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International Journal of Microbiology
Volume 2010, Article ID 523654, 6 pages
Research Article

Expression and Localization of an Hsp70 Protein in the Microsporidian Encephalitozoon cuniculi

Department of Microbiology, James H. Quillen College of Medicine, East Tennessee State University, Box 70579, Johnson City, TN 37614, USA

Received 19 April 2010; Accepted 22 June 2010

Academic Editor: Robert P. Gunsalus

Copyright © 2010 Carrie E. Jolly et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.


Microsporidia spore surface proteins are an important, under investigated aspect of spore/host cell attachment and infection. For comparison analysis of surface proteins, we required an antibody control specific for an intracellular protein. An endoplasmic reticulum-associated heat shock protein 70 family member (Hsp70; ECU02_0100; “C1”) was chosen for further analysis. DNA encoding the C1 hsp70 was amplified, cloned and used to heterologously express the C1 Hsp70 protein, and specific antiserum was generated. Two-dimensional Western blotting analysis showed that the purified antibodies were monospecific. Immunoelectron microscopy of developing and mature E. cuniculi spores revealed that the protein localized to internal structures and not to the spore surface. In spore adherence inhibition assays, the anti-C1 antibodies did not inhibit spore adherence to host cell surfaces, whereas antibodies to a known surface adhesin (EnP1) did so. In future studies, the antibodies to the ‘C1’ Hsp70 will be used to delineate spore surface protein expression.