Induction of reaginic (IgE) gonococcal antibodies in the rat by a common antigen of Neisseria gonorrhoeae

1979 ◽  
Vol 25 (2) ◽  
pp. 138-145
Author(s):  
F. E. Ashton ◽  
H. M. Vijay ◽  
G. Lavergne ◽  
B. R. Brodeur ◽  
B. B. Diena
Keyword(s):  
Molecular Weight ◽  
Neisseria Gonorrhoeae ◽  
Cross Reactivity ◽  
Low Molecular Weight ◽  
Common Antigen ◽  
Rat Serum ◽  
Ige Antibody ◽  
Antigenic Activity ◽  
Diethylaminoethyl Cellulose ◽  
The Common

An antigen (ZAB) common to Neisseria gonorrhoeae was prepared by stepwise elution of a crude gonococcal antigen (ZA) from columns of diethylaminoethyl cellulose employing 0.02 M phosphate buffers, pH 7.6, containing increasing concentrations of sodium chloride. Rats immunized with ZAB produced reaginic (IgE) antibody which cross-reacted with ZA prepared from eight gonococcal strains by the passive cutaneous anaphylaxis (PCA) test. Heatingof the sera at 56 °C for 4 h destroyed the PCA activity. The PCA activity of the anti-ZAB rat serum was removed after absorption with ZAB antigen or with rabbit anti-rat IgE but not after absorption with gonococcal lipopolysaccharide or with heat-killed or formalinized gonococci. Treatment of ZAB with trypsin or heating at 100 °C for 30 min destroyed or reduced the antigenic activity respectively. Further purification of ZAB by filtration through Sephadex G-100 gave a preparation (ZAB2) which contained the common antigen as shown by the cross-reactivity of anti-ZAB2 rat serum with seven strains of N. gonorrhoeae. Fraction ZAB2 contained material which had a molecular weight less than 13 700 and was associated with the presence of material absorbing at 260 nm. The results of this study indicate that a low molecular weight antigen, which appears to be protein in nature and associated with nucleic acid, is common to the gonococcus and is the main antigenic component inducing reaginic (IgE) antibody in the rat.

scholarly journals Novel Role for Albumin in Innate Immunity: Serum Albumin Inhibits the Growth of Blastomyces dermatitidis Yeast Form In Vitro

2003 ◽  
Vol 71 (11) ◽  
pp. 6648-6652 ◽  
Author(s):  
Steven Giles ◽  
Charles Czuprynski
Keyword(s):  
Molecular Weight ◽  
Inhibitory Activity ◽  
Mammalian Species ◽  
Blastomyces Dermatitidis ◽  
Low Molecular Weight ◽  
Rat Serum ◽  
Yeast Form ◽  
Domain Iii

ABSTRACT In this study we found that serum inhibitory activity against Blastomyces dermatitidis was principally mediated by albumin. This was confirmed in experiments using albumin from several mammalian species. Analbuminemic rat serum did not inhibit B. dermatitidis growth in vivo; however, the addition of albumin restored inhibitory activity. Inhibitory activity does not require albumin domain III and appears to involve binding of a low-molecular-weight yeast-derived growth factor.

scholarly journals Serological grouping ofTreponema hyodysenteriae

1990 ◽  
Vol 105 (1) ◽  
pp. 79-85 ◽  
Author(s):  
D. J. Hampson ◽  
J. R. L. Mhoma ◽  
B. G. Combs ◽  
J. I. Lee
Keyword(s):  
Molecular Weight ◽  
Gel Electrophoresis ◽  
Vaccine Development ◽  
Polyacrylamide Gel Electrophoresis ◽  
Cross Reactivity ◽  
Low Molecular Weight ◽  
Serological Response ◽  
Double Immunodiffusion ◽  
Sds Page ◽  
Treponema Hyodysenteriae

SUMMARYTwo Australian isolates ofTreponema hyodysenteriaewhich did not fit within the current serological grouping system for these bacteria wrere examined by agarose gel double immunodiffusion tests (AGDP). Isolate Vic1 was serologically unique, and we propose that it becomes the type organism for a new sixth serological group ofT. hyodysenteriae(Group F). Isolate Q1 was unusual in that lipopolysaccharide (LPS) extracted from it reacted strongly in AGDP with serum raised against the type organism for serogroup D (A1), and also weakly with serum raised against the type organism for serogroup B (WA1). The nature of this cross-reactivity was examined by using cross-absorbed antisera in AGDP, and by SDS-polyacrylamide gel electrophoresis (SDS-PAGE) and Western blot analysis.The pattern of serological cross-reactivity between Q1, A1 and WA1 was complex and was not fully defined, but the isolate Q1 apparently shared low molecular weight ‘serogroup’ LPS antigens with A1, and shared higher molecular weight LPS antigens with WA1. On this basis Q1 was designated as belonging to serogroup D, although it was recommended that this be qualified as D (B) to indicate the presence of weak cross-reactivity with serogroup B. Such serological cross-reactivity may have significance in relation to the development of immunity toT. hyodysenteriae. Isolate Q1 may be a potentially useful organism for vaccine development because of its ability to induce a good serological response to LPS of treponemes from both serogroups D and B.

