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PubMed1973

Detection of idiotypic cross-reactions among streptococcal antisera from related rabbits.

Idiotypic cross-reactions among antibodies to Group C streptococcal carbohydrate were studied using idiotypic antisera prepared in allotypically matched rabbits. Antibodies with idiotypic cross-specificity to one proband antibody were detected in 58% of the antisera from related rabbits, while approximately 1% of nonrelated rabbits produced antibody with this specificity. The cross-specificity was related to the group a (V(H)) allotype of 133 rabbits tested with only one exception. Studies utilizing antisera against a second proband antibody failed to detect antibodies with idiotypic cross-reactivity among the same group of related rabbits. This result emphasizes the variation in expression of idiotypic determinants of antibodies. It was further shown that the presence of anti-IgG's in the streptococcal antisera interfere with the detection of idiotypic cross-reactions. These anti-IgG's masked the presence of antibodies with idiotypic cross-specificity when inhibition of precipitation tests were used for their detection.

Animals↗
PubMed1983

Precipitating cross-reactions among pneumococcal types.

Data accumulated over many years are brought together on cross-reactions of 46 among the more than 80 pneumococcal serological types, with the idea of correlating cross-reactions with the structures of the relevant type-specific capsular polysaccharides, insofar as these have been determined. The precipitin reaction was carried out with the polysaccharides and antibodies raised in horses, rabbits, and a mule. Quantitative values (micrograms of antibody nitrogen per milliliter of antiserum at 0 to 1 degree C) are given in many instances and discussed, together with arbitrary qualitative data, in terms of the known structures of the polysaccharides. Some precise relationships are uncovered, and an attempt is made to determine why some of the cross-reactions are reciprocal and why others are only unilateral.

Cross Reactions↗
PubMed1987

How probable are antibody cross-reactions?

Antibodies to polypeptides are increasingly being used in research. Their specificity and tight but reversible binding make them ideal for applications such as identification of proteins, immunological quantification or purification, and peptide mapping. Antibodies are also used in medicine to deliver loads to specific sites in tissues, and in electron microscopy as heavy metal conjugates to locate antigens in thin sections. While these techniques depend on specificity of antibody binding, it is occasionally observed that cross-reactions occur. These cross-reactions are attributed to the existence of one or more antibody binding sites common to both polypeptides. It is important to know whether these cross-reactions are expected due to chance alone, or if they are improbable and likely due to some causative agent. Examples of such causative agents might include gene duplication events or convergence due to functional constraints. At the present time, good methods for predicting the probability and therefore the frequency of cross-reactions are unavailable. In this paper we apply some recently reported mathematical results to address the following questions: (1) What is the probability that polyclonal or monoclonal antibodies raised against a given polypeptide will cross-react with another polypeptide due to chance alone? (2) What is the probability that polyclonal or monoclonal antibodies raised against a given polypeptide will cross-react with one or more polypeptides in a pool of polypeptides? Approximate answers to these questions are presented for cases where amino acid compositions of linear polypeptides are known or unknown, but the amino acid sequence of one or more of the polypeptides is not known. Implications of the results for antibody use in protein research are discussed.

Amino Acid Sequence↗
PubMed1995

[Contact allergies to corticosteroids. Prevalence, cross-reactions and methods of detection].

Topical corticosteroids (CS) are frequently used to treat of allergic contact dermatitis, so that their own potential for sensitization is rarely detected. However, increasing numbers of hypersensitivity reactions to corticosteroids have been reported during the last 10 years, and allergic skin reactions to over 50 particular compounds have been observed. CS must now be regarded as a rather frequent contact allergen, the prevalence being twice as high in women as in men. Contact allergy to CS is clinically characterized by a chronic and persistent, corticosteroid-resistant dermatitis. In general, hypersensitivity to CS is a type I and/or type IV mediated allergic reaction. Cross-sensitivity between individual corticosteroid preparations has been described owing to their closely related chemical structures (e.g. hydrocortisone and tixocortol pivalate). Contact allergy to CS can be confirmed by patch-tests, intradermal injection tests or application tests; because of the delayed appearance of positive skin reactions a prolonged evaluation period of up to 120 h is recommended. For routine screening the use of the patient's own material and of tixocortol pivalate and budesonide as test marker substances seems appropriate. The development of further marker substances is a target for ongoing research.

