Search PubMedSearch

SEARCH · Search PubMed

Results for “Cross Reactions”

Search indexed PubMed citations on genomics, clinical trials, systematic reviews and public health. Explore titles, authors and supplied subject terms, then open the PubMed record.

Quote a phrase for an exact phrase match. Source license links do not imply unrestricted reuse.

At least 37 records · Page 2Linked to original sources

Cross-reactions between 2, 4-dinitrophenyl and menadione (vitamin K3) and the general problem of antibody specificity.

Early and late antisera to 2, 4-dinitrophenyl (DNP) and to menadione (K3)4 were compared for reactivity with diverse DNP and K3 ligands. Late antisera were generally more reactive (higher affinity) than early antibodies. Nevertheless, the early antibodies had higher affinity for homologous ligands than late antibodies had for heterologous ligands; the exception, a small (ca. 5%) and possibly heteroclitic subset from late anti-DNP sera, had higher affinity for K3-butyrate than for DNP-lysine. Early antisera appeared to be more specific than late antisera by one criterion (the precipitin reaction), but less specific by a more fundamental criterion (KO/KX, the ratio of intrinsic affinities for homologous and cross-reacting ligands). By several methods (precipitation, binding to heterologous immunoadsorbants) 25 to 75% of the antibodies in both anti-DNP and anti-K3 sera were cross-reactive; even more cross-reactivity was evident by equilibrium dialysis, where it appeared that virtually all anti-DNP antibodies can bind K3 and that virtually all anti-K3 can bind DNP. This extreme level of cross-reaction is not as "strange" as was once thought, it seems unwarranted to regard this cross-reaction as support for the view that antibodies in general are multispecific.

Animals

Bovine reaginic antibody III. Cross-reaction of antihuman IgE and antibovine reaginic immunoglobulin antisera with sera from several species of mammals.

Using antisera specific for the heavy chain of human IgE and bovine reaginic immunoglobulin, the degree of cross-reaction amongst sera from pig, rat, rabbit, guinea pig, goat, cow, horse, dog, cat and human was tested. Antihuman IgE antiserum gave strong reactions with pig, rabbit, cow, goat and human sera (100% to 15.1%) and weak reactions with rat, guinea pig, horse, dog and cat sera (10.1% to 3.22%). Antibovine reagin antiserum produced a considerable amount of cross-reaction with sera from pig, rat, rabbit, goat, horse and human (43.6% to 20.1%) with limited reactions with guinea pig, dog and cat sera (13.9% to 9.3%).

Animals

Occurrence of cross reactions to foot-and-mouth disease virus in normal swine sera.

Sera from 101 swine never exposed to foot-and-mouth disease virus were tested by the plaque-reduction neutralization (PRN) and radial immunodiffusion techniques for cross-reactions to 5 types of foot-and-mouth disease viruses. Depending on the group of sera and the virus used, the percentage of sera cross-reacting at low levels varied from 0 to 50% with the PRN technique and 0 to 20% with the radial immunodiffusion technique. 5erum-neutralization tests in mice support the finding of neutralizing antibody by the PRN technique. Ultracentrifugation and 2-mercaptoethanol studies indicate that the cross-reactions are the result of immunoglobulin M or similar macroglobulins.

Animals

Streptococcal M protein extracted by nonionic detergent. III. Correlation between immunological cross-reactions and structural similarities with implications for antiphagocytosis.

Three immunologically cross-reactive and non-cross-reactive streptococcal M proteins were analyzed by a chromatographic tryptic peptide mapping system. The results indicate that cross-reactions correlate with the extent of structural similarity among the M protein molecules analyzed. The data also reveal that free lysine is released by the action of trypsin from these three M proteins, suggesting a common lys-lys or arg-lys sequence. In addition, only one peptide has been found to be common within all three M types. This limited structural relatedness among the three M proteins examined indicates that sequence variation plays a major role in the immunological specificity of the M antigens. However, despite sequence variation, all M protein molecules have a common antiphagocytic activity. The fact that no common opsonic antibody has yet been found, even against limited M types, argues against this biological activity being solely the result of a common sequence. Based on these data, it is suggested that the antiphagocytic effect of M protein may be due to a conformationally created environment on the surface of the molecule which is selected by both immunological and biological pressure.

Antigens, Bacterial

[Studies on cross reactions of antisera against nucleotid-protein conjugates with denaturated desoxyribonucleic acids].

