A structural study of the capsular antigen of Klebsiella serotype K43
- Authors: Aereboe, Michael
- Date: 1993
- Subjects: Polysaccharides , Klebsiella , Antigens , Enterobacteriaceae
- Language: English
- Type: Thesis , Masters , MSc
- Identifier: vital:3740 , http://hdl.handle.net/10962/d1003218 , Polysaccharides , Klebsiella , Antigens , Enterobacteriaceae
- Description: This thesis presents a detailed chemical and spectroscopic determination of the capsular, polysaccharide K-antigen isolated from the Klebsiella bacterium, serotype K43 (culture #2482). The repeating unit of the capsular polysaccharide was found to be of the "3 + 2" repeating unit type. A uronic acid was found as part of a disaccharide side chain and the main chain of the polysaccharide was found to be composed of a neutral trisaccharide of mannose and galactose. The work forms part of an ongoing research interest in bacterial polysaccharides of this laboratory and now completes the structural elucidation of all the Klebsiella K-antigens, bar three antigens which were originally assigned to other laboratories. These data together with the respective serological characteristics of each serotype are available to the molecular biologist, and may result in the production of: vaccine(s) against Klebsiella infections, diagnostic products and novel carrier molecules enabling targeted drug delivery.
- Full Text:
- Authors: Aereboe, Michael
- Date: 1993
- Subjects: Polysaccharides , Klebsiella , Antigens , Enterobacteriaceae
- Language: English
- Type: Thesis , Masters , MSc
- Identifier: vital:3740 , http://hdl.handle.net/10962/d1003218 , Polysaccharides , Klebsiella , Antigens , Enterobacteriaceae
- Description: This thesis presents a detailed chemical and spectroscopic determination of the capsular, polysaccharide K-antigen isolated from the Klebsiella bacterium, serotype K43 (culture #2482). The repeating unit of the capsular polysaccharide was found to be of the "3 + 2" repeating unit type. A uronic acid was found as part of a disaccharide side chain and the main chain of the polysaccharide was found to be composed of a neutral trisaccharide of mannose and galactose. The work forms part of an ongoing research interest in bacterial polysaccharides of this laboratory and now completes the structural elucidation of all the Klebsiella K-antigens, bar three antigens which were originally assigned to other laboratories. These data together with the respective serological characteristics of each serotype are available to the molecular biologist, and may result in the production of: vaccine(s) against Klebsiella infections, diagnostic products and novel carrier molecules enabling targeted drug delivery.
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Structural analysis of some Escherichia coli capsular antigens
- Authors: Hackland, Peter Linton
- Date: 1992
- Subjects: Antigens , Enterobacteriaceae , Escherichia
- Language: English
- Type: Thesis , Doctoral , PhD
- Identifier: vital:3758 , http://hdl.handle.net/10962/d1003236 , Antigens , Enterobacteriaceae , Escherichia
- Description: The work presented in this thesis forms part of a collaborative effort to determine the chemical structures of the surface antigens of bacteria which belong to the Enterobacteriaceae. These antigens are largely polysaccharides and occur as lipopolysaccharides and capsular polysaccharides which give rise to the somatic or 0 antigens and the capsular or K antigens, respectively. In recent years interest has mostly been focused on the extracellular polysaccharide antigens expressed by the genus Escherichia coli because of the effect they exert on normal immunological processes and their structural relatedness to the surface antigens of other more pathogenic bacteria. Therefore the molecular structures of the capsular polysaccharides (Kantigens)produced by E. coli 09:K35(AI04a) and 09:K38(A262a) have been determined by novel enzymic, chemical and spectroscopic procedures. These investigations show that the structures of these polysaccharides can be determined by a combination of chemical and spectroscopic procedures , or almost entirely by n.m.r. spectroscopy alone. The in vitro bacteriophage mediated depolymerisation of the native E. coli K35 polysaccharide demonstrates the value of this method for the isolation of oligosaccharides representing the repeating- unit and multiples thereof. Finally E. coli K37 and K38 capsular polysaccharides were used as model compounds for the evaluation of partial and selective reductive cleavage as methods of generating oligosaccharide for further structural analysis. The products of these reactions were analysed largely by a combination of mass spectrometric procedures.
- Full Text:
- Authors: Hackland, Peter Linton
- Date: 1992
- Subjects: Antigens , Enterobacteriaceae , Escherichia
- Language: English
- Type: Thesis , Doctoral , PhD
- Identifier: vital:3758 , http://hdl.handle.net/10962/d1003236 , Antigens , Enterobacteriaceae , Escherichia
- Description: The work presented in this thesis forms part of a collaborative effort to determine the chemical structures of the surface antigens of bacteria which belong to the Enterobacteriaceae. These antigens are largely polysaccharides and occur as lipopolysaccharides and capsular polysaccharides which give rise to the somatic or 0 antigens and the capsular or K antigens, respectively. In recent years interest has mostly been focused on the extracellular polysaccharide antigens expressed by the genus Escherichia coli because of the effect they exert on normal immunological processes and their structural relatedness to the surface antigens of other more pathogenic bacteria. Therefore the molecular structures of the capsular polysaccharides (Kantigens)produced by E. coli 09:K35(AI04a) and 09:K38(A262a) have been determined by novel enzymic, chemical and spectroscopic procedures. These investigations show that the structures of these polysaccharides can be determined by a combination of chemical and spectroscopic procedures , or almost entirely by n.m.r. spectroscopy alone. The in vitro bacteriophage mediated depolymerisation of the native E. coli K35 polysaccharide demonstrates the value of this method for the isolation of oligosaccharides representing the repeating- unit and multiples thereof. Finally E. coli K37 and K38 capsular polysaccharides were used as model compounds for the evaluation of partial and selective reductive cleavage as methods of generating oligosaccharide for further structural analysis. The products of these reactions were analysed largely by a combination of mass spectrometric procedures.