Administration, Topical↗
PubMed1982

Evolution of HLA antigenic determinants: species cross-reactions of monoclonal antibodies.

The reactions of mouse monoclonal HLA-A-, -B-, -C-specific antibodies on cells from 50 species were analyzed by binding assay. Antibodies which are monomorphic in humans generally show monomorphic behavior in other species and many significant cross-reactions were seen. Antibodies which recognize highly specific polymorphic determinants gave few cross-reactions with other species. Antibodies which recognize broad polymorphic determinants in humans cross-reacted in a polymorphic manner with many other species. The patterns of cross-reaction for both monomorphic and broadly polymorphic determinants correlated roughly with the current picture of phylogenetic relationships. These results show there are two fundamentally different classes of polymorphic determinants, one which appears relatively conserved in evolution and one which is the product of recent change. They probably correlate with the public and private antigens of mouse H-2 antigens. A simple genetic model of HLA-A, -B, -C genes, whereby all specificities at a locus are true alleles, is sufficient to explain these patterns of cross-reaction. It seems likely that cross-reactions previously seen with alloantisera were due to broadly polymorphic antibodies rather than to allele-specific antibodies. If this were the case, then no experimental basis for Bodmer's model of MHC polymorphism being due to control of expression of a tandem array of genes exists.

Animals↗
PubMed1980

The nature of secretory agglutinins and aggregating factors. III. Secretory conglutinin-like factor SKF detects a cross-reaction between bacteria and complement component C3.

Secretory conglutinin-like factor (SKF) reacts directly with an unknown surface component of some, but not all, oral gram-positive organisms. The absorption of SKF by bacteria is EDTA-sensitive and cannot be blocked with immunoglobulins. High levels of SKF in EDTA extracts of washed salivary sediment reveal the direct in vivo reaction of SKF with oral bacteria. Mixed aggregation with alexinated erythrocytes showed the SKF corresponds to the secretory bacterial aggregating factor (SBAF) for Streptococcus mutans serotype c and also that for Streptococcus mitis. These reactions represent a cross-reaction between bacteria and complement component C3. SKF/SBAF non-mucin glycoproteins and immunoglobulins possess receptors for bacterial components while mucins are passive carriers of blood group determinants.

Agglutinins↗
PubMed1996

Contact dermatitis due to topical steroids with conceivable cross reactions between topical steroid preparations.

Steroids are usually employed to inhibit inflammation. However, allergic contact dermatitis has been reported with topical steroids. We have experienced contact dermatitis due to active ingredients of topical steroids in 11 patients. Therefore, we make it a rule to carry out the patch test with as many topical steroids as possible. Five patients were confirmed to be positive to several corticosteroids in the patch test. Papers on patients allergic to steroids indicate that some patients react to several. It is difficult to evaluate whether the reaction is caused by multisensitivity or by cross reaction. However, even if steroids differ in type, they may often cause cross reactions when they have a common chemical structure. Considering this chemical structure, we tried to classify steroids reported to cause allergy in patients into the following four types: 1) The type recognizing betamethasone and/or dexamethasone. Regardless of whether the methyl group at the C-16 position of the D ring is on the alpha or beta side, the size of the blocking group of the hydroxy residue seems to be associated with the reaction. 2) The type in which a chlormethylketone group at the C-17 position of the D ring seems to be associated with the reaction. 3) The type in which a cis-diaxial-diol side chain in the alpha side of C-16 and C-17 positions of the ring D or its ketal blocking group seems to be associated with the reaction. 4) The type in which the size of the ester protecting the hydroxy group at the C-17 alpha position seems to be associated with the reaction. In patients showing a reaction, there may be receptors recognizing each steroid. If the steroid administered is changed, the receptor appears to recognize the changed steroid in a relatively short period. Thus the receptor may not be constant.

