Microparticulate Formulation for a Pneumococcal Capsular Polysaccharide Antigen

2015 ◽  
pp. 115-126
Author(s):  
Bernadette D'Souza ◽  
Prathap Shastri ◽  
Gabrielle Hammons ◽  
Lakshmi Kolluru ◽  
Nihal Mulla ◽  
...  
Keyword(s):  
Capsular Polysaccharide ◽  
Polysaccharide Antigen

scholarly journals Whole-Genome Sequences of Two Salmonella enterica Serovar Dublin Strains That Harbor the viaA, viaB, and ompB Loci of the Vi Antigen

2019 ◽  
Vol 8 (14) ◽  
Author(s):  
Manal Mohammed ◽  
Marie-Leone Vignaud ◽  
Sabrina Cadel-Six
Keyword(s):  
Salmonella Enterica ◽  
Capsular Polysaccharide ◽  
Raw Milk ◽  
Genome Sequences ◽  
Polysaccharide Antigen ◽  
Content Type ◽  
Vi Capsular Polysaccharide ◽  
Raw Milk Cheese ◽  
Salmonella Enterica Serovar Dublin ◽  
Vi Antigen

Here, we report the genome sequences of two Salmonella enterica serovar Dublin strains, 03EB8736SAL and 03EB8994SAL, isolated from raw-milk cheese and milk filtrate, respectively. Analysis of the draft genomes of the two isolates reveals the presence of the viaA, viaB, and ompB loci of the Vi capsular polysaccharide antigen (Vi antigen).

scholarly journals Chromatographically purified Vi-capsular polysaccharide antigen for vaccination against Typhoid fever

1998 ◽  
pp. 240
Author(s):  
I.V. Ankudinov ◽  
M.E. Golovina ◽  
V.L. L'vov ◽  
N.P. Vaneeva ◽  
I.C. Verner ◽  
...  
Keyword(s):  
Typhoid Fever ◽  
Capsular Polysaccharide ◽  
Polysaccharide Antigen ◽  
Vi Capsular Polysaccharide

Structural determination of the group K capsular polysaccharide of Neisseriameningitidis: a 2D-NMR analysis

1985 ◽  
Vol 63 (10) ◽  
pp. 2781-2786 ◽  
Author(s):  
Francis Michon ◽  
Jean Robert Brisson ◽  
René Roy ◽  
Harold J. Jennings ◽  
Fraser E. Ashton
Keyword(s):  
Capsular Polysaccharide ◽  
2D Nmr ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Electronic Effects ◽  
Nmr Studies ◽  
Polysaccharide Antigen ◽  
One Dimensional ◽  
The One

The capsular polysaccharide antigen of Neisseriameningitidis group K was isolated by Cetavlon precipitation and purified by ion-exchange chromatography. The structure of the K polysaccharide was determined to a large extent by comprehensive proton and carbon-13 nuclear magnetic resonance (nmr) studies. In these studies one-dimensional and two-dimensional experiments were carried out directly on the K polysaccharide. The K polysaccharide is composed of the following repeating unit: -4)β-D-ManpNAcA(1→3) [4-OAc]β-D-ManpNAcA(1→. Except for the one-bond couplings between their anomeric carbons and protons [Formula: see text], all the nmr spectroscopic evidence was consistent with both 2-acetamido-2-deoxy-D-mannopyranosyluronic acid residues adopting the 4C1 (D) conformation and having the β-D-configuration. This ambiguity in [Formula: see text] is probably due to through-space electronic effects generated by the presence of contiguous carboxylated sugar residues in the K polysaccharide. The O-acetyl substituents of the K polysaccharide are essential for its antigenicity to group K polysaccharide-specific antibodies.

scholarly journals STUDIES ON A NON-HEMOLYTIC STREPTOCOCCUS ISOLATED FROM THE RESPIRATORY TRACT OF HUMAN BEINGS

1944 ◽  
Vol 80 (5) ◽  
pp. 431-440 ◽  
Author(s):  
George S. Mirick ◽  
Lewis Thomas ◽  
Edward C. Curnen ◽  
Frank L. Horsfall
Keyword(s):  
Respiratory Tract ◽  
Capsular Polysaccharide ◽  
Type I ◽  
Capsular Polysaccharides ◽  
Human Beings ◽  
Streptococcus Salivarius ◽  
Polysaccharide Antigen ◽  
Hemolytic Streptococcus ◽  
Immunological Relationship

The results of studies on the immunological relationship between streptococcus MG and Streptococcus salivarius type I are described. Evidence is presented to show that Streptococcus salivarius type I, like streptococcus MG, possesses a capsular polysaccharide antigen. Similarities in the capsular polysaccharides of these two different species of non-hemolytic streptococci appear to be responsible for their immunological relationship.

