A borreliacidal factor in Amblyomma americanum saliva is associated with phospholipase A2 activity
Autor: | Marc C. Dolan, Donald E. Champagne, Nordin S. Zeidner, Joseph Piesman, Amy J. Ullmann, Cherilyn Sackal, Gabrielle Dietrich |
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Rok vydání: | 2009 |
Předmět: |
Saliva
Ixodidae Phospholipase A2 Inhibitors Phosphorylcholine Trypsin inhibitor Immunology Microbiology Amblyomma americanum fluids and secretions stomatognathic system medicine Animals Electrophoresis Gel Two-Dimensional Trypsin Enzyme Inhibitors Borrelia burgdorferi Phospholipase A Ixodes biology General Medicine biology.organism_classification Specific Pathogen-Free Organisms Phospholipases A2 stomatognathic diseases Infectious Diseases Ixodes scapularis Chromatography Gel Electrophoresis Polyacrylamide Gel Parasitology medicine.drug |
Zdroj: | Experimental Parasitology. 121:370-375 |
ISSN: | 0014-4894 |
DOI: | 10.1016/j.exppara.2009.01.002 |
Popis: | Previous work in our laboratory described the in vitro killing of Borrelia burgdorferi when co-cultured with saliva from adult Amblyomma americanum. Borreliacidal activity was not evident using Ixodes scapularis saliva. Mixing trypsin with saliva eliminated the borreliacidal activity of A. americanum saliva, while incorporating a trypsin inhibitor restored all borreliacidal activity, indicating this factor was of protein or peptide origin. One-dimensional PAGE indicated at least 7 major protein differences between I. scapularis and A. americanum saliva. To determine the borreliacidal factor, A. americanum saliva was fractionated by gel filtration and subsequent killing of B. burgdorferi was associated with a single fraction. Two-dimensional gel analysis indicated protein and/or peptide(s) in borreliacidal fractions running between 38 and 64 kDa. Finally, admixing saliva with the phospholipase A2 inhibitor oleyloxyethyl phosphorylcholine completely eliminated the ability of A. americanum saliva to kill B. burgdorferi. These studies indicate the borreliacidal activity found in A. americanum saliva is likely due to phospholipase A2 enzymatic activity. |
Databáze: | OpenAIRE |
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