| Longistatin, a plasminogen activator, is key to the availability of blood-meals for ixodid ticks. | |
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MedLine Citation:
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PMID: 21423674 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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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. |
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Authors:
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Anisuzzaman; M Khyrul Islam; M Abdul Alim; Takeharu Miyoshi; Takeshi Hatta; Kayoko Yamaji; Yasunobu Matsumoto; Kozo Fujisaki; Naotoshi Tsuji |
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Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't Date: 2011-03-10 |
Journal Detail:
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Title: PLoS pathogens Volume: 7 ISSN: 1553-7374 ISO Abbreviation: PLoS Pathog. Publication Date: 2011 Mar |
Date Detail:
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Created Date: 2011-03-22 Completed Date: 2011-07-11 Revised Date: 2011-07-27 |
Medline Journal Info:
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Nlm Unique ID: 101238921 Medline TA: PLoS Pathog Country: United States |
Other Details:
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Languages: eng Pagination: e1001312 Citation Subset: IM |
Affiliation:
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Department of Global Agricultural Sciences, Graduate School of Agricultural and Life Sciences, The University of Tokyo, Tokyo, Japan. |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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Animals Anticoagulants / metabolism Blood* Calcium-Binding Proteins / physiology* Feeding Behavior / physiology* Fibrin / metabolism Fibrinogen / metabolism Fibrinolysin / metabolism Host-Parasite Interactions / physiology* Ixodidae / physiology* Plasminogen Activators / physiology* Protozoan Proteins / physiology* RNA, Double-Stranded / genetics RNA, Messenger / metabolism Reverse Transcriptase Polymerase Chain Reaction Salivary Proteins and Peptides / physiology* |
| Chemical | |
Reg. No./Substance:
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0/Anticoagulants; 0/Calcium-Binding Proteins; 0/Protozoan Proteins; 0/RNA, Double-Stranded; 0/RNA, Messenger; 0/Salivary Proteins and Peptides; 0/longistatin protein, Haemaphysalis longicornis; 9001-31-4/Fibrin; 9001-32-5/Fibrinogen; EC 3.4.21.-/Plasminogen Activators; EC 3.4.21.7/Fibrinolysin |
| Comments/Corrections | |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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