Proteomic profiling of Rhipicephalus (Boophilus) microplus midgut responses to infection with Babesia bovis.
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 Ca(2+)-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.
Rachinsky
Anna
A
Knipling-Bushland US Livestock Insects Research Laboratory, U.S. Department of Agriculture-Agricultural Research Service, 2700 Fredericksburg Road, Kerrville, TX 78028, USA. Anna.Rachinsky@ars.usda.gov
Guerrero
Felix D
FD
Scoles
Glen A
GA
D000818:Animals; D001096:Arachnid Vectors / Q000469:parasitology; D016793:Babesia bovis / Q000472:pathogenicity*; D001404:Babesiosis / Q000635:transmission / Q000662:veterinary; D002417:Cattle; D002418:Cattle Diseases / Q000635:transmission; D002851:Chromatography, High Pressure Liquid / Q000662:veterinary; D004587:Electrophoresis, Agar Gel / Q000662:veterinary; D015180:Electrophoresis, Gel, Two-Dimensional / Q000662:veterinary; D005260:Female; D020869:Gene Expression Profiling / Q000662:veterinary; D006790:Host-Parasite Interactions; D007525:Isoelectric Focusing / Q000662:veterinary; D013058:Mass Spectrometry / Q000662:veterinary; D008565:Membrane Proteins / Q000235:genetics / Q000378:metabolism*; D020543:Proteome / Q000235:genetics / Q000378:metabolism*; D048494:Rhipicephalus / Q000378:metabolism* / Q000469:parasitology*; D015854:Up-Regulation
D008565:Membrane Proteins; D020543:Proteome