Alterations in serum opsonic activity and complement levels in pneumococcal disease

1980 ◽  
Vol 29 (3) ◽  
pp. 1062-1066
Author(s):  
G S Giebink ◽  
T H Dee ◽  
Y Kim ◽  
P G Quie
Keyword(s):  
Host Defense ◽  
Complement Activation ◽  
Pneumococcal Disease ◽  
Capsular Polysaccharide ◽  
Defense Mechanism ◽  
Polysaccharide Antigen ◽  
Opsonic Activity ◽  
Factor B ◽  
Host Defense Mechanism ◽  
Important Host

Pneumococcal opsonic activity and concentrations of pneumococcal capsular polysaccharide antigen, C3, C4 factor B, C3 and factor B breakdown products were measured in the serum obtained acutely from 12 patients with serious pneumococcal disease. One patient showed markedly reduced pneumococcal opsonic activity, borderline-low C3, and the presence of C3 and factor B breakdown products and died. Although eight additional patients showed depressed levels of C3 or C4 or the presence of C3 or factor B breakdown products, none had reduced pneumococcal opsonic activity. All of the three remaining patients had normal opsonic activity and C3 and C4 levels. Covalescent serum was obtained from eight patients; six had normal C3 and C4 levels, and two had persistent C4 depression. These data show that complement is activated during pneumococcal disease and suggest that extensive complement activation may impair pneumococcal opsonic activity in certain patients and thereby compromise an important host defense mechanism.

scholarly journals THE EFFECT OF THE BACTERIOLYTIC ENZYME OF PNEUMOCOCCUS UPON THE ANTIGENICITY OF ENCAPSULATED PNEUMOCOCCI

1937 ◽  
Vol 66 (1) ◽  
pp. 113-123 ◽  
Author(s):  
René J. Dubos
Keyword(s):  
Capsular Polysaccharide ◽  
Specific Resistance ◽  
Bacterial Species ◽  
Antigenic Property ◽  
Type I ◽  
Subsequent Infection ◽  
Polysaccharide Antigen ◽  
Bacteriolytic Enzyme ◽  
Active Immunity ◽  
Specific Polysaccharide

1. Mice immunized with heat-killed cells of virulent pneumococci (Type I) which have been treated with active preparations of the bacteriolytic enzyme, develop a certain degree of type specific resistance to subsequent infection. This active immunity, however, appears to be due to the small amount of free acetyl polysaccharide present in the suspension of digested bacteria, and is always of a less pronounced degree than that obtained with intact heat-killed cells. 2. Virulent pneumococci killed by heat or iodine when subjected to the action of active preparations of the bacteriolytic enzyme lose the antigenic property of stimulating in rabbits the formation of precipitating antibodies for the type specific polysaccharide. 3. The enzyme prepared from S or R pneumococci, irrespective of type derivation, is equally effective against the capsular polysaccharide antigen of any specific type of this bacterial species. 4. The inactivation of the capsular polysaccharide antigen is observed when the cells are merely rendered Gram-negative, without being caused to undergo actual disintegration or lysis. 5. These observations emphasize the importance of minimizing the chances of alterations due to the action of cellular enzymes in the course of preparation of the cell suspension to be used as immunizing agents.

Antibody immunity andCryptococcus neoformans

1995 ◽  
Vol 73 (S1) ◽  
pp. 1180-1186 ◽  
Author(s):  
Arturo Casadevall
Keyword(s):  
Cryptococcus Neoformans ◽  
Capsular Polysaccharide ◽  
Cell Function ◽  
Protein Vaccine ◽  
Polysaccharide Antigen ◽  
Chimeric Antibodies ◽  
Protective Antibodies ◽  
Human Infections

Recently there has been renewed interest in the potential of antibody immunity for the prevention and therapy of human Cryptococcus neoformans infections. Historically, the role of antibody immunity in protection against C. neoformans has been controversial. Experiments with polyclonal sera have produced evidence for and against the importance of antibody immunity in host defence. However, three groups have now shown that administration of monoclonal antibody (mAb) to the C. neoformans capsular polysaccharide (CPS) can modify the course of infection in mice. The quantity, isotype, and specificity of mAb appear to be important parameters of antibody efficacy against C. neoformans. Protective and nonprotective mAbs to CPS have been identified, suggesting a possible explanation for the divergent results obtained with polyclonal preparations, which presumably contain both types of antibodies. mAb administration has been shown to prolong survival, decrease organ fungal burden, and reduce serum polysaccharide antigen. The mechanism(s) by which mAb modify the course of infection is uncertain. In vitro experiments strongly suggest that antibodies mediate protection by enhancing effector cell function. The combination of antibody and amphotericin B is more effective than either agent alone for the treatment of murine cryptococcosis. Human–mouse chimeric antibodies with activity against C. neoformans have been constructed that may have advantages over mouse mAbs for therapy of human infections. A highly immunogenic capsular polysaccharide–protein vaccine has been made that can elicit protective antibodies in mice. Antibody immunity can modify the course of infection to the benefit of the host and may be useful in the prevention and treatment of human cryptococcosis. Key words: antibody, Cryptococcus neoformans, macrophage, vaccine, AIDS.

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