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Comparison of the Surface Proteins and Glycoproteins On Erythrocytes of Calves Before and During Infection With Babesia Bovis
Author(s) -
HOWARD RUSSELL J.,
RODWELL BARRY J.,
SMITH PATRICIA M.,
CALLOW L. L.,
MITCHELL GRAHAM F.
Publication year - 1980
Publication title -
the journal of protozoology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.067
H-Index - 77
eISSN - 1550-7408
pISSN - 0022-3921
DOI - 10.1111/j.1550-7408.1980.tb04690.x
Subject(s) - glycoprotein , galactose oxidase , babesia bovis , gel electrophoresis , biology , sodium dodecyl sulfate , microbiology and biotechnology , membrane protein , biochemistry , membrane glycoproteins , polyacrylamide gel electrophoresis , lactoperoxidase , blood proteins , red blood cell , proteinase k , chemistry , membrane , virology , babesia , enzyme , peroxidase
The surface proteins and glycoproteins on red cells from normal and Babesia bovis ‐infected calf blood have been compared. Several radiolabeling probes were used to label specifically external membrane molecules which were then separated by sodium dodecyl sulfate‐polyacrylamide gel electrophoresis and identified by autoradiography or fluorography. No differences were observed among the Coomassie Blue‐stained membrane proteins of erythrocytes from individual uninfected calves. Comparison of red cells from these animals also indicated no qualitative differences in the surface proteins with accessible tyrosyl residues labeled by lactoperoxidase‐catalyzed radioiodnation, although some quantitative variation in the uptake of radioactivity into particular proteins was observed. the major radioiodinated bands on normal bovine erythrocytes had Mr of 165, 130, 90, and 45 kiloDaltons. However, labeling of surface glycoproteins by the periodate/[ 3 H]NaBH 4 and galactose oxidase (± neuraminidase)/[ 3 H]NaBH 4 methods showed significant differences in the surface proteins of red cells from individual uninfected calves. of 14 animals tested, 5 had major labeled glycoproteins of unique Mr. No changes were observed in radioiodinated surface proteins of total red cell samples from infected calves with 0.5‐6% parasitemia. Radioiodination of concentrated infected red cells from the same samples (concentrated by selective hypotonic lysis of uninfected erythrocytes in KC1) resulted in the labeling of 3 new surface proteins, with Mr of 118, 115, and 60 kiloDaltons. the same new 125 I‐labeled bands were identified on infected cells from 3 avirulent strains of B. bovis used in vaccine production. Furthermore, in concentrated infected cells there was very poor radiolabeling of major bands strongly labeled on uninfected cells (Mr 165, 130, and 90 kiloDaltons), suggesting parasite‐induced loss of these proteins. Although there were some differences in 3 H‐labeled surface glycoproteins of red cells from normal and. B. bovis ‐infected blood, they were restricted to minor labeled bands and were not seen consistently. the labeled surface glycoproteins of concentrated infected cells were very similar to those of the uninfected red blood cells from infected blood.