The reactivity of anti-nucleotide-sera (anti-UMP, anti-AMP, anti-GMP) with denatured DNA's of 10 different sources was investigated by means of quantitative complement fixation. The haptene specificity of the anti-nucleotide antibodies was shown by haptene inhibition of the reaction with DNA. Anti-UMP showed cross-reactions with other pyrimidine-derivatives, but to a lesser extent; anti-GMP cross-reacted with adenine structures. Quantitative differences were observed in the reaction of anti-UMP, anti-AMP and anti-GMP with DNA's of various (G + C)-contents. These differences could not be correlated in all cases with the overall base composition of the DNA.

Animals

Immunochemistry of serum albumin. VI. A dynamic approach to the immunochemical cross reactions of proteins using serum albumins from various species as models.

Antisera against bovine serum albumin were raised in two rabbits. Serial bleedings were obtained at different times after the first immunization, and antisera from these serial bleedings were not mixed but were kept and studied separately. The immunochemical cross-reactions of these antisera with serum albumins from bovine, goat, sheep, porcine, horse, human and chicken were determined by immunoadsorbent studies. These were done by titration so that the values of maximum (plateau) binding by each albumin of radioiodinated antibodies were determined. In each rabbit, the immunochemical cross-reactivity was not static but increased progressievly with time after the first immunization. In the interval 7 days to 398 days the increases in cross-reaction were extremely large. pH dissociation studies revealed that, together with the increase in cross-reactivity of a given albumin with time after immunization, there was a restriction in the antibody heterogeneity towards populations possessing higher affinity. These results provide a rational explanation for the different values of cross-reactivities for a given albumin from different laboratories. The findings are analyzed in relation to the antigenic structure of albumin and their significance in evolutionary studies discussed.

Animals

Cross-reactions between Bordetella pertussis and twenty-eight other bacterial species.

Cross-reactions between B. pertussis and 28 other bacterial species were studied by various quantitative immunoelectrophoretic methods. A sonicated B. pertussis antigen preparation and a corresponding pooled rabbit antiserum were used as reference system. Two of the B. pertussis antigens were cross-reactive with antigens from 17, respectively 19, other bacterial species mainly gram-negative species. As judged by absorption of antibodies, the degree of cross-reactivity of these B. pertussis antigens with antigens from other species was found to be in the range 25-30%. Antigens from B. parapertussis and B. bronchiseptica were found to cross-react very extensively with B. pertussis, and only 4, respectively 2, of the 44 antigens of the B. pertussis reference system could not be absorbed with antigens from these two Bordetella species.

Antibodies, Bacterial

Some serological cross-reactions between Streptococcus mutans, S sanguis, and other dental plaque streptococci.

From the preliminary observations described in this report, the following conclusions may be drawn. When attempting to produce diagnostic antiserums specific for S mutans, S mitior, or S sanguis, care must be taken to eliminate cross-reactions as a result of antibodies against extracellular glucans or dextrans. Other antigenic components, associated with the cell wall, may be common to different species. One soluble protein or polypeptide antigen normally present in S sanguis and S mitior may also be demonstrated in certain strains of S mutans. Antiserums prepared against S sanguis, S mitior, or S mutans should be carefully checked for interspecies cross-reactions before being used for identification purposes.

Agglutination

Cross reactions of normal bovine sera with foot-and-mouth disease virus: incidence, duration, and effect of shipping stress.

Serum samples were obtained from 30 Hereford steers in an area known to be free of foot-and-mouth disease (FMD) viruses as follows: before shipment and 4 times during a 70-day period after shipment; the sera were tested for the presence of cross-reacting antibody to various viruses. Percentages of sera containing cross-reacting antibody to FMD virus detected by the plaque-reduction neutralization and the radial immunodiffusion techniques were higher for the FMD viruses Asia and SAT I5 than for the FMD viruses A5, O1, and C1. Cross-reacting antibody was usually of low titer and usually present in only 1 or 2 consecutive serum samples. The incidence of cross reactions increased after stress of shipping and thus an infective agent may be responsible. These results were compared with results from sera collected from Herefords and Holstein-Friesians in a 2nd area; results did not indicate that Herefords have an excess of cross reactions with FMD viruses.

Animals

Cross-reactions between tryptic polypeptides of staphylococcal enterotoxins B and C.

