Document Type
Article
Date of Original Version
2009
Department
Plant Sciences and Entomology
Abstract
A novel antimicrobial peptide was isolated from the saliva of the Lyme disease tick vector, Ixodes scapularis, henceforth designated as ISAMP (I. scapularis Antimicrobial Peptide). ISAMP was purified using a sequential method including ultra filtration, gel filtration and reverse-phase high performance liquid chromatography. The purified peak had a molecular weight of 5.3 kDa by MALDI/TOF-MS and its amino acid sequence, determined by Edman degradation was PDxGxPxxVKAGRxPxxSI. A BLASTP search revealed that the protein is a putative 5.3 kDa secreted protein (AAM93656) from I. scapularis. The predicted protein is composed of 69 amino acids with no conserved domain motifs. Purified ISAMP was found to have antimicrobial activities against bacteria. Gene expression studies were carried out to observe ISAMP expression in different tick tissues. RT-PCR results indicated that the gene was expressed in hemocytes, fat body and salivary gland but virtually no expression was observed in the midgut. ISAMP is only similar to other Ixodid tick proteins, thus it is a member of a unique family.
Citation/Publisher Attribution
Pichu, S., Ribeiro, J. M.C., & Mather, T. N. (2009). Purification and characterization of a novel salivary antimicrobial peptide from the tick, Ixodes scapularis. Biochemical and Biophysical Research Communications, 390(3), 511-515. doi: 10.1016/j.bbrc.2009.09.127
Available at: https://doi.org/10.1016/j.bbrc.2009.09.127
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