Characterization of the transcriptional initiation regions of genes for the major secreted protein antigens 85C and MPB51 ofMycobacterium bovisBCG

1997 ◽  
Vol 23 (5) ◽  
pp. 303-310 ◽  
Author(s):  
Naoya Ohara ◽  
Takeshi Nishiyama ◽  
Naoko Ohara-Wada ◽  
Sohkichi Matsumoto ◽  
Takemitsu Matsuo ◽  
...  
Keyword(s):  
Secreted Protein ◽  
Protein Antigens ◽  
Transcriptional Initiation

scholarly journals Immunological and functional characterization of Mycobacterium leprae protein antigens: an overview

1995 ◽  
Vol 18 (5) ◽  
pp. 791-800 ◽  
Author(s):  
Jelle E.R. Thole ◽  
Brigitte Wieles ◽  
Josephine E. Clark-Curtiss ◽  
Tom H.M. Ottenhoff ◽  
Tobias F. Rinke de Wit
Keyword(s):  
Functional Characterization ◽  
Mycobacterium Leprae ◽  
Protein Antigens

Characterization of allergen extracts by two-dimensional electrophoretic techniques: Micropolyspora faeni antigens.

1982 ◽  
Vol 28 (4) ◽  
pp. 993-997 ◽  
Author(s):  
O Vesterberg ◽  
K Holmberg
Keyword(s):  
Isoelectric Focusing ◽  
One Dimension ◽  
Protein Antigens ◽  
Thermophilic Actinomycetes ◽  
Saprobic Fungi ◽  
Increased Sensitivity ◽  
Electrophoretic Techniques ◽  
Protein Components ◽  
Allergen Extracts

Abstract Thermophilic actinomycetes and saprobic fungi are important in the etiology of allergic occupational diseases such as "farmer's lung" disease. Each such organism produces several protein antigens. Inhaled, these antigens stimulate production of antibodies. Detection of precipitating antibodies has been useful in the diagnosis of diseases so induced. Characterization of allergen extracts from microorganisms associated with these diseases is important, to improve the sensitivity and precision of the precipitin analysis. For this purpose we submitted crude allergen extracts to electrophoresis and isoelectric focusing in agarose gels. Staining the gels revealed many protein components in each extract, especially after isoelectric focusing. After separation in one dimension, a lane of gel was cut out and the proteins were electrophoresed at right angles into another gel, which contained antibodies. Several arcs of immunoprecipitates, indicating different antigens, were seen. This technique ("crossed immunoelectrofocusing") has earlier been used with polyacrylamide in the first dimension, but it is improved by using instead agarose of a special quality. Further to improve the quantification, we isolated pieces of gel containing the proteins of interest and used them as samples in zone immunoelectrophoresis assay. This method is straightforward, easy to evaluate, and about 100-fold as sensitive as radial immunodiffusion. The amount of protein in each sample is usually proportional to the distance from the upper gel surface to the front of each immunoprecipitate. The increased sensitivity allows study of many hitherto unexamined antigens.

scholarly journals BIOLOGICAL CHARACTERIZATION OF AN IMMUNOSUPPRESSANT FROM GROUP A STREPTOCOCCI

1971 ◽  
Vol 134 (5) ◽  
pp. 1253-1265 ◽  
Author(s):  
Artin H. Malakian ◽  
John H. Schwab
Keyword(s):  
Antibody Formation ◽  
Memory Cell ◽  
Primary Response ◽  
Repeated Injection ◽  
Group A Streptococci ◽  
Biological Characterization ◽  
Protein Antigens ◽  
Immunosuppressive Action ◽  
Group A

A component in extracts of Group A streptococci suppresses antibody formation in mice against heterologous erythrocyte and protein antigens. Large doses are not toxic and repeated injection does not change its effectiveness. It is most effective when injected 1 or 2 days before antigen and it is not suppressive when given after antigen. The active factor occurs as a large polydisperse complex and activity can be increased 10- to 25-fold by filtration through Sepharose 2B. Both direct (γM) and indirect (γG) antibody-forming cells are suppressed in primary and secondary responses. Injection before a primary response does not reduce memory cell development. It increases rather than depresses the "background" antibody-forming cells to sheep erythrocytes, and is equally effective if injected intraperitoneally or intravenously. Ribonuclease increases activity while deoxyribonuclease has no effect. Proteases destroy immunosuppressive action.

