scholarly journals The serological relationship betweenBrucellaspp.,Yersinia enterocoliticaserotype IX andSalmonellaserotypes of Kauffmann-White group N

1975 ◽  
Vol 75 (1) ◽  
pp. 151-171 ◽  
Author(s):  
M. J. Corbel
Keyword(s):  
Complement Fixation ◽  
Fluorescent Antibody ◽  
High Titre ◽  
Antigenic Structure ◽  
Antigenic Determinants ◽  
Serological Relationship ◽  
Homologous Strain ◽  
Cross Absorption ◽  
Salmonella Serotypes ◽  
Monospecific Antisera

SUMMARYThe serological relationship betweenBrucellaspp.,Yersinia enterocoliticaIX, and the group N salmonella serotypesS. godesberg, S. landau, S. morehead, S. neusdorf, S. soerengaandS. urbanawas examined using agglutination, antiglobulin, complement fixation, immunodiffusion and fluorescent antibody methods.Antisera to the group N salmonella serotypes all reacted to significant titres in agglutination and complement fixation, but not antiglobulin or immunodiffusion tests with smooth brucella antigens. These antisera also reacted in agglutination, but not antiglobulin, tests withY. enterocoliticaIX. They did not react significantly in any tests with rough brucella antigens.Conversely, antisera to smoothBrucellaspp. agglutinated group N salmonellas to low titre andY. enterocoliticaIX to titres similar to those given against the homologous strain. Antiserum toY. enterocoliticaIX on the other hand reacted with smooth brucella antigens to high titre in agglutination, complement fixation and antiglobulin tests, and with the group N salmonella antigens to substantial titres in agglutination tests.In direct fluorescent antibody tests, smoothBrucellastrains andY. enterocoliticaIX reacted strongly with FITC-labelled antibody toBr. abortuswhereas the group N salmonella strains reacted weakly.In tests with monospecific antisera to the A and M determinants ofBr. abortusandBr. melitensisrespectively,Y. enterocoliticaIX reacted only with the antiserum to the A determinant whereas group N salmonellas reacted to low titre with both A and M antisera.The results of cross-absorption tests confirmed this relationship and suggested that the O30 antigens of group N salmonella serotypes contained antigenic determinants similar to, but not identical with, the antigenic structure shared by smoothBrucellaspp. andY. enterocoliticaIX.

scholarly journals Differentiation of the serological response to Yersinia enterocolitica and Brucella abortus in cattle

1970 ◽  
Vol 68 (4) ◽  
pp. 519-530 ◽  
Author(s):  
M. J. Corbel ◽  
G. A. Cullen
Keyword(s):  
Yersinia Enterocolitica ◽  
Rose Bengal ◽  
Brucella Abortus ◽  
Complement Fixation ◽  
High Titre ◽  
Antibody Responses ◽  
Serological Response ◽  
Diagnostic Use ◽  
Cross Absorption ◽  
Serum Agglutination

SUMMARYThe serological responses of cattle to inoculation with Brucella abortus and Yersinia enterocolitica type IX were compared. Complete cross-reactions were found in serum agglutination, antiglobulin, complement fixation and Rose Bengal plate tests. The cross-reaction between Br. abortus and Y. enterocolitica IX was confirmed by immunodiffusion tests. Although antibodies specific for each organism could also be detected by immunodiffusion tests with high titre rabbit or bovine sera, these tests were insufficiently sensitive for routine diagnostic use.A quantitative Rose Bengal plate test, using Rose Bengal stained Br. abortus and Y. enterocolitica IX, was developed which enabled the antibody responses to the two organisms to be differentiated. The specificity of this test was confirmed by cross-absorption experiments and its sensitivity was sufficient to permit evaluation of all bovine sera giving positive reactions to the serum agglutination test.

