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6 - Tick lectins and fibrinogen-related proteins
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- By L. Grubhoffer, Biology Centre of the Academy of Sciences of the Czech Republic Institute of Parasitology Branisovska 31 370 05 Ceske Budejovice Czech Republic, R. O. M. Rego, Laboratory of Zoonotic Pathogens Rocky Mountain Laboratories NIAID NIH 903 South 4th Street Hamilton MT 59840 USA, O. Hajdušek, Faculty of Biological Sciences University of South Bohemia Branisovska 31 370 05 Ceske Budejovice Czech Republic, V. Hypša, Faculty of Biological Sciences University of South Bohemia Branisovska 31 370 05 Ceske Budejovice Czech Republic, V. Kovář, Biology Centre of the Academy of Sciences of the Czech Republic Institute of Parasitology Branisovska 31 370 05 Ceske Budejovice Czech Republic, N. Rudenko, Biology Centre of the Academy of Sciences of the Czech Republic Institute of Parasitology Branisovska 31 370 05 Ceske Budejovice Czech Republic, J. H. Oliver, Georgia Southern University Institute of Arthropodology and Parasitology P.O. Box 8056 Statesboro GA 30460 USA
- Edited by Alan S. Bowman, University of Aberdeen, Patricia A. Nuttall
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- Book:
- Ticks
- Published online:
- 21 August 2009
- Print publication:
- 04 December 2008, pp 127-142
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- Chapter
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Summary
INTRODUCTION
Tissue-specific lectin/haemagglutinin activities have been investigated for both soft and hard ticks, although there are comparatively few papers published. Some tick lectins are proteins with binding affinity for sialic acid, various derivatives of hexosamines and different glycoconjugates. Most tick lectin/haemagglutinin activities are blood-meal enhanced, and could serve as molecular factors of self/non-self recognition in defence reactions against bacteria or fungi, as well as in pathogen/parasite transmission. Dorin M, the plasma lectin of Ornithodoros moubata, is the first tick lectin to be purified from tick haemolymph, and the first that has been fully characterized. Partial characterization of other tick lectins/haemagglutinins has been performed mainly with respect to their carbohydrate-binding specificities and immunochemical features. The main goal of this review is to provide an overview of our knowledge of lectins as tissue specific carbohydrate-binding proteins of ticks with emphasis on their structural properties and functional roles either in defence reactions or pathogen transmission. Other lectin reviews have been published dealing with tissue-specific lectins in blood-sucking arthropods (e.g. Ingram & Molyneux, 1991; Grubhoffer, Hypša & Volf, 1997; Grubhoffer & Jindrák, 1998). In addition, several publications have drawn attention to plant and animal lectins, and to lectins as tools in modern glycobiological research (e.g. Jacobson & Doyle, 1996; Rhodes & Milton, 1998).
Research on lectins began in 1888 with publication of the doctoral thesis of Herman Stilmark at the University of Dorpat, Estonia, on the agglutinins of the seeds of castor bean Ricinus communis (Sharon & Lis, 1988).
Tick lectins: structural and functional properties
- L. GRUBHOFFER, V. KOVÁŘ, N. RUDENKO
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- Journal:
- Parasitology / Volume 129 / Issue S1 / October 2004
- Published online by Cambridge University Press:
- 19 April 2005, pp. S113-S125
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- Article
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Few papers have been published on tick lectins so far, and therefore more data are needed to complete the mosaic of knowledge of their structural and functional properties. Tissue-specific lectin/haemagglutinin activities of both soft and hard ticks have been investigated. Some tick lectins are proteins with binding affinity for sialic acid, various derivatives of hexosamines and different glycoconjugates. Most tick lectin/haemagglutinin activities are blood meal enhanced, and could serve as molecular factors of self/non-self recognition in defence reactions against bacteria or fungi, as well as in pathogen/parasite transmission. Dorin M, the plasma lectin of Ornithodoros moubata, is the first tick lectin purified so far from tick haemolymph, and the first that has been fully characterized. Partial characterization of other tick lectins/haemagglutinins has been performed mainly with respect to their carbohydrate binding specificities and immunochemical features.