scholarly journals Characterization of Serogroup ANeisseria meningitidisfrom Invasive Meningococcal Disease Cases in Canada Between 1979 and 2006: Epidemiological Links to Returning Travellers

2008 ◽  
Vol 19 (3) ◽  
pp. 227-232 ◽  
Author(s):  
Angela M Sloan ◽  
Averil M Henderson ◽  
Raymond SW Tsang
Keyword(s):  
Meningococcal Disease ◽  
Clonal Complex ◽  
Disease Incidence ◽  
Developing Nations ◽  
Invasive Meningococcal Disease ◽  
Protein Antigens ◽  
Genes Encoding ◽  
Returning Travellers ◽  
The 1960S

INTRODUCTION: Serogroup ANeisseria meningitidishas repeatedly caused epidemics of invasive meningococcal disease (IMD) in developing nations since the 1960s. The present study is the first detailed study of serogroup A bacteria isolated in Canada.METHODS: Thirty-four serogroup A meningococcal isolates collected from individuals with IMD in Canada between 1979 and 2006 were characterized by serology and multilocus sequence typing of seven housekeeping enzyme genes and genes encoding three outer membrane protein antigens.RESULTS: Isolates were assigned to either the sequence type (ST)-1 or the ST-5 clonal complex. Clones within the ST-1 complex were recovered between 1979 and 1992, while clones of the ST-5 complex were isolated between 1987 and 2006; respectively, they accounted for 70.6% and 29.4% of all isolates studied. Isolates of the ST-1 complex were characterized by serosubtype antigen P1.3 or P1.3,6 with PorB allele 60 (serotype 4) and FetA sequence F5-1, while isolates of the ST-5 complex were characterized by serosubtype antigen P1.9 with PorB allele 47 (also serotype 4) and FetA sequence F3-1.CONCLUSIONS: The Canadian serogroup A IMD isolates likely originated in travellers returning from hyperendemic or epidemic areas of the globe where serogroup A bacteria circulate. Although the Canadian cases of serogroup A IMD were caused by clones known to have caused epidemics in developing countries, disease incidence remained low in Canada.

Characterization of Brucella canis protein antigens and polypeptide antibody responses of infected dogs

1989 ◽  
Vol 19 (4) ◽  
pp. 373-387 ◽  
Author(s):  
Leland E. Carmichael ◽  
Jean C. Joubert ◽  
Laura Jones
Keyword(s):  
Antibody Responses ◽  
Protein Antigens ◽  
Brucella Canis

scholarly journals Characterization of the yeast KEX1 gene product: a carboxypeptidase involved in processing secreted precursor proteins.

1989 ◽  
Vol 9 (6) ◽  
pp. 2706-2714 ◽  
Author(s):  
A Cooper ◽  
H Bussey
Keyword(s):  
Amino Acids ◽  
Gene Product ◽  
Killer Toxin ◽  
Secreted Protein ◽  
Serine Carboxypeptidase ◽  
Carboxypeptidase B ◽  
Basic Amino Acids ◽  
Precursor Proteins ◽  
In Cells

We have identified and partially characterized the Saccharomyces cerevisiae KEX1 gene product, Kex1p, to assess its role in processing secreted protein precursors. Anti-Kex1p antibodies identified a 113-kilodalton protein that was absent in cells in which the KEX1 gene has been disrupted and that was more abundant in cells overexpressing the KEX1 gene. Kex1p was found to be a membrane-associated glycoprotein with N-linked carbohydrate. The N-linked oligosaccharide(s) was modified in a progressive manner after synthesis, causing the glycoprotein to slowly increase in mass to 115 kilodaltons. After a Kex2p-mediated cleavage event at specific pairs of basic amino acids, alpha-factor and K1 killer toxin precursors have COOH-terminal dibasic residue extensions and require a carboxypeptidase B-like enzyme to process the precursors to maturity. A carboxypeptidase activity, with apparent specificity for basic amino acids, was detected in KEX1 cells. Disruption of the KEX1 gene abolished this activity, while overexpression of KEX1 increased it. Our results provide biochemical evidence consistent with earlier genetic work, that KEX1 encodes a serine carboxypeptidase involved in the processing of precursors to secreted mature proteins.

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