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Excretion of host immunoglobulin in tick saliva and detection of IgG-binding proteins in tick haemolymph and salivary glands

Published online by Cambridge University Press:  06 April 2009

H. Wang  and
P. A. Nuttall
H. Wang
Affiliation:
NERC Institute of Virology and Environmental Microbiology, Mansfield Road, Oxford OX1 3SR
P. A. Nuttall
Affiliation:
NERC Institute of Virology and Environmental Microbiology, Mansfield Road, Oxford OX1 3SR
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Summary

Host immunoglobulin G (IgG) crossed the gut wall into the haemocoel of adult Rhipicephalus appendiculatus female ticks when they fed on guinea-pigs. Guinea-pig IgG was also found in saliva of the feeding ticks. The concentration and antibody activity of IgG in haemolymph, salivary gland extract (SGE) and saliva at different stages of tick feeding were detected by enzyme-linked immunoassay. Specific activity of the IgG in tick samples was determined by feeding ticks on guinea-pigs which were immunized with killed Escherichia coli: 35–42% of the antibody activity in guinea-pig immune serum remained in the tick samples. The high relative concentration of IgG in tick saliva at later stages of feeding suggests that the tick may have a mechanism for getting rid of foreign proteins via the salivary gland. Such a mechanism could involve lgG binding proteins (1GBPs) which were found in both haemolymph and SGE of female ticks at day 6 of feeding using a guinea-pig IgG–agarose affinity column. In female ticks, the Mr of 1GBPs in SGE (23 and 57 kDa) were less than those in haemolymph (78 and > 100 kDa). The existence of 1GBPs in both the tick salivary gland and haemolymph indicate that haemolymph and salivary gland cooperate to remove foreign proteins, e.g. host immunoglobulin, from the body during feeding. This mechanism may be a part of the tick self-defence system.

Keywords

Rhipicephalus appendiculatustick salivatick haemolymphimmunoglobulinimmunoglobulin binding protein.
Type
Research Article
Information
Parasitology , Volume 109 , Issue 4 , November 1994 , pp. 525 - 530
Copyright
Copyright © Cambridge University Press 1994

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