Synthesis of three Salmonella epitopes for biosensor studies of carbohydrate–antibody interactions

2002 ◽  
Vol 80 (8) ◽  
pp. 1131-1140 ◽  
Author(s):  
Henry N Yu ◽  
Chang-Chun Ling ◽  
David R Bundle
Keyword(s):  
Key Words ◽  
Self Assembled Monolayers ◽  
Antigenic Determinants ◽  
Amino Group ◽  
Assembled Monolayers ◽  
Construction Of Self ◽  
Terminal Amino ◽  
Salmonella Serotypes ◽  
O Antigens ◽  
Antibody Interactions

Disaccharides 1-3 corresponding to the antigenic determinants of Salmonella serotypes A, B, and D1 were synthesized in a form suited for use in biosensors. The disaccharide determinants each contain a unique 3,6-dideoxyhexose, namely abequose (3,6-dideoxy-D-xylo-hexose), paratose (3,6-dideoxy-D-ribohexose), and tyvelose (3,6-dideoxy-D-arabino-hexose), are α-linked to the 3-position of D-mannopyranose. The disaccharides were further derivatized with a linear aglycon that has a terminal amino group, and can be readily coupled to pertinent chains carrying a terminal thiol for the construction of self-assembled monolayers (SAMs). Efficient routes that employed a single 3,6-dideoxygenation step were developed for the synthesis of paratoside 15 and tyveloside 22.Key words: Salmonella O-antigens, lipopolysaccharide, abequose, paratose, tyvelose, 3,6-dideoxyhexose, deoxygenation, glycoside tethers, immobilization via pentenyl glycosides.

scholarly journals IMMUNOLOGIC STUDIES OF WATER-SOLUBLE HUMAN AMYLOID FIBRILS

1969 ◽  
Vol 130 (4) ◽  
pp. 797-808 ◽  
Author(s):  
Edward C. Franklin ◽  
Mordechai Pras
Keyword(s):  
Human Serum ◽  
Comparative Studies ◽  
Amyloid Fibrils ◽  
Complement Fixation ◽  
Cross Reactivity ◽  
Water Soluble ◽  
Antigenic Determinants ◽  
Normal Tissues ◽  
Absorption Studies ◽  
Normal Human

Eight preparations of soluble amyloid and degraded amyloid (DAM) were compared immunologically. Unlike amyloid fibrils, six of eight preparations of DAM proved to be relatively strong immunogens. Antisera to DAM reacted weakly or not at all with normal human serum or extracts of normal tissues, but were specifically reactive with amyloid fibrils or DAM. Comparative studies of DAM'S from eight different subjects showed some degree of cross-reactivity among them, yet demonstrated that they were not identical. Similar conclusions were obtained by quantitative precipitin and complement fixation analyses. Comparison of the amyloid fibrils with the homologous DAM by complement fixation and absorption studies demonstrated the existence in DAM of antigenic determinants that were lacking or inaccessible in the native fibrils. A search for amyloid precursors and antibodies to amyloid in the sera of 12 patients proved unsuccessful.

Fluorescent Antibody and Complement-Fixation Tests of Agents Isolated In Tissue Culture from Measles Patients.

1955 ◽  
Vol 90 (1) ◽  
pp. 118-122 ◽  
Author(s):  
S. M. Cohen ◽  
I. Gordon ◽  
F. Rapp ◽  
J. C. Macaulay ◽  
S. M. Buckley
Keyword(s):  
Tissue Culture ◽  
Complement Fixation ◽  
Fluorescent Antibody

A study of possible biohazards in the fluorescent antibody test using adenovirus, coxsackievirus, herpesvirus, and respiratory syncytial virus as antigens

1976 ◽  
Vol 4 (4) ◽  
pp. 322-325
Author(s):  
D Bardell
Keyword(s):  
Respiratory Syncytial Virus ◽  
Infectious Virus ◽  
Fluorescent Antibody ◽  
Antibody Test ◽  
Adenovirus Type ◽  
Antigenic Determinants ◽  
Syncytial Virus ◽  
Simplex Virus ◽  
Adenovirus Type 5