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A structural study of the capsular antigens of escherichia coli K36 and klebiella K68
- Authors: Stanley, Shawn Mark Ross
- Date: 1987 , 2013-03-11
- Subjects: Enterobacteriaceae , Klebsiella , Escherichia , Antigens
- Language: English
- Type: Thesis , Masters , MSc
- Identifier: vital:3814 , http://hdl.handle.net/10962/d1004613 , Enterobacteriaceae , Klebsiella , Escherichia , Antigens
- Description: From Introduction: Bacterial cells all have a cytoplasmic membrane (see Figure 1) which regulates the movement of ions and molecules into and out of the bacterium. Enclosing this membrane is a cell wall of which there are two general types, which are differentiated by the Gram stain(02) as being either gram positive or gram negative (depending upon whether they hold the gram stain after washing with ethanol). The cell wall provides the cell with shape and rigidity and is composed, in the case of gram positive types, of peptidoglycan, and in the case of gram negative bacteria, of a peptidoglycan and an outer membrane (see Figure 2). The peptidoglycan layer, common to both cell wall types, consists of a backbone of alternating units of N-acetylglucosamine and N-acetylmuramic acid to which peptides are attached by amide links. This heteropolymer is a highly cross linked mosaic and this gives it strength and rigidity. In gram positive bacteria, this layer also contains two carbohydr ate antigens, a simple polysaccharide and a teichoic acid; these are usually the type specific or major group antigens of the bacterium. Many of the bacteria also produce exopolysaccharides (see Figure 3) either as discrete capsules (for example, the Enterobacteriaceae K antigens) or unattached slime layers (for example, the Enterobacteriaceae M antigens). The vast majority of these polysaccharides are heteroglycans(03) composed of contiguous oligosaccharide repeating units. Their monosaccharide components are largely neutral hexoses, 6-deoxy hexoses and also amino sugars. (03) Pentose units are rare. (03) The capsular polysaccharides usually have a high content of acidic constituents such as uronic acids, phosphate groups, or pyruvate ketals. (01) , KMBT_363 , Adobe Acrobat 9.53 Paper Capture Plug-in
- Full Text:
- Authors: Stanley, Shawn Mark Ross
- Date: 1987 , 2013-03-11
- Subjects: Enterobacteriaceae , Klebsiella , Escherichia , Antigens
- Language: English
- Type: Thesis , Masters , MSc
- Identifier: vital:3814 , http://hdl.handle.net/10962/d1004613 , Enterobacteriaceae , Klebsiella , Escherichia , Antigens
- Description: From Introduction: Bacterial cells all have a cytoplasmic membrane (see Figure 1) which regulates the movement of ions and molecules into and out of the bacterium. Enclosing this membrane is a cell wall of which there are two general types, which are differentiated by the Gram stain(02) as being either gram positive or gram negative (depending upon whether they hold the gram stain after washing with ethanol). The cell wall provides the cell with shape and rigidity and is composed, in the case of gram positive types, of peptidoglycan, and in the case of gram negative bacteria, of a peptidoglycan and an outer membrane (see Figure 2). The peptidoglycan layer, common to both cell wall types, consists of a backbone of alternating units of N-acetylglucosamine and N-acetylmuramic acid to which peptides are attached by amide links. This heteropolymer is a highly cross linked mosaic and this gives it strength and rigidity. In gram positive bacteria, this layer also contains two carbohydr ate antigens, a simple polysaccharide and a teichoic acid; these are usually the type specific or major group antigens of the bacterium. Many of the bacteria also produce exopolysaccharides (see Figure 3) either as discrete capsules (for example, the Enterobacteriaceae K antigens) or unattached slime layers (for example, the Enterobacteriaceae M antigens). The vast majority of these polysaccharides are heteroglycans(03) composed of contiguous oligosaccharide repeating units. Their monosaccharide components are largely neutral hexoses, 6-deoxy hexoses and also amino sugars. (03) Pentose units are rare. (03) The capsular polysaccharides usually have a high content of acidic constituents such as uronic acids, phosphate groups, or pyruvate ketals. (01) , KMBT_363 , Adobe Acrobat 9.53 Paper Capture Plug-in
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The structural elucidation of the capsular antigen of klebsiella serotype k69
- Authors: Hackland, Peter Linton
- Date: 1987
- Subjects: Antigens , Klebsiella
- Language: English
- Type: Thesis , Masters , MSc
- Identifier: vital:3816 , http://hdl.handle.net/10962/d1004901 , Antigens , Klebsiella
- Full Text:
- Authors: Hackland, Peter Linton
- Date: 1987
- Subjects: Antigens , Klebsiella
- Language: English
- Type: Thesis , Masters , MSc
- Identifier: vital:3816 , http://hdl.handle.net/10962/d1004901 , Antigens , Klebsiella
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A novel adjuvant : polymerised serum albumin beads
- Authors: Dewar, John Barr
- Date: 1985
- Subjects: Antigens , Serum albumin