Administration, Topical↗
PubMedDate not supplied

[Cross-reactions between the antigens of healthy pulmonary tissue and Moraxella catarrhalis].

The study of cross-reactions between healthy pulmonary tissue antigens and Moraxella catarrhalis with the use of SDS-electrophoresis and immunoblotting revealed that in the component of healthy pulmonary tissue with a mol. wt. of 40 kD epitopes existed to which antibodies were produced, capable of cross reaction with the components of M. catarrhalis with a mol. wt. of 35 kD and 70 kD. In addition, the presence of cross-reactions between cytokeratin-8, protein contained in healthy pulmonary tissue, and M. catarrhalis antigens was established.

Antigens↗
PubMed1996

Serological cross reaction between legionella and campylobacter in the rapid microagglutination test.

AIMS: To investigate the serological cross reaction between legionella and campylobacter using the rapid microagglutination test (RMAT). METHODS: Serum samples from 49 patients with campylobacter infection were tested for legionella antibodies using the indirect fluorescent antibody test (IFAT) and the RMAT. Serum samples that had positive RMAT titres were retested in the presence of a campylobacter immunosorbent. The specificity of the immunosorbent was evaluated with serum from patients with genuine legionella infection (legionella culture or antigen positive, or both). RESULTS: Fourteen (28%) patients with campylobacter infection had positive IFAT titres (> or = 16) and 16 (32%) patients had positive RMAT titres (> or = 8) in one or more serum samples. In addition, serum samples from 11 of 17 patients with campylobacter infection, previously shown to have positive legionella IFAT titres, were also RMAT positive. Sixteen patients had RMAT titres of > or = 32, including seven with titres of > or = 128. RMAT titres from all but one patient were significantly reduced after campylobacter absorption, but serum samples from 48 patients with legionella infection were unaffected. CONCLUSIONS: Serological cross reaction between campylobacter and legionella can occur in the legionella RMAT, as well as the IFAT. This cross reaction can be eliminated in most cases by incorporating a campylobacter immunosorbent in the RMAT.

Agglutination Tests↗
PubMed1983

Serologic cross-reactions among rabbit secretory IgA molecules: evidence for multiple subclasses of secretory IgA-f molecules.

Serologic cross-reactions among allotypes of rabbit secretory IgA (sIgA) of the f-subclass were examined by quantitative radiobinding assays with various allo-anti-alpha chain reagents. Numerous cross-reactions were observed which demonstrated the complexity of the C alpha f allotypes. One of the reagents used in these studies reacted not only with all sIgA molecules of the immunogen C alpha f allotype but also with all sIgA molecules of the other C alpha f allotypes. Aliquots of the antiserum were each adsorbed with IgA molecules of these C alpha f allotypes and then used in radiobinding studies with sIgA-f molecules of the various C alpha f allotypes. The adsorbed reagents reacted with some but not all sIgA-f molecules, thus indicating that the C alpha f allotypes each comprise more than one serologically distinguishable subset. Results from these radiobinding experiments were used to develop a model in which each of the five IgA-f allotypes comprises at least two serologically distinguishable subsets. Each of these subsets expresses a unique pattern of C alpha determinants. These C alpha determinants appear to be protein in nature rather than carbohydrate as periodate oxidation of the sIgA-f glycoproteins does not affect the reactions of the molecules with the cross-reactive alloreagents. IgA molecules of the serologically distinguishable subsets presumably differ in amino acid sequence in the constant region and, thus, would be products of distinct C alpha genes. Therefore, it is probable that the cross-reactions of these molecules, which were previously thought to comprise a single subclass, sIgA-f, may reflect the presence of more than one subclass of sIgA-f molecules, i.e., a third subclass of rabbit sIgA.

