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Biochemical surface components of Brugia pahangi microfilariae

Published online by Cambridge University Press:  06 April 2009

G. Sayers
Affiliation:
Wolfson Tropical Pathology Unit and Medical Helminthology, London School of Hygiene and Tropical Medicine, London
C. D. Mackenzie
Affiliation:
Wolfson Tropical Pathology Unit and Medical Helminthology, London School of Hygiene and Tropical Medicine, London
D. A. Denham
Affiliation:
Wolfson Tropical Pathology Unit and Medical Helminthology, London School of Hygiene and Tropical Medicine, London

Summary

The sheath and cuticle of microfilariae of Brugia pahangi were examined by electron microscopy and the presence of various proteins, carbohydrate and enzymes sought. The epicuticle of microfilariae consists of a pentalaminate structure (24·0 ± 1·4 nm), a cortex (13·7 ± 3·6 nm) and a basal zone (27·8 ±4·8 nm) which is often banded in appearance. The pentalaminate layers are not continuous at the base of the interannular grooves. The sheath and the epicuticle of B. pahangi stained positively with concanavalin A and saccharated iron oxide. The sheath of approximately 50% of microfilariae showed activity for acid phosphatase, 5′ nucleotidase and peroxidase, but not for ATPases, alkaline phosphatase or esterase. No enzymes were detected in the epicuticle although the cortex and basal layers of the cuticle did show enzymic activity. Structures beneath the cuticle in the main body of the worms contained considerable enzymic activity. Microfilariae directly isolated from the blood of infected cats were found by immunochemical means to carry serum proteins on their sheaths but not on their cuticles. These studies extend the definition of the outer structures of microfilariae and confirm that they significantly differ in morphology and enzyme content from typical mammalian cell membranes.

Type
Research Article
Copyright
Copyright © Cambridge University Press 1984

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