scholarly journals Rectus Sheath Haematoma Associated with Low Molecular Weight Heparin: A Case Series

2007 ◽  
Vol 89 (3) ◽  
pp. 309-312 ◽  
Author(s):  
J Donaldson ◽  
CH Knowles ◽  
SK Clark ◽  
I Renfrew ◽  
MD Lobo
Keyword(s):  
Molecular Weight ◽  
Low Molecular Weight Heparin ◽  
Case Series ◽  
Rectus Sheath ◽  
Low Molecular Weight ◽  
Recent Treatment ◽  
Life Threatening ◽  
Benign Nature ◽  
The Common

A report of three cases of spontaneous rectus sheath haematoma within a 1-month period in a single hospital. The common feature was the recent treatment with low molecular weight heparin. In contrast to the perceived benign nature of the classically-described haematoma, the cases described were life-threatening and required aggressive intervention.

Heparin-induced Thrombocytopenia: IgG Binding to PF4-Heparin Complexes in the Fluid Phase and Cross-reactivity with Low Molecular Weight Heparin and Heparinoid

1998 ◽  
Vol 80 (08) ◽  
pp. 292-297 ◽  
Author(s):  
Peter Newman ◽  
Rebecca Swanson ◽  
Beng Chong
Keyword(s):  
Molecular Weight ◽  
Fluid Phase ◽  
Cross Reactivity ◽  
Low Molecular Weight ◽  
Absolute Contraindication ◽  
Low Molecular Weight Heparins ◽  
Heparin Induced Thrombocytopenia ◽  
Igg Binding ◽  
Heparin Complexes ◽  
Low Levels

SummaryEarly diagnosis of heparin-induced thrombocytopenia (HIT) is essential to reduce morbidity and mortality. We report an enzyme immunoassay which detects the binding of HIT IgG to PF4-heparin in the fluid phase. Our fluid phase assay produces consistently low background and can detect low levels of anti-PF4-heparin. It is suited to testing alternative anticoagulants because, unlike in an ELISA, a clearly defined amount of antigen is available for antibody binding. We were able to detect anti-PF4-heparin IgG in 26/28 (93%) HIT patients. We investigated cross-reactivity of anti-PF4-heparin antibodies with PF4 complexed to alternative heparin-like anticoagulants. Low molecular weight heparins cross-reacted with 23/26 (88%) of the sera from HIT patients while half of the HIT sera weakly cross-reacted with PF4-danaparoid (Orgaran). The thrombocytopenia and thrombosis of most of these patients resolved during danaparoid therapy, indicating that detection of low affinity antibodies to PF4-danaparoid by immunoassay may not be an absolute contraindication for danaparoid administration.

A low molecular weight peptide from snow mold with epitopic homology to the winter flounder antifreeze protein

1994 ◽  
Vol 72 (3-4) ◽  
pp. 152-156 ◽  
Author(s):  
W. Jay Newsted ◽  
Sandra Polvi ◽  
Bob Papish ◽  
Ed Kendall ◽  
Mohammed Saleem ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Antifreeze Protein ◽  
Cross Reactivity ◽  
Winter Flounder ◽  
Low Molecular Weight ◽  
Culture Temperature ◽  
Snow Mold ◽  
Typhula Incarnata ◽  
Magnetic Resonance Microimaging ◽  
Nuclear Magnetic Resonance Microimaging

Evidence for a small size protein (ca. 3500 kDa) exhibiting epitopic homology to the Atlantic winter flounder antifreeze protein (AFP) is found in the snow molds Coprinus psychromorbidus, Myriosclerotinia borealis, and Typhula incarnata. The protein shows strong cross-reactivity with antisera specific for the flounder AFP. Preliminary studies suggest that the protein is synthesized in response to lowering the culture temperature, and that it is membrane associated and, therefore, may function in an analogous capacity to the fish AFP. Also, the protein is shown to have antifreeze properties as determined by nuclear magnetic resonance microimaging experiments.Key words: antifreeze proteins, low temperature stress, snow mold, winter flounder.