Infectious adenovirus type 5 and coxsackievirus type B5, both nonlipid-containing viruses, were isolated from cells fixed in acetone at 22 degrees C for 15 min, from acetone used for fixation, from the solution used for washing slides during the fluorescent antibody procedure, and after complete processing of antigen preparations with serial twofold dilutions of human antisera and fluorescein-labeled goat anti-human immunoglobulin G. Lipid-containing herpes simplex virus type 1 and respiratory syncytial virus were inactivated by acetone, and infectious virus could not be recovered at any stage in the fluorescent antibody test. Fixation in acetone at 56 degrees C destroyed the infectivity of adenovirus 5 and coxsackievirus B5 within 30 min, but no adverse effect on the antigenic determinants of either virus occurred until after 60 min, thus demonstrating that these antigens can be utilized without the hazard of infectious virus.

scholarly journals Immunochemical characterization of human plasma fibronectin

1980 ◽  
Vol 191 (3) ◽  
pp. 719-727 ◽  
Author(s):  
M Vuento ◽  
E Salonen ◽  
K Salminen ◽  
M Pasanen ◽  
U K Stenman
Keyword(s):  
Human Plasma ◽  
Antigenic Structure ◽  
Antigenic Determinants ◽  
Proteolytic Degradation ◽  
Plasma Fibronectin ◽  
Native Protein ◽  
Covalent Interaction ◽  
Antigenic Activity ◽  
Haemagglutinating Activity

Human plasma fibronectin has been purified by a non-denaturing affinity chromatography procedure [Vuento & Vaheri, (1979) Biochem.J. 183, 331–337], and antisera have been raised by immunizing rabbits with the native protein. The antisera reacted strongly with native fibronectin, but only weakly with reduced and alkylated fibronectin or with heat-denaturated fibronectin. Denaturation also affected the haemagglutinating and gelatin-binding activities of fibronectin and increased its susceptibility to proteolytic degradation. The antisera reacted with fragments of fibronectin obtained by proteolysis with plasmin. Large fragments (mol.wt. 180000–200000), lacking the region harbouring the interchain disulphide bridges but containing the sites responsible for gelatin-binding and haemagglutinating activity, showed as intense a reaction with the antisera as intact fibronectin. Smaller peptides showed a weaker reaction. All fragments tested showed sensitivity to denaturation in their reaction with the antisera. The results were interpreted as showing that: (1) native fibronectin has an ordered conformation that is easily perturbed by denaturation; (2) most of the antigenic determinants of the protein are dependent on conformation; (3) the region of the fibronectin molecule containing the interchain disulphide bridges has only few antigenic determinants; and (4) covalent interaction of the two subunits does not contribute to the antigenic structure recognized by rabbit antisera. The observed correlation between the antigenic activity and a structural and functional intactness of fibronectin suggests that the antibodies to native fibronectin could be used as a conformational probe in studies on this protein.

scholarly journals Immunocytochemical Studies on Platelets. The Demonstration of a Common Antigen in Human Platelets and Megakaryocytes

Blood ◽  
1960 ◽  
Vol 16 (1) ◽  
pp. 968-974 ◽  
Author(s):  
JACINTO J. VAZQUEZ ◽  
JESSICA H. LEWIS
Keyword(s):  
Idiopathic Thrombocytopenic Purpura ◽  
Direct Evidence ◽  
Fluorescent Antibody ◽  
Human Platelets ◽  
Antigenic Structure ◽  
Common Antigen ◽  
Thrombocytopenic Purpura ◽  
Morphologic Study ◽  
Idiopathic Thrombocytopenia ◽  
Immunocytochemical Studies

Abstract By means of the fluorescent antibody technic of Coons and Kaplan it was possible to demonstrate a common antigenic structure in human platelets and megakaryocytes, both in nonthrombocytopenic cases and in cases with idiopathic thrombocytopenic purpura. Direct evidence for a marked increase in the number of platelets in the spleens of two cases of idiopathic thrombocytopenia is given. The pathogenetic significance of this finding is discussed. It is concluded that the fluorescent antibody technic is a valuable tool for the chemical and morphologic study of platelets and megakaryocytes both in tissues and smears.

