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Plasmodium falciparum lacks sialidase and trans-sialidase activity

Published online by Cambridge University Press:  06 April 2009

B. Clough ,
F. A. Atilola ,
N. Healy ,
M. E. A. Pereira ,
R. C. Bethell ,
C. R. Penn  and
G. Pasvol
B. Clough*
Affiliation:
Department of Infection and Tropical Medicine, Imperial College School of Medicine, Northwick Park Hospital, Middlesex HA 1 3UJ, UK
F. A. Atilola
Affiliation:
Department of Infection and Tropical Medicine, Imperial College School of Medicine, Northwick Park Hospital, Middlesex HA 1 3UJ, UK
N. Healy
Affiliation:
Glaxo Research and Development Ltd, Stevenage, Hertfordshire, UK
M. E. A. Pereira
Affiliation:
Tropical Diseases Research Unit, Tupper Research Institute, Tufts-New England Medical Centre Hospitals, Boston, Massachusetts, USA
R. C. Bethell
Affiliation:
Glaxo Research and Development Ltd, Stevenage, Hertfordshire, UK
C. R. Penn
Affiliation:
Glaxo Research and Development Ltd, Stevenage, Hertfordshire, UK
G. Pasvol
Affiliation:
Department of Infection and Tropical Medicine, Imperial College School of Medicine, Northwick Park Hospital, Middlesex HA 1 3UJ, UK
*
* Corresponding author.
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Summary

Sialic acid on the red cell surface plays a major role in invasion by the malaria parasite Plasmodium falciparum. The NeuAc(α2,3) Gal motif on the O-linked tetrasaccharides of the red cell glycophorins is a recognition site for the parasite erythrocyte-binding antigen (EBA-175). Consequently, the interaction of P. falciparum and the red cell might share homology with that of the influenza virus. The cellular interactions of P. falciparum were examined for their sensitivity to 4-guanidino-2,3-didehydro-D-N-acetyl neuraminic acid (4-guanidino Neu5Ac2en), a potent inhibitor of influenza virus sialidase. Parasite invasion and subsequent development was unaffected by the sialidase inhibitor. The inhibitor did not affect rosette formation of parasite-infected erythrocytes with uninfected cells nor their cytoadherence to C32 melanoma cells. Furthermore, we were unable to confirm the presence of a previously reported parasite sialidase using sensitive fluorometric or haemagglutination assays, neither was any malarial trans-sialidase identified. We conclude that P. falciparum possesses neither sialidase nor trans-sialidase activity and that an inhibitor of influenza virus sialidase has no effect on important cellular interactions of this parasite.

Keywords

malariasialidaseinvasionrosettingcytoadherence.
Type
Research Article
Information
Parasitology , Volume 112 , Issue 5 , May 1996 , pp. 443 - 449
Copyright
Copyright © Cambridge University Press 1996

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