The lipopolysaccharide (R type) as a common antigen of Neisseria gonorrhoeae. II. Use of hen antiserum to gonococcal lipopolysaccharide in a rapid slide test for the identification of N. gonorrhoeae from primary isolates and secondary cultures

1978 ◽  
Vol 24 (2) ◽  
pp. 124-128 ◽  
Author(s):  
R. Wallace ◽  
F. E. Ashton ◽  
A. Ryan ◽  
B. B. Diena ◽  
C. Malysheff ◽  
...  
Keyword(s):  
Neisseria Gonorrhoeae ◽  
Rapid Identification ◽  
Cross Reactivity ◽  
Agglutination Test ◽  
Common Antigen ◽  
Colony Type ◽  
Neisseria Lactamica ◽  
Slide Agglutination Test ◽  
Slide Test ◽  
Branhamella Catarrhalis

An antiserum has been prepared in hens to R-type gonococcal lipopolysaccharide (LPS) and used in a simple slide-agglutination test for the identification of Neisseria gonorrhoeae. Anti-LPS serum agglutinated gonococcal cells representative of the four colony types of N. gonorrhoeae. Absorption of the antiserum with LPS removed the agglutinating activity. Secondary cultures (1120) were tested without observation of the colony type and all were agglutinated. No agglutination occurred with strains of Neisseria meningitidis, Neisseria lactamica, non-pathogenic Neisseria, Pseudomonas aeruginosa, Branhamella catarrhalis, or with species of lactobacilli and Acinetobacter. Cross-reactivity of the antiserum occurred with some streptococci. The anti-LPS serum was used to identify N. gonorrhoeae in primary isolates from the cervix, urethra, and pharynx. Of 251 gonococcal isolates tested, 249 were agglutinated by the antiserum, while all of the corresponding secondary cultures were agglutinated. The antiserum did not agglutinate N. meningitidis found in primary isolates from pharyngeal specimens. Anti-LPS hen serum should be useful for the rapid identification of N. gonorrhoeae in primary isolates or secondary cultures.

Hypersensitivity reactions to low molecular weight heparins: different patterns of cross-reactivity in 3 patients

2018 ◽  
Vol 96 (4) ◽  
pp. 428-432 ◽  
Author(s):  
Danica Juricic Nahal ◽  
Ivana Cegec ◽  
Viktorija Erdeljic Turk ◽  
Ksenija Makar Ausperger ◽  
Iva Kraljickovic ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Challenge Test ◽  
Cross Reactivity ◽  
Skin Tests ◽  
Delayed Type Hypersensitivity ◽  
Low Molecular Weight ◽  
Hypersensitivity Reactions ◽  
Low Molecular Weight Heparins ◽  
Safe Alternative ◽  
Delayed Reactions

Low molecular weight heparins (LMWHs) are used for a variety of indications. The most common type of hypersensitivity reactions to LMWHs are delayed-type hypersensitivity reactions (DHR). Immediate-type hypersensitivity reactions (IHR) occur only sporadically. Cross-reactivity of different LMWHs is a common and unpredictable problem. We present 2 cases of patients who developed DHR to nadroparin and enoxaparin, respectively. The third case presents a patient who developed IHR to nadroparin. Skin tests confirmed the hypersensitivity in all cases. In the cases of DHR, a skin test negative LMWH was identified and was tolerated in a challenge test. In the IHR case, cross-reactivity to all tested LMWHs was established. We hypothesize that the degree of cross-reactivity might depend on the type of hypersensitivity reaction with immediate reactions linked to more extensive cross-reactivity than delayed reactions. This is important to consider because, at least in some cases, a safe alternative LMWH can be identified.

Heparin-Induced Thrombocytopenia (HIT): An Overview of 230 Patients Treated with Orgaran (Org 10172)

1993 ◽  
Vol 70 (04) ◽  
pp. 554-561 ◽  
Author(s):  
H N Magnani
Keyword(s):  
Molecular Weight ◽  
Oral Anticoagulants ◽  
Cross Reactivity ◽  
Low Molecular Weight ◽  
Heparin Induced Thrombocytopenia ◽  
Antithrombotic Activity ◽  
Valuable Alternative ◽  
Alternative Anticoagulation ◽  
Prostacyclin Analogues ◽  
Venous Thromboses

SummaryHeparin-induced thrombocytopenia (HIT) with thrombosis occurs in about 1 in 2,000 heparin-treated patients. The arterial or venous thromboses may threaten life and limb hence alternative anticoagulation is needed. Some alternative treatments are possible i.e. LMWH, Ancrod, prostacyclin analogues, Dextran, aspirin and oral anticoagulants, but each has its drawbacks. This report reviews treatment of HIT patients with Orgaran (Org 10172), a low molecular weight heparinoid.Because of its proven antithrombotic activity Orgaran was used to treat 230 HIT patients. One hundred and fifty, nine patients presented with at least one thrombotic problem, which in 88 was due to the heparin use. 92.8% of the patients were considered to have adequately responded to Orgaran during the treatment period. Fifty-nine deaths (25.7%) occurred of which 7 (3.0%) were attributed to Orgaran use. The remaining 52 deaths, 27 of which occurred after Orgaran treatment was successfully terminated, were due to the severe underlying disorders in these patients. These results and the lower cross-reactivity rate (≈10%) with the heparin-induced antibody compared with that of the LMWH (>90%) suggest that although problems remain, Orgaran can be a valuable alternative treatment for patients who suffer from HIT and who require anticoagulation.

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