IrAM-An alpha2-macroglobulin from the hard tick Ixodes ricinus: characterization and function in phagocytosis of a potential pathogen Chryseobacterium indologenes
Jazyk angličtina Země Spojené státy americké Médium print-electronic
Typ dokumentu časopisecké články, práce podpořená grantem
PubMed
18948134
DOI
10.1016/j.dci.2008.09.011
PII: S0145-305X(08)00211-5
Knihovny.cz E-zdroje
- MeSH
- alfa-makroglobuliny chemie genetika imunologie farmakologie MeSH
- Chryseobacterium imunologie MeSH
- fagocytóza imunologie MeSH
- fenantroliny farmakologie MeSH
- hemocyty účinky léků imunologie mikrobiologie MeSH
- hemolymfa imunologie MeSH
- klíště genetika imunologie mikrobiologie MeSH
- metaloproteasy účinky léků metabolismus MeSH
- methylaminy farmakologie MeSH
- molekulární sekvence - údaje MeSH
- RNA interference MeSH
- sekvence aminokyselin MeSH
- sekvence nukleotidů MeSH
- sekvenční seřazení MeSH
- zvířata MeSH
- Check Tag
- zvířata MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
- Názvy látek
- 1,10-phenanthroline MeSH Prohlížeč
- alfa-makroglobuliny MeSH
- fenantroliny MeSH
- metaloproteasy MeSH
- methylamine MeSH Prohlížeč
- methylaminy 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.
Citace poskytuje 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
GENBANK
EU835901