- Language: English
- Type: Thesis , Masters , MSc
- Identifier: vital:4104 , http://hdl.handle.net/10962/d1011146 , Antigens , Serum albumin
- Description: Lee, T. et al (1981) proposed the encapsulation of hormones such as progesterone into serum albumin beads, such that their in vivo proteolysis would allow a gradual release of hormone at low levels, for extended hormone action. It was proposed, in the Department of Microbiology, Rhodes University, to replace the hormone component of the above bead formulation, with virus as antigen, in the development of a vaccine. Beads optimally crosslinked at 1% final glutaraldehyde concentration, containing Nodamura virus, were shown to promote an adjuvant effect in vivo, analogous to the release of antigen from Freund's Complete Adjuvant (FCA), so that extended immunostimulation resulted. It was shown that soluble antigen promoted a short-lived primary immune response, peaking around day 25 following inoculation. Antigen presented in beads, on the other hand, initially elicited a low humoral response, but this response gradually increased up to a peak around day 110 post inoculation, before decreasing. No apparent adverse side-effects were noted following inoculation of antigen-containing serum albumin beads, compared to necrosis following antigen in FCA inoculation, supporting the proposal of using albumin homotypic for the test inoculee animal, so that the beads would themselves be non-immunogenic and would merely act as a vehicle in the vaccine formulation. The indirect enzyme-linked immunosorbent assay (ELISA) was used to monitor the humoral response to antigen following inoculation. Results showed that covalent crosslinking of albumin in the formation of the beads did not promote immunogenicity on the part of the chemically altered albumin. The ELISA test was used to indicate the kinetics of the IgG response to Nodamura virus when presented in formulations such as: Freely soluble virus or its subunit; soluble intact virus inactivated by treatment with glutaraldehyde; intact virus entrapped in serum albumin beads cross; linked at different percentage final glutaraldehyde concentrations and also virus subunit prepared in albumin beads. The presence of virus-neutral ising antibodies was noted in serum obtained from rabbits inoculated with virus entrapped in albumin beads. Virus infectivity, titrated in mice, showed protection against virus challenge after incubation of virus with serum obtained above.
- Full Text:
- Authors: Dewar, John Barr
- Date: 1985
- Subjects: Antigens , Serum albumin
- Language: English
- Type: Thesis , Masters , MSc
- Identifier: vital:4104 , http://hdl.handle.net/10962/d1011146 , Antigens , Serum albumin
- Description: Lee, T. et al (1981) proposed the encapsulation of hormones such as progesterone into serum albumin beads, such that their in vivo proteolysis would allow a gradual release of hormone at low levels, for extended hormone action. It was proposed, in the Department of Microbiology, Rhodes University, to replace the hormone component of the above bead formulation, with virus as antigen, in the development of a vaccine. Beads optimally crosslinked at 1% final glutaraldehyde concentration, containing Nodamura virus, were shown to promote an adjuvant effect in vivo, analogous to the release of antigen from Freund's Complete Adjuvant (FCA), so that extended immunostimulation resulted. It was shown that soluble antigen promoted a short-lived primary immune response, peaking around day 25 following inoculation. Antigen presented in beads, on the other hand, initially elicited a low humoral response, but this response gradually increased up to a peak around day 110 post inoculation, before decreasing. No apparent adverse side-effects were noted following inoculation of antigen-containing serum albumin beads, compared to necrosis following antigen in FCA inoculation, supporting the proposal of using albumin homotypic for the test inoculee animal, so that the beads would themselves be non-immunogenic and would merely act as a vehicle in the vaccine formulation. The indirect enzyme-linked immunosorbent assay (ELISA) was used to monitor the humoral response to antigen following inoculation. Results showed that covalent crosslinking of albumin in the formation of the beads did not promote immunogenicity on the part of the chemically altered albumin. The ELISA test was used to indicate the kinetics of the IgG response to Nodamura virus when presented in formulations such as: Freely soluble virus or its subunit; soluble intact virus inactivated by treatment with glutaraldehyde; intact virus entrapped in serum albumin beads cross; linked at different percentage final glutaraldehyde concentrations and also virus subunit prepared in albumin beads. The presence of virus-neutral ising antibodies was noted in serum obtained from rabbits inoculated with virus entrapped in albumin beads. Virus infectivity, titrated in mice, showed protection against virus challenge after incubation of virus with serum obtained above.
- Full Text:
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