diseases, New England Medical Center Hospitals, Tufts University School of Medicine, Boston, Massachusetts.
  • M E Pereira
    Division of Geographic Medicine and Infectious Diseases, New England Medical Center Hospitals, Tufts University School of Medicine, Boston, Massachusetts.
Investigative Ophthalmology & Visual Science November 1991, Vol.32, 3061-3066. doi:
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      J L Pellegrin, E Ortega-Barria, M Barza, J Baum, M E Pereira; Neuraminidase activity in acanthamoeba species trophozoites and cysts.. Invest. Ophthalmol. Vis. Sci. 1991;32(12):3061-3066.

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Abstract

Acanthamoeba species, a widely distributed group of free-living amoeba, can infect humans and spread hematogenously after direct interaction with the mucosal surfaces. The mechanism underlying Acanthamoeba damage to the target cell is unknown. The authors report that trophozoites and cysts of Acanthamoeba species exhibit a neuraminidase activity that is membrane associated and released into the culture medium at the start of the logarithmic phase of growth. The enzyme activity is optimal at pH 5 and at 25-30 degrees C. Live parasites release sialic acid from human cells. Therefore, the neuraminidase of Acanthamoeba species could be relevant in the colonization and damage of the sialic acid-rich corneal epithelium and in the alterations of glycolipids associated with meningoencephalitis.

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