Animals↗
PubMed1976

Immunologic cross-reactions between the specifically localizing cells (SLC) generated in response to sheep RBC and the red cells of other species.

Some of the lymphoid cells selectively incorporating radioactive thymidine 3 days after primary immunization with SRBC which are capable of specifically localizing in the lymph nodes of adoptively immunized syngeneic recipients challenged with SRBC (SLC-SRBC)2 are also capable of specifically localizing in lymph nodes challenged with the red blood cells of a varieth of other mammalian species. The one nonmammalian RBC tested, CRBC, failed to cross-react with SRBC by this parameter even qualitatively, although it remains possible that a feeble cross-reaction might be demonstrated with large enough experimental groups. As expected, the magnitude of the observed cross-reactions seems to vary inversely with the phylogenetic distance between the species, with ORBC showing the strongest cross-reaction (41 to 49%), ARBC showing the weakest (8 to 13%), and BRBC and HRBC occupying intermediate positions (13 to 20%). Cross-reaction between secondary anti-SRBC antibodies and the red cells of the other species were weak and inconstant, suggesting that the observed cross-reactions of specific localization may involve T cells more than B cells. During the course of these studies, it was also possible to verify experimentally our impression that with existing methods of selectively labeling SLC it is possible to study the phenomenon of specific localization using only one population of labeled cells, providing certain essential controls are employed.

Animals↗
PubMed2005

Cross-reaction between antibodies to the major epitope of Ro60 kD autoantigen and a homologous peptide of Coxsackie virus 2B protein.

Coxsackie virus RNA has recently been detected in biopsy specimens of minor salivary glands from patients with primary Sjögren's Syndrome (pSS). A peptide derived from Coxsackie virus 2B protein (pepCoxs) presents 87% sequence homology with the 222-229 region of the major linear B-cell epitope of Ro60 kD autoantigen (pep216-232). Synthetic peptides corresponding to pep216-232: (216)KALSVETEKLLKYLEAV(232) and pepCoxs: (31)MVTSTITEKL LKNLVKI(47), were prepared. Sera from 42 patients with pSS and 43 patients with systemic lupus erythematosus (SLE) as well as sera from 27 healthy individuals (normal controls) and sera from 30 patients with rheumatoid arthritis (disease controls) were tested against the two homologous peptides. Twenty-five percent of SLE sera and 33.3% of pSS sera reacted against pep216-232, whereas 28% of SLE sera and 37% of pSS sera recognized the pepCoxs. The sera reacting with pep216-232 were apparently the same as those reacting with pepCoxs. Normal sera and disease control sera presented only a limited reactivity against both peptides (ranging from 3.7% to 10%). Both peptides reacted more prominently with anti-Ro/La (+) sera from pSS patients. Thus, pep216-232 was recognized by 17% of the anti-Ro (+) sera and by 42% of the anti-Ro/La (+) sera, whereas pepCoxs was recognized by 28.5% and 38% of the a-Ro(+) and a-Ro/La(+) sera, respectively. Purified anti-pep216-232 antibodies readily reacted with both peptides while inhibition experiments revealed the specificity of this reaction. These results suggest a possible cross-reaction between antibodies to the major linear B-cell epitope of Ro60 kD autoantigen and the homologous pepCoxs in pSS patients. This cross-reaction might potentially play a role in autoantibody formation and the perpetuation of the autoimmune response against Ro/SSA and La/SSB.

Antigens, Viral↗
PubMedDate not supplied

Elimination of mycoplasmal plate agglutination cross-reactions in sera from chickens inoculated with infectious bursal disease viruses.