The strong cross-reactions demonstrated for staphylococcal enterotoxins B (SEB) and C1 (SEC1) by measurement of antigen-binding capacity were reflected in well defined polypeptides obtained by limited tryptic digestion from SEB and SEC1. Two antigenic determinants on each enterotoxin were capable of reacting with heterologous antibody, one on the first 57 amino acids and one on the last 150 residues of the polypeptide backbone. The larger, carboxyl terminal polypeptides bound efficiently to homologous antiserum but about two orders of magnitude less efficiently to heterologous antibody. The amino terminal peptides showed only weak homologous binding but nearly comparable heterologous binding. It is proposed that the determinant on the amino terminal polypeptides is largely responsible for the strong reciprocal binding of the intact enterotoxins and that their low antigen-binding capacity is due to a random or a structurally distorted conformation in solution.

Animals

Actomyosin content of Physarum plasmodia and detection of immunological cross-reactions with myosins from related species.

The content of myosin in plasmodia of the myxomycete Physarum polycephalum was measured by an immunological technique, quantitative microcomplement (C') fixation. Migrating plasmodia (starved after growth on rolled oats) contained 0.60 +/- 0.08 (SD) mg myosin per g fresh plasmodia. Myosin comprised 0.77% +/- 0.05 (SD) of the total plasmodial protein. When total plasmodial proteins were separated by electrophoresis on SDS-polyacrylamide gels, a large amount of protein appeared in a band comigrating with muscle actin. Densitometry performed after Coomassie blue staining indicated that as much as 15-25% of the total protein in the plasmodium could be actin. This gives an actin/myosin ratio by weight in the myxomycete plasmodium as high as 19-33, a very "actin-rich" actomyosin compared with rabbit skeletal muscle actomyosin with an actin/myosin ratio of 0.6. Starvation stimulates rapid migration and is correlated with a higher percent of both myosin and actin in the total protein of the plasmodium compared with normally growing cultures. Immunological cross-reaction of myosins from a variety of species was measured by C' fixation using an antiserum produced against purified native myosin from P. polycephalum. Although myxomycete and vertebrate striated muscle myosins have very similar morphological and biochemical properties, and apparently possess similar binding properties to F-actin, only myosins from myxomycetes in the order Physarales, rather closely related to P. polycephalum, gave detectable cross-reactions. This finding suggests that many amino acid sequences in myosin have been variable during evolution.

Actins

Use of RAST technique in wasp sting hypersensitivity. Cross-reactions between various insect antigens are specially considered.

Clinical hypersensitivity to wasp stings was found to be fairly well correlated with the presence of serum IgE-antibodies against yellow jacket venom as detected by the RAST technique. Such antibodies were never found in a control group of non-allergic blood donors, but they were detected in a surprisingly large proportion of patients with bee sting allergy without known allergic reactions to wasps. Studies using RAST inhibition technique failed to prove cross-reactions between bee and wasp venoms. Considerably better results were obtained when venom antigens instead of whole body antigens were used in the RAST. RAST inhibition studies suggested that IgE-antibodies detected with RAST using whole body antigen are directed against bee venom constituents in the whole body extract.

Antibodies

Immunohistochemistry of carcinoembryonic antigen: characterisation of cross-reactions with other glycoproteins.

In the course of demonstrating carcinoembryonic antigen (CEA) in normal human small intestine cross-reactivity of specific antiserum against red blood cells, vascular endothelium, and Paneth cell granules was noted. Pretreatment of sections with periodic acid eliminated these cross-reactions without affecting the staining of CEA, indicating that the antigenic determinants shared between CEA and other glycoproteins are in the carbohydrate portion of the molecules. These findings emphasise the caution with which immunohistochemical results should be regarded even when they are apparently well controlled.

Carcinoembryonic Antigen

Enzyme immunoassay of antibody to Rochalimaea quintana: diagnosis of trench fever and serologic cross-reactions among other rickettsiae.

Enzyme immunoassay (EIA) tests were used to diagnose trench fever and to determine cross-reactions of Rochalimaea quintana with other rickettsiae. The results were compared with those obtained by counterimmunoelectrophoresis (CIE). All sera from cases of primary or relapsed forms of trench fever were positive both in EIA, with serum antibody titers of 1:20-1:640, and in CIE, giving one to three precipitin lines. Sera from patients with other rickettsial infections were also tested for reactivity with R. quintana antigen: typhus group (Rickettsia prowazekii, Ricketsia mooseri), 15 sera; spotted fever group (Ricketsia ricketsii, Rickettsia akari), eight sera; and scrub typhus (Rickettsia tsutsugamushi), six sera. Strong reactions occurred with four sera from patients with scrub typhus, giving one or two lines in CIE and EIA titers of 1:40-1:160; these results were extended to guinea pig antisera to R. tsutsugamushi. About 50% of typhus group sera reacted with a single line in CIE and had antibody titers of 1:20-1:80 by EIA. The results show that EIA is accurate for the diagnosis of trench fever and, with the results obtained by CIE, suggest that R. quintana is antigenically related to R. tsutsugamushi and possibly to rickettsiae in the typhus group as well.

