Parasitology Research

, Volume 107, Issue 3, pp 761–764 | Cite as

Glycosylation of the major polar tube protein of Encephalitozoon cuniculi

  • Boumediene Bouzahzah
  • Louis M. WeissEmail author
Short Communication


To infect their host cells the Microsporidia use a unique invasion organelle, the polar tube complex. During infection, the organism is injected into the host cell through the hollow polar tube formed during spore germination. Currently, three proteins, PTP1, PTP2, and PTP3 have been identified by immunological and molecular techniques as being components of this structure. Genomic data suggests that Microsporidia are capable of O-linked, but not N-linked glycosylation as a post-translational protein modification. Cells were infected with Encephalitozoon cunicuili, labeled with radioactive mannose or glucosamine, and the polar tube proteins were examined for glycosylation. PTP1 was clearly demonstrated to be mannosylated consistent with 0-glycosylation. In addition, it was evident that several other proteins were mannosylated, but no labeling was seen with glucosamine. The observed post-translational mannosylation of PTP1 may be involved in the functional properties of the polar tube, including its adherence to host cells during penetration.


Polar Tube Mannose Glucosamine Spore Wall Host Cell Membrane 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.



This work was supported by Grant AI31788 from the National Institute of Allergy and Infectious Diseases.


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Copyright information

© Springer-Verlag 2010

Authors and Affiliations

  1. 1.Department of Pathology, Division of Parasitology and Tropical MedicineAlbert Einstein College of MedicineBronxUSA
  2. 2.Department of Medicine, Division of Infectious DiseasesAlbert Einstein College of MedicineBronxUSA

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