Sera from chickens inoculated with various challenge infectious bursal disease viruses or infectious bursal disease vaccines were found to cross-react in the Mycoplasma gallisepticum (MG) and Mycoplasma synoviae (MS) serum plate agglutination (SPA) tests. Two-fold dilutions of these cross-reacting sera with phosphate-buffered saline before retesting eliminated all non-specific agglutination in the MG and MS SPA tests. Cross-reactions were observed in the SPA test using sera from chickens inoculated with either MG or MS. Dilutions of these sera 1:2 had little effect on the number of these cross-reactions. At 1:4 serum dilutions, however, the number of cross-reactions between MG and MS was reduced. At 1:8 dilution of test sera, cross-reactions between MG and MS were further reduced. Some reduction in specific MG and MS SPA reactions, however, also occurred at the 1:8 dilution of sera with some of the plate antigen.

Agglutination Tests↗
PubMed1998

Lack of cross-reaction between antibodies to beta2-glycoprotein-I and oxidized low-density lipoprotein in patients with antiphospholipid syndrome.

Previous studies have shown a cross-reaction between anticardiolipin and anti-oxidized low-density lipoprotein (LDL) antibodies in patients with the antiphospholipid syndrome (APS). The aim was to investigate the existence of a cross-reaction between anti-beta2-glycoprotein-I (beta2-GP-I) and anti-oxidized LDL antibodies in a group of APS patients. Ninety-three patients with APS were included in the study; 47 of these patients were diagnosed as primary APS, while the rest (46 patients) fulfilled criteria for the classification of systemic lupus erythematosus (SLE). All patients were positive for the IgG isotype of anticardiolipin antibodies (aCL). Twelve (26%) SLE-associated APS and 14 (29.7%) primary APS patients had raised concentrations of IgG antibodies to oxidized LDL. There was no correlation between anti-beta2-GP-I and anti-oxidized LDL antibodies. Inhibition experiments showed no cross-reaction either between anti-beta2-GP-I and anti-oxidized LDL antibodies, or between anti-beta2-GP-I and anti-native LDL antibodies. Our study suggests that the presence of both anti-beta2-GP-I and anti-oxidized LDL antibodies in patients with APS is not due to the structural similarity and consequent cross-reaction, and that they are two different populations of antibodies directed against different antigens.

Adolescent↗
PubMed1995

Cross-reactions of sera from Toxascaris leonina and Ascaris suum infected mice with Toxocara canis, Toxascaris leonina and Ascaris suum antigens.

The ELISA method using larval ES products and homogenized Toxocara canis, Toxascaris leonina and Ascaris suum adult worms extract, was used to determine the possible cross-reactions in BALB/c and C57BL/10 mice inoculated with embryonated eggs or adult worms extract of T. leonina of T. leonina or A. suum in single and multiple doses. When we used sera of mice infected with embryonated eggs of T. leonina against different heterologous Ag, no cross-reactions against T. canis ES and A. suum ES Ag were observed using a single dose. Similarly, in multiple doses no response against T. canis ES Ag was observed. In mice inoculated with adult worms extract of T. leonina cross-reactions with T. canis ES and A. suum ES Ag did not occur. Sera from BALB/c mice infected with embryonated eggs of A. suum, was tested using ES Ag from both A. suum and T. canis and no reactions were observed. This fact confirmed the resistance of this murine strain to A. suum embryonated eggs. When we used sera of susceptible C57BL/10 mice infected against different heterologous Ag, we observed no cross-reactions against T. canis ES Ag. In the case of both BALB/c and C57BL/10 and C57BL/10 mice immunized with a single dose of A. suum adult crude extract no cross-reactions were seen against ES T. canis Ag and with sera from C57BL/10 mice against ES T. leonina. These facts confirmed the specificity of the ES T. canis Ag.

Animals↗
PubMedDate not supplied

[The background of the serological cross-reaction between Yersinia and Brucella and the possibility of differential diagnostics by the ELISA technique and the electroimmuno assay (rocket electrophoresis) (author's transl)].

