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1.
Parasit Vectors ; 11(1): 594, 2018 Nov 14.
Article in English | MEDLINE | ID: mdl-30428923

ABSTRACT

Vector-borne diseases constitute 17% of all infectious diseases in the world; among the blood-feeding arthropods, ticks transmit the highest number of pathogens. Understanding the interactions between the tick vector, the mammalian host and the pathogens circulating between them is the basis for the successful development of vaccines against ticks or the tick-transmitted pathogens as well as for the development of specific treatments against tick-borne infections. A lot of effort has been put into transcriptomic and proteomic analyses; however, the protein-carbohydrate interactions and the overall glycobiology of ticks and tick-borne pathogens has not been given the importance or priority deserved. Novel (bio)analytical techniques and their availability have immensely increased the possibilities in glycobiology research and thus novel information in the glycobiology of ticks and tick-borne pathogens is being generated at a faster pace each year. This review brings a comprehensive summary of the knowledge on both the glycosylated proteins and the glycan-binding proteins of the ticks as well as the tick-transmitted pathogens, with emphasis on the interactions allowing the infection of both the ticks and the hosts by various bacteria and tick-borne encephalitis virus.


Subject(s)
Glycomics/methods , Host-Pathogen Interactions/physiology , Ixodes/physiology , Tick-Borne Diseases/physiopathology , Anaplasma/pathogenicity , Animals , Borrelia/pathogenicity , Carbohydrates/physiology , Encephalitis Viruses, Tick-Borne/pathogenicity , Glycosylation , Ixodes/microbiology , Ixodes/virology , Lectins/metabolism , Polysaccharides/metabolism , Proteomics
2.
Carbohydr Res ; 389: 93-9, 2014 May 07.
Article in English | MEDLINE | ID: mdl-24680516

ABSTRACT

The presence of sialylated structures in tick organs was observed previously using lectin staining. Recently, we demonstrated the presence of sialylated N-glycans using mass spectrometry in tick salivary glands and the gut. However, we proposed a host (blood) origin for these glycans and mapped the transport of sialylated molecules from the gut to the salivary glands. In this report, we performed quantitation of whole sialic acid and of metabolically incorporated sialic acid (N-azido neuraminic acid) in Ixodes ricinus tick samples. We show that the majority of sialylated molecules in the adult tick originate in the host (blood) and are not synthesized by the tick. Similar results were observed for tick cell cultures. The almost complete absence of tick sialylated molecules and the specific transport and localization of host structures into the tick salivary glands and the saliva raises many questions on the role of these molecules in the physiology and, specifically, the blood-feeding of ticks.


Subject(s)
Glycoproteins/blood , Glycoproteins/metabolism , Host-Parasite Interactions , Ixodes/metabolism , N-Acetylneuraminic Acid/metabolism , Animals , Cell Line , Female , Ixodes/physiology , Saliva/metabolism
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