IrAM-An alpha2-macroglobulin from the hard tick Ixodes ricinus: characterization and function in phagocytosis of a potential pathogen Chryseobacterium indologenes
Language English Country United States Media print-electronic
Document type Journal Article, Research Support, Non-U.S. Gov't
PubMed
18948134
DOI
10.1016/j.dci.2008.09.011
PII: S0145-305X(08)00211-5
Knihovny.cz E-resources
- MeSH
- alpha-Macroglobulins chemistry genetics immunology pharmacology MeSH
- Chryseobacterium immunology MeSH
- Phagocytosis immunology MeSH
- Phenanthrolines pharmacology MeSH
- Hemocytes drug effects immunology microbiology MeSH
- Hemolymph immunology MeSH
- Ixodes genetics immunology microbiology MeSH
- Metalloproteases drug effects metabolism MeSH
- Methylamines pharmacology MeSH
- Molecular Sequence Data MeSH
- RNA Interference MeSH
- Amino Acid Sequence MeSH
- Base Sequence MeSH
- Sequence Alignment MeSH
- Animals MeSH
- Check Tag
- Animals MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- 1,10-phenanthroline MeSH Browser
- alpha-Macroglobulins MeSH
- Phenanthrolines MeSH
- Metalloproteases MeSH
- methylamine MeSH Browser
- Methylamines MeSH
The universal protease inhibitors of the alpha(2)-macroglobulin (alpha(2)M) family are evolutionarily conserved constituents of innate immunity, presumably because they guard organisms against undesired proteolytic attacks of a different origin. Here, we determined the primary structure of alpha(2)-macroglobulin from the hard tick Ixodes ricinus (IrAM) by sequencing of overlapping PCR products. Predicted disulfide and glycosylation patterns, post-translational cleavage and alternative splicing within its 'bait region' demonstrate that IrAM is closely related to the alpha(2)-macroglobulin from the soft tick Ornithodoros moubata. The IrAM message is expressed in all tick developmental stages and tissues, except for the gut, and the protein was detected to be mainly present in the hemolymph. Silencing of IrAM by dsRNA interference markedly reduced the phagocytosis of a potential pathogen, Chryseobacterium indologenes, by tick hemocytes both in vitro and in vivo. In contrast, phagocytosis of the Lyme disease spirochete Borrelia burgdorferi or a commensal bacteria Staphylococcus xylosus was not affected by the IrAM knock-down. Similar results were obtained upon deactivation of all thioester proteins in tick hemolymph by methylamine. We have further demonstrated that phagocytosis of C. indologenes is dependent on an active metalloprotease secreted by the bacteria. These data indicate that interaction of tick alpha(2)-macroglobulin with a protease of an invading pathogen is linked with cellular immune response.
References provided by Crossref.org
Tick Immune System: What Is Known, the Interconnections, the Gaps, and the Challenges
Sialomes and Mialomes: A Systems-Biology View of Tick Tissues and Tick-Host Interactions
Deep Sequencing Analysis of the Ixodes ricinus Haemocytome
Interaction of the tick immune system with transmitted pathogens
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