Characterisation of Sarcoptes scabiei antigens.
In pig herds, the status of Sarcoptes scabiei infections is routinely monitored by serodiagnosis. Crude antigen for ELISA is usually prepared from S. scabiei var. canis or other variations and may lead to variations in the outcome of different tests, making assay standardisation difficult. This study was performed to investigate the antigen profiles of S. scabiei, including differences between hydrophilic and more hydrophobic protein fractions, by Western blotting with sera from pigs with defined infection status. Potential cross-reactivity among S. scabiei (var. canis, suis and bovis), Dermatophagoides farinae and Tyrophagus putrescentiae was also analysed. Hydrophobic S. scabiei antigens were detectable in the range of 40-50 kDa, whilst the hydrophilic fraction showed no specific antigenicity. In the hydrophobic fractions of D. farinae and T. putrescentiae, two major protein fractions in a similar size range could be identified, but no cross-reactivity with Sarcoptes-positive sera was detectable. However, examination of the hydrophilic fractions revealed cross-reactivity between Sarcoptes-positive sera and both the house dust mite and the storage mite in the range of 115 and 28/38 kDa. Specific bands in the same range (42 and 48 kDa) could be detected in blots from hydrophobic fractions of all three tested variations of S. scabiei (var. canis, bovis and suis). These results show that there are considerable differences in mange antibody reactivity, including reactions with proteins from free-living mites, which may interfere with tests based on hydrophilic antigens. Further refinement of antigen and the use of specific hydrophobic proteins could improve ELISA performance and standardisation.
Hejduk
Gloria
G
Institute of Parasitology, Department of Pathobiology, University of Veterinary Medicine Vienna, Veterinaerplatz 1, 1210, Vienna, Austria.
Hofstätter
Katja
K
Löwenstein
Michael
M
Peschke
Roman
R
Miller
Ingrid
I
Joachim
Anja
A
D000818:Animals; D039741:Antigens, Dermatophagoides / Q000737:chemistry / Q000276:immunology; D000953:Antigens, Protozoan / Q000737:chemistry / Q000276:immunology*; D015153:Blotting, Western; D002417:Cattle; D003429:Cross Reactions; D004285:Dogs; D015180:Electrophoresis, Gel, Two-Dimensional; D057927:Hydrophobic and Hydrophilic Interactions; D019476:Insect Proteins / Q000737:chemistry / Q000276:immunology*; D007525:Isoelectric Focusing; D010273:Parasitic Diseases, Animal / Q000469:parasitology*; D039981:Pyroglyphidae / Q000276:immunology / Q000378:metabolism; D012520:Sarcoptes scabiei / Q000276:immunology* / Q000378:metabolism; D012532:Scabies / Q000097:blood / Q000662:veterinary*; D013045:Species Specificity; D013552:Swine
D039741:Antigens, Dermatophagoides; D000953:Antigens, Protozoan; D019476:Insect Proteins