A strong serological cross-reaction appears between different species of genus Brucella and Yersinia enterocolitica (Y.e.) serotype 0--9, which seriously complicates the diagnostic works of brucellosis and yersiniosis both in humans and animals. This cross-reaction makes it impossible to perform a differential serological diagnosis using common routine procedures such as the agglutination test and the complement fixation test. By the use of immunological, immunochemical and structural chemical methods it has been shown that the common antigenic structures of Brucella and Yersinia are situated in the lipopolysaccharides (LPS) of the cellwalls. In order to do structure analysis gaschromatography in combination with mass spectrometry of LPS from Brucella and Yersinia bacteria has been achieved. The results show that two monosaccharides (glucose and galactose) constitute common components of the LPS-molecules. A discovered cross-reaction between Y.e. 0--9 and Salmonella urbana (0--30) confirms the hypothesis that glucose and galactose are responsible for the serological cross-reaction between Brucella and Y.e. 0--9. An enzyme-linked immunosorbent assay (ELISA) has been developed in order to be used as a differential routine test. The results show that by using ELISA, a differentiation between antibodies against Y.e. 0--9 and B. abortus can be done with high sensitivity and accuracy. Another differential diagnostic system has been developed by the use of electroimmuno assay (rocket electrophoresis). This method raises the possibility of a rapid and a simple qualitative differentiation of antibodies against Brucella and Yersinia.

Agglutination Tests↗
PubMed1984

Serological cross-reactions between Mycoplasma genitalium and Mycoplasma pneumoniae.

The recently discovered mycoplasma species Mycoplasma genitalium was isolated from urethral specimens from men with nongonococcal urethritis (Tully et al., Lancet i:1288-1291, 1981). In a previous report (K. Lind, Lancet ii:1158-1159, 1982), prominent serological cross-reactions were demonstrated between this mycoplasma and M. pneumoniae. In the present study, the two mycoplasma species were compared more extensively. In classical mycoplasma medium without thallium acetate, M. genitalium grew more slowly than M. pneumoniae did but finally formed similar amounts of acetic acid and lactic acid from glucose. Although their colonies on solid medium were indistinguishable, transmission electron microscopy showed that the flask-formed cells of M. genitalium (especially their necks) were shorter than those of M. pneumoniae. The two species were distinct since DNA hybridization showed only 1.8% homology in base sequences, and sodium dodecyl sulfate-polyacrylamide gel electrophoresis revealed significantly different profiles of the two strains. However, considerable similarities were found in their antigenic reactions in various serological tests. The presence of common or closely related antigens was demonstrated in the two species with rabbit immune sera in complement fixation test with chloroform-methanol-extracted antigens by an indirect immunofluorescence test on microcolonies, and by metabolism inhibition and growth inhibition tests. Cross-reactions were also demonstrated by crossed immunoelectrophoresis. The role of M. genitalium as a human pathogen in the genital tract has not been assessed. If serological tests are to be used in this assessment, caution must be exercised due to the extensive cross-reactions demonstrated. Some of the species-specific antigens which we have demonstrated would be appropriate for use in such tests and would help to circumvent problems caused by cross-reactions.

Animals↗
PubMed1978

Cross-reactions between Neisseria meningitidis and twenty-seven other bacterial species.

Cross-reactions between antigens from N. meningitidis and antigens from 27 other bacterial species from clinical isolates representing 20 different genera were studied by quantitative immunoelectrophoretic methods. A water-soluble N. meningitidis antigen preparation and a corresponding pooled rabbit antiserum regularly presenting 48 immunoprecipitates were used as reference system. Antigens from 16 other bacterial genera cross-reacted with one to four N. meningitidis antigens, whereas antigens from six other Neisseria species cross-reacted with 37 to 48 N. meningitidis antigens. Antigens from only three bacterial genera (Streptococcus, Staphylococcus and Bacteroides) did not show any cross-reactions. The degree of cross-reactivity between the antigens were 25--100%, as judged by absorption of antibodies. Three of the cross-reacting antigens reacted with normally occurring precipitating antibodies in serum from humans and rabbits.

Antigens, Bacterial↗