Journal
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
Volume 305, Issue 4, Pages 869-875Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/S0006-291X(03)00857-X
Keywords
Ixodes seapularis; Borrelia burgdorferi; tick; hematophagy; collagen; fibrinogen; fibrino(gen)olytic; ADAM; reprolysin; blood-sucking
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Funding
- Intramural NIH HHS [Z01 AI000810-11, Z99 AI999999] Funding Source: Medline
- NIAID NIH HHS [R01 AI 37230, R01 AI037230] Funding Source: Medline
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The full-length sequence of tick salivary gland cDNA coding for a protein similar to metalloproteases (NIP) of the reprolysin family is reported. The Ixodes scapularis NIP is a 488 amino acid (aa) protein containing pre- and pro-enzyme domains, the zinc-binding motif HExxHxxGxxH common to metalloproteases, and a cysteine-rich region. In addition, the predicted amino-terminal sequences of I. scapularis MPs were found by Edman degradation of PVDF-transferred SDS/PAGE-separated tick saliva proteins, indicating that these putative enzymes are secreted. Furthermore, saliva has a metal-dependent proteolytic activity towards gelatin, fibrin(ogen). and fibronectin, but not collagen or laminin. Accordingly, L scapularis saliva has a rather specific metalloprotease similar to the hemorrhagic proteases of snake venoms. This is the first description of such activity in tick saliva and its role in tick feeding and Borrelia transmission is discussed. (C) 2003 Elsevier Science (USA). All rights reserved.
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