Isolation and characterization of a neutrophil chemotactic factor from Tritrichomonas foetus organisms.
A neutrophil chemotactic factor (TfNCF) was isolated from the crude extract of Tritrichomonas foetus organisms by a combination of anion-exchange chromatography on DE52 and gel filtration on Sephacryl S200. TfNCF showed homogenicity by both PAGE and SDS-PAGE. The molecular weight of TfNCF was estimated to be 22 and 24 kDa, by Sephacryl S200 gel chromatography and by SDS-PAGE under reducing conditions. Immunization of TfNCF caused almost complete protection against T. foetus infection in mice. Western blot analysis probed with anti-TfNCF antibody showed that the epitopes on TfNCF were not commonly shared on the other components of T. foetus organisms nor other helminthous parasite-derived components. Furthermore, pre-incubation of neutrophils with antigens of other helminthous parasites or N-formylmethionyl-leucyl-phenylalanine did not affect the neutrophil chemotactic activity for TfNCF. These results suggest that TfNCF is a novel NCF consisting of unique epitopes for both antigenicity and neutrophil chemotactic activity. The role of NCF in the initiation of the immune response is discussed.
Owhashi
M
M
Faculty of Integrated Arts and Sciences, University of Tokushima, Japan.
Tomiyoshi
F
F
Hayashi
H
H
D000818:Animals; D015153:Blotting, Western; D002850:Chromatography, Gel; D002852:Chromatography, Ion Exchange; D004591:Electrophoresis, Polyacrylamide Gel; D005260:Female; D016209:Interleukin-8 / Q000032:analysis* / Q000302:isolation & purification / Q000502:physiology; D051379:Mice; D008815:Mice, Inbred Strains; D009240:N-Formylmethionine Leucyl-Phenylalanine / Q000494:pharmacology; D010533:Peritoneal Lavage; D015800:Protozoan Proteins / Q000032:analysis* / Q000302:isolation & purification; D016835:Tritrichomonas foetus / Q000737:chemistry*
D016209:Interleukin-8; D015800:Protozoan Proteins; D009240:N-Formylmethionine Leucyl-Phenylalanine