Academic Journal
Longistatin, a plasminogen activator, is key to the availability of blood-meals for ixodid ticks.
| العنوان: | Longistatin, a plasminogen activator, is key to the availability of blood-meals for ixodid ticks. |
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| المؤلفون: | Anisuzzaman, M Khyrul Islam, M Abdul Alim, Takeharu Miyoshi, Takeshi Hatta, Kayoko Yamaji, Yasunobu Matsumoto, Kozo Fujisaki, Naotoshi Tsuji |
| المصدر: | PLoS Pathogens, Vol 7, Iss 3, p e1001312 (2011) |
| بيانات النشر: | Public Library of Science (PLoS) |
| سنة النشر: | 2011 |
| المجموعة: | Directory of Open Access Journals: DOAJ Articles |
| مصطلحات موضوعية: | Immunologic diseases. Allergy, RC581-607, Biology (General), QH301-705.5 |
| الوصف: | Ixodid ticks are notorious blood-sucking ectoparasites and are completely dependent on blood-meals from hosts. In addition to the direct severe effects on health and productivity, ixodid ticks transmit various deadly diseases to humans and animals. Unlike rapidly feeding vessel-feeder hematophagous insects, the hard ticks feed on hosts for a long time (5-10 days or more), making a large blood pool beneath the skin. Tick's salivary glands produce a vast array of bio-molecules that modulate their complex and persistent feeding processes. However, the specific molecule that functions in the development and maintenance of a blood pool is yet to be identified. Recently, we have reported on longistatin, a 17.8-kDa protein with two functional EF-hand Ca(++)-binding domains, from the salivary glands of the disease vector, Haemaphysalis longicornis, that has been shown to be linked to blood-feeding processes. Here, we show that longistatin plays vital roles in the formation of a blood pool and in the acquisition of blood-meals. Data clearly revealed that post-transcriptional silencing of the longistatin-specific gene disrupted ticks' unique ability to create a blood pool, and they consequently failed to feed and replete on blood-meals from hosts. Longistatin completely hydrolyzed α, β and γ chains of fibrinogen and delayed fibrin clot formation. Longistatin was able to bind with fibrin meshwork, and activated fibrin clot-bound plasminogen into its active form plasmin, as comparable to that of tissue-type plasminogen activator (t-PA), and induced lysis of fibrin clot and platelet-rich thrombi. Plasminogen activation potentiality of longistatin was increased up to 4 times by soluble fibrin. Taken together, our results suggest that longistatin may exert potent functions both as a plasminogen activator and as an anticoagulant in the complex scenario of blood pool formation; the latter is critical to the feeding success and survival of ixodid ticks. |
| نوع الوثيقة: | article in journal/newspaper |
| اللغة: | English |
| تدمد: | 1553-7366 1553-7374 |
| Relation: | http://europepmc.org/articles/PMC3053353?pdf=render; https://doaj.org/toc/1553-7366; https://doaj.org/toc/1553-7374; https://doaj.org/article/68c968e36830417bbddd086e5db4d0b0 |
| DOI: | 10.1371/journal.ppat.1001312 |
| الاتاحة: | https://doi.org/10.1371/journal.ppat.1001312 https://doaj.org/article/68c968e36830417bbddd086e5db4d0b0 |
| رقم الانضمام: | edsbas.13FC4857 |
| قاعدة البيانات: | BASE |
Full Text Finder | تدمد: | 15537366 15537374 |
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| DOI: | 10.1371/journal.ppat.1001312 |