Antibodies, Bacterial

Immunodiffusion studies on Schistosoma mansoni and its host stage specific antigens. 2. Immunoelectrophoresis cross-reactions between hepato-pancreas of Biomphalaria glabrata and Biomphalaria alexandrina.

IMMUNOELECTROPHORESIS was used for studies on immunological cross-reactions between both Schistosoma mansoni (S. m.) intermediate host snails Biomphalaria glabrata and Biomphalaria alexandrina. The preparation of antigens and their corresponding antisera from hepato-pancreas of S. m. infected and non infected snails was described as the homologous reactions of both snails either infected or non infected were rather similar, close immunological relationship between B. glabrata and B. alexandrina could be deduced.

Animals

Cross-reactions of Streptococcus mutans due to cell wall teichoic acid.

Antisera to the whole cells of Streptococcus mutans cross-reacted with antigen extracts from four other gram-positive species, as well as with those of three other oral streptococci. Similarly, antisera to these bacteria cross-reacted with extracts from S. mutans and with those from each other. Using a purified phenol extract of the walls of S. mutans, which was identified by chemical, immunochemical, and enzymatic analyses as glycerol teichoic acid, the cross-reactions were shown to be specific for a determinant of the teichoic acid backbone. Results were confirmed in immunodiffusion tests where clear bands of identify were shown. These observations point out the need for caution in sereological research empolying extracts of gram-positive bacteria and may be of interest in investigations of periodontal disease.

Antibodies, Bacterial

Cross-reactions between serum proteins and water soluble liver tissue antigens of the nine-banded armadillo (Dasypus novemcinctus Linn.) and man.

Cross-reactions between serum proteins and water soluble liver antigens of the nine-banded armadillo (Dasypus novemcinctus Linn.) and man were studied by crossed immunoelectrophoresis (CIE). Armadillo serum tested with rabbit antiserum against human serum proteins gave twelve components in CIE. Nine of these cross-reacting proteins were identified and showed partial identity with the corresponding human proteins. The electrophoretic mobility of alpha 2-macroglobulin and Gc-globulin differed in the two species. An ultrasonicate of normal armadillo liver gave twenty-eight anodic and eight cathodic components in CIE. By absorption experiments with armadillo serum, twenty of the former and seven of the latter were shown to be liver tissue components. A combination of CIE and crossed-line immunoelectrophoresis (CLIE) revealed the presence of twelve anodic and six cathodic liver tissue components cross-reacting with man. A cathodic armadillo liver antigen called (CALA-17) showed partial identity with that of man both in tandem and fused rocket immunoelectrophoresis. The implications of the findings are discussed in relation to the use of armadillo-grown M. leprae for skin testing and other purposes in man.

Animals

L-forms of Pseudomonas aeruginosa. 3. The serological cross-reactions among stable L-forms of Pseudomonas aeruginosa, L-form of Streptococcus pyogenes and mycoplasmas.

The serological cross-reactions among stable L-forms of Pseudomonas aeruginosa, or of Streptococcus pyogenes and mycoplasmas were investigated in passive hemagglutination (PHA) and agar gel diffusion tests. (1) PHA active fraction which reacts most strongly with homologous serum was obtained from the sodium dodecyl sulfate soluble fraction of L-form membrane after disruption by Braun cell homogenizer. (2) Antiserum prepared against L-forms in rabbits showed high-level stimulation of PHA antibodies, while it showed little stimulation of agglutinating antibodies. (3) In PHA and agar gel diffusion tests, antiserum to L-form of P. aeruginosa strain IFO-3,455 reacted with L-form of strain N-10, which is serologically different in serotype from strain IFO-3,455. Furthermore, the two L-forms of P. aeruginosa cross-reacted with a L-form of S. pyogenes. 4) L-forms of P. aeruginosa and S. pyogenes did not react with five strains of mycoplasmas in PHA and agar gel diffusion tests.

Antigens, Bacterial