Proteomic analysis of saliva from partially and fully engorged adult female Rhipicephalus microplus (Acari: Ixodidae).

ABSTRACT

Rhipicephalus microplus salivary gland secretes a number of complex bioactive proteins during feeding. These components are important in feeding and affect anti-coagulation, anti-inflammation and also have anti-microbial effects. In this study, tick saliva was collected from partially engorged female (PEF) and fully engorged female (FEF) ticks. Liquid chromatography tandem-mass spectrometry (LC-MS/MS) and isobaric tags for relative and absolute quantification (iTRAQ) were used to identify and quantify R. microplus salivary proteins. A total of 322 unique peptides were detected and 151 proteins were characterized in both PEF and FEF. Of these, 41 proteins are considered as high-confidence proteins. Fifteen high-confidence proteins were upregulated and six high-confidence proteins were downregulated (p < 0.05; PEFFEF ratio ≥ 1.2 or PEFFEF ratio ≤ 0.83); 17 high-confidence proteins are slightly changed (PEFFEF ratio > 0.83 and < 1.2). These high-confidence proteins are involved in several physiological roles, including egg development, transportation of proteins, immunity and anti-microorganism, anti-coagulant, and adhesion. In comparison with PEF, the number of upregulated proteins exceeded the number of proteins downregulated. Salivary protein may be induced by the blood-meal and these proteins contribute to successful feeding.