IMMUNOCHEMICAL IDENTIFICATION OF A THROMBOSPONDIN -LIKE ANTIGEN IN ARTERIAL THROMBOGENIC MICROFIBRILS

1987 ◽  
Author(s):  
F FAUVEL-LAFEVE ◽  
Y J LEGRAND
Keyword(s):  
Platelet Aggregation ◽  
Blood Platelets ◽  
Antigenic Structure ◽  
Second Step ◽  
Antigenic Determinants ◽  
Inhibit Platelet Aggregation ◽  
Type Vi Collagen ◽  
Immunochemical Identification ◽  
Similar Affinity ◽  
Fibronectin Type

The biochemical structure of arterial microfibrils (MFS) is unknown. Presently, the most probable hypothesis is that elastin associated MFS contain several antigenic determinants with MW varying between 31 and 200 KD.From our previous studies we know that MFS extracted by 6 M GuCl contain a major glycoprotein with a 128 KD MV (GP128). GP 128 is essential for the reactivity of MFS towards blood platelets but due tc the high insolubility of the extracted material it was not possible to isolate and study this GP 128. We have used immunoblotting to determine if MFS contain determinants recognized by antibodies against connective tissue glycoproteins such as fibronectin, type VI collagen or anti-platelet thrombospondin (TSP). 'The results showed that MFS do not contain fibronectin or type VI collagen but that anti-TSP IgG reacted with GP 128. Furthermore, the Fab fragments from anti-TSP IgG inhibited platelet aggregation induced by MFS but not by collagen or ADP . In a second step,to raise antibodies against GP 128, we prepared blots from entire MFS, the nitrocellulose band corresponding to GP 128 was cut, dissolved in DMSO, and wrs injected to rabbits. Such obtained antibodies recognized only GP 128 in arterial MFS and also TSP in a platelet lysate confirming that GP 128 and TSP have a common antigenic structure. IgG from anti-GP 128 inhibit platelet aggregation induced by MFS but not by collagen or ADP. Previously reported observations showed that tissue TSP and endothelial cells derived GP 128 have a similar affinity for chromatography supports and have the same effect on platelet-MFS interactions. All these results led us to propose that TSP, GP 128, and MFS recognize a common determinant on platelet membrane. This assumption would be strenghened if GP 128 indeed is derived from tissue TSP.

scholarly journals Recovery and Altered Neutralization Specificities of Chimeric Viruses Containing Capsid Protein Domain Exchanges from Antigenically Distinct Strains of Feline Calicivirus

2000 ◽  
Vol 74 (3) ◽  
pp. 1079-1084 ◽  
Author(s):  
John D. Neill ◽  
Stanislav V. Sosnovtsev ◽  
Kim Y. Green
Keyword(s):  
Capsid Protein ◽  
Antigenic Variation ◽  
Infectious Clone ◽  
Protein Domain ◽  
Antigenic Structure ◽  
Antigenic Determinants ◽  
Feline Calicivirus ◽  
Hyperimmune Serum ◽  
E Region ◽  
Chimeric Viruses

ABSTRACT Feline calicivirus (FCV) strains can show significant antigenic variation when tested for cross-reactivity with antisera produced against other FCV strains. Previous work has demonstrated the presence of hypervariable amino acid sequences in the capsid protein of FCV (designated regions C and E) that were postulated to constitute the major antigenic determinants of the virus. To examine the involvement of hypervariable sequences in determining the antigenic phenotype, the nucleotide sequences encoding the E regions from three antigenically distinct parental FCV strains (CFI, KCD, and NADC) were exchanged for the equivalent sequences in an FCV Urbana strain infectious cDNA clone. Two of the three constructs were recovered as viable, chimeric viruses. In six additional constructs, of which three were recovered as viable virus, the E region from the parental viruses was divided into left (N-terminal) and right (C-terminal) halves and engineered into the infectious clone. A final viable construct contained the C, D, and E regions of the NADC parental strain. Recovered chimeric viruses showed considerable antigenic variation from the parental viruses when tested against parental hyperimmune serum. No domain exchange was able to confer complete recognition by parental antiserum with the exception of the KCD E region exchange, which was neutralized at a near-homologous titer with KCD antiserum. These data demonstrate that it is possible to recover engineered chimeric FCV strains that possess altered antigenic characteristics. Furthermore, the E hypervariable region of the capsid protein appears to play a major role in the formation of the antigenic structure of the virion where conformational epitopes may be more important than linear in viral neutralization.

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