Immunolocalisation of an ABC transporter, P-glycoprotein, in the eggshells and cuticles of free-living and parasitic stages of Haemonchus contortus

Recent data have suggested that P-glycoprotein (Pgp), working as membrane efflux “pumps”, plays a major role in the transport of anthelmintic drugs in parasitic nematodes of ruminants. Flow cytometry analyses has shown that active Pgp is probably present in the external layers of Haemonchus contortu...

Full description

Saved in:
Bibliographic Details
Published inParasitology research (1987) Vol. 96; no. 3; pp. 142 - 148
Main Authors RIOU, Mickaël, KOCH, Christine, DELALEU, Bernadette, BERTHON, Patricia, KERBOEUF, Dominique
Format Journal Article
LanguageEnglish
Published Berlin Springer-Verlag 01.06.2005
Springer
Springer Verlag (Germany)
Subjects
Online AccessGet full text

Cover

Loading…
More Information
Summary:Recent data have suggested that P-glycoprotein (Pgp), working as membrane efflux “pumps”, plays a major role in the transport of anthelmintic drugs in parasitic nematodes of ruminants. Flow cytometry analyses has shown that active Pgp is probably present in the external layers of Haemonchus contortus eggshells, following staining with the mouse monoclonal anti-human MDR1 antibody UIC2, which binds to Pgp in its active conformation. We evaluated the presence and distribution of this protein in the envelopes (eggshells and cuticles) of H. contortus and compared the various stages (eggs, L₁–L₂ larvae, L₃ larvae, adult male and female worms). Electrophoresis revealed a 170-kDa band, corresponding to the molecular weight of Pgp in all stages. Indirect immunofluorescence staining with UIC2 showed Pgp to be located in the external layer of eggshells or cuticles. Transmission electron microscopy was used to localise Pgp more accurately in the three layers of the eggshells and cuticles. The conformation and biological functions of this protein, which we did not expect to find in such structures, remain to be determined.
Bibliography:http://dx.doi.org/10.1007/s00436-005-1345-3
ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
ISSN:0932-0113
1432-1955
DOI:10.1007/s00436-005-1345-3