Search results for: Rabbit Anti-Streptococcus Group A Antibodies
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Heart-reactive antibodies in rabbit anti-Streptococcus mutans sera fail to cross-react with Streptococcus mutans.
Immunization of rabbits with Streptococcus mutans antigens results in the production of serum antibodies that bind in vitro to human, rabbit, and monkey cardiac muscle. Antibodies to heart, however, have also been reported to occur at lower titers in the sera of unimmunized rabbits. In this study, the specificities of heart-reactive antibodies (HRA) in sera of unimmunized and S. mutans-immunized rabbits were compared using indirect immunofluorescence, Western blot, and Bio-Dot immunoassays. Both groups of sera gave striational indirect immunofluorescence-staining patterns on thin sections of native human and monkey cardiac muscle. Western blot analyses revealed that antibodies in normal sera bound 9 to 20 components of human, rabbit, and monkey heart. The major bands had Mr of 205,000, 160,000, 135,000, and 70,000. Several of the normal sera did not have antibody activity to S. mutans antigens, indicating that these HRA do not cross-react with these bacteria. Although immunization of rabbits with S. mutans caused increased titers of HRA (two to three doubling dilutions), Western blot assays using anti-S. mutans sera showed banding patterns qualitatively similar to those of normal sera on heart extracts. Antibodies to skeletal muscle myosin were detected in both serum groups. Of eighteen normal rabbit sera sixteen had antimyosin titers of 10 to 40, whereas all eighteen anti-S. mutans sera had titers of 10 to 160. Affinity-purified antimyosin antibodies isolated from anti-S. mutans serum did not bind to S. mutans components. Conversely, affinity-purified antibodies to S. mutans antigens did not bind to myosin or to other cardiac muscle components. Among these were antibodies to the 185-kDa cell wall protein (also known as B, I/II, IF, Spa A, and P1) previously believed to possess antigenic mimicry. HRA were removed from anti-S. mutans sera by absorption with S. mutans but this effect was not specific, because a non-cross-reactive internal standard antibody was also absorbed to the same extent. Because previous evidence for antigenic mimicry between S. mutans and cardiac muscle was based on serum cross-absorption experiments, this immunologic relationship is not substantiated. These results indicated that naturally occurring antibodies to cardiac muscle components are present in the sera of unimmunized rabbits and that immunization with S. mutans does not stimulate production of new heart-reactive antibody, but rather serves to boost antibody production by preexisting clones of self-reactive B-lymphocytes.F J Swartzwelder, P K Barua, B Albini, M W Stinson
2483 related Products with: Heart-reactive antibodies in rabbit anti-Streptococcus mutans sera fail to cross-react with Streptococcus mutans.
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Phosphoenolpyruvate-sugar phosphotransferase transport system of Streptococcus mutans: purification of HPr and enzyme I and determination of their intracellular concentrations by rocket immunoelectrophoresis.
