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Title: Proteomic profiling of Rhipicephalus (Boophilus) microplus midgut responses to infection with Babesia bovis

Author
item Rachinsky, Anna
item Guerrero, Felicito
item Scoles, Glen

Submitted to: Veterinary Parasitology
Publication Type: Peer Reviewed Journal
Publication Acceptance Date: 12/18/2007
Publication Date: 4/15/2008
Citation: Rachinsky, A.S., Guerrero, F., Scoles, G.A. 2008. Proteomic profiling of Rhipicephalus (Boophilus) microplus midgut responses to infection with Babesia bovis. Veterinary Parasitology. 152(3-4):294-313.

Interpretive Summary: The current study describes an extensive survey of proteins that are regulated in response to infection of the southern cattle tick, Rhipicephalus (Boophilus) microplus, with the cattle fever causing protozoan parasite Babesia bovis. This study is part of an ongoing effort to establish a proteome database that can be utilized to identify specific proteins that may be involved in successful pathogen transmission. Tick midgut proteins were extracted from control ticks and B. bovis-infected ticks and separated by gel electrophoresis. A selection of proteins that appeared to be expressed at distinctly higher or lower levels in ticks infected with B. bovis were subjected to analysis by mass spectrometry. Among the identified Babesia-affected tick midgut proteins were several proteins that are implicated in signaling processes, five metabolic enzymes, a molecular chaperone, a cytoskeletal protein and a multifunctional protein of the prohibitin family. Identification of these proteins may provide new insights into the molecular interactions between B. bovis and its tick vector, and could lead to identification of anti-tick and transmission blocking vaccine candidates.

Technical Abstract: Differences in protein expression in midgut tissue of uninfected and Babesia bovis-infected southern cattle ticks, Rhipicephalus (Boophilus) microplus, were investigated in an effort to establish a proteome database containing proteins involved in successful pathogen transmission. The electrophoretic separation of midgut membrane proteins was greatly improved by using liquid phase isoelectric focusing combined with one-dimensional or two-dimensional (2-D) gel electrophoresis. A selection of differentially expressed proteins were subjected to analysis by capillary-HPLC-electrospray tandem mass spectrometry (HPLC-ESI-MS/MS). Among the identified Babesia-affected tick midgut proteins were six proteins that are implicated in signaling processes, including three Ca2+-binding proteins, a guanine nucleotide-binding protein, a protein with signal peptide activity and a translocon-associated receptor protein. Up-regulation of five metabolic enzymes indicated parasite-induced changes in electron and proton transport, protein processing and retinoic acid metabolism. Among the down-regulated proteins were a molecular chaperone, a cytoskeletal protein and a multifunctional protein of the prohibitin family. Identification of these proteins may provide new insights into the molecular interactions between B. bovis and its tick vector, and could lead to identification of anti-tick and transmission blocking vaccine candidates.