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• W2102846935 startingPage "511" @default.
• W2102846935 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." @default.
• W2102846935 created "2016-06-24" @default.
• W2102846935 creator A5016846953 @default.
• W2102846935 creator A5037580313 @default.
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• W2102846935 date "2009-12-01" @default.
• W2102846935 modified "2023-09-27" @default.
• W2102846935 title "Purification and characterization of a novel salivary antimicrobial peptide from the tick, Ixodes scapularis" @default.
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• W2102846935 doi "https://doi.org/10.1016/j.bbrc.2009.09.127" @default.
• W2102846935 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3740409" @default.
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