Enzyme I and HPr, the general proteins of the phosphoenolpyruvate-sugar phosphotransferase system, play a pivotal role in the control of sugar utilization in gram-negative and gram-positive bacteria. To determine whether growth conditions could modify the rate of biosynthesis of these proteins in Streptococcus mutans, we first purified to homogeneity enzyme I and HPr from S. mutans ATCC 27352. Using specific antibodies obtained against these proteins, we determined by rocket electrophoresis the intracellular levels of enzyme I and HPr in cells of S. mutans 27352 grown under various batch culture conditions and in a number of glucose-grown cells of other strains of S. mutans. HPr was purified by the procedure reported by Gauthier et al. (L. Gauthier, D. Mayrand, and C. Vadeboncoeur, J. Bacteriol. 160:755-763, 1984) and displayed a single band with a molecular weight of 6,650 when analyzed by sodium dodecyl sulfate-urea gel electrophoresis. Enzyme I was purified by DEAE-cellulose chromatography, affinity chromatography on an anti-Streptococcus salivarius column, and preparative electrophoresis. The protein migrated as a single band in native and denaturating gel electrophoresis. The subunit molecular weight of enzyme I determined by electrophoresis under denaturating conditions was 68,000. In gel filtration chromatography at 4 degrees C, the enzyme migrated as a 135,000- to 160,000-molecular-weight species, suggesting that enzyme I is a dimer. In double immunodiffusion experiments, antibodies against HPr reacted with several oral streptococci, Streptococcus lactis, Streptococcus faecium, and Lactobacillus casei, but not with Bacillus subtilis, Staphylococcus aureus, and Escherichia coli. Antibodies against enzyme I of S. mutans 27352 cross-reacted with enzyme I from all the other oral streptococci tested. No cross-reaction was observed with other gram-positive and gram-negative bacteria. The levels of enzyme I and HPr determined by rocket electrophoresis in S. mutans 27352 varied at the most by twofold, depending on the growth conditions. Glucose-grown cells of other S. mutans strains contained levels of enzyme I and HPr which were similar to those found in S. mutans 27352.L Thibault, C Vadeboncoeur
1650 related Products with: Phosphoenolpyruvate-sugar phosphotransferase transport system of Streptococcus mutans: purification of HPr and enzyme I and determination of their intracellular concentrations by rocket immunoelectrophoresis.
5 G1000 tests5x96 well plate200ug100ug Lyophilized1 mg100 mg25 mg100ug Lyophilized10 mg
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Chemical and immunochemical studies on lipopolysaccharides from pyocin 103-sensitive and -resistant Neisseria gonorrhoeae.
The chemical and immunochemical properties of lipopolysaccharides (LPS) isolated from pyocin 103-sensitive and -resistant Neisseria gonorrheae were investigated. Marked differences were found in immunochemical behavior of LPS from pyocin-sensitive gonococcal strain JW31 and its isogenic pyocin-resistant variant JW31R. JW31 LPS readily precipitated wheat-germ agglutinin, soybean lectin, and rabbit anti-Streptococcus faecalis or horse anti-type 14 pneumococcal antibody. In contrast, JW31R LPS precipitated only soybean lectin. The combining-site specificity of anti-S. faecalis cross-precipitated by JW31 LPS, or type 14 pneumococcal capsular polysaccharide, was examined by hapten inhibition, and lactose found to be the most potent inhibitor. Horse anti-pneumococcal type 14 antibodies, cross-precipitated by JW31 LPS and streptococcal lactose polymer, exhibited heterogeneity with respect to combining site specificity. Gel filtration of LPS-derived core oligosaccharide showed both strain JW31 and JW31 R to possess R-type lipopolysaccharide with cores having a Mr approximately 1800. JW31R LPS contains more galactose but less hexosamine than JW31 LPS. Both JW31 and JW31R core oligosaccharides possess D-glucosamine and D-galactosamine, probably N-acetylated, as the only nonreducing end-groups, and (1 leads to 4)-linked D-glucose residues. Chemical data support immunochemical findings which indicate that lactose units occur as a structural feature of JW31 gonococcal LPS.M C Connelly, P Z Allen
1939 related Products with: Chemical and immunochemical studies on lipopolysaccharides from pyocin 103-sensitive and -resistant Neisseria gonorrhoeae.
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Reactivity of antistreptococcus hyperimmune sera with human myocardial tissue.
Antimyocardial antibodies were determined in hyperimmune rabbit sera against group A streptococci. The detection method was indirect immunofluorescence in human myocardial tissue sections. Positively reacting sera were absorbed with group A streptococcus cell walls and cytoplasmic membranes, the objective being to locate the cross-reacting antigen in the streptococcus cell under the given experimental conditions. Cell walls gave the better absorption results. Whether or not the streptococci possessed the Fc-reacting factor was without influence on the absorption result.R Bícová, J Stefan