Physicochemical Properties of the Vi Antigen Before and After Mild Alkaline Hydrolysis

Jarvis, F. G.; Mesenko, Marianne T.; Martin, Donald G.; Perrine, Theodore D.

doi:10.1128/jb.94.5.1406-1410.1967

Cited by 15 publications

(10 citation statements)

References 7 publications

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“…1). This behavior is typical for Enterobacteriaceae capsular polysaccharides, and it has been repeatedly postulated (e.g., 20,22,23,30) that, in the native material, the single glycan strands may be cross-linked by alkali-labile (possibly uronic acid ester) bonds. In the case of E. coli K29 polysaccharide, this view was strengthened by the detection (30; L.B.…”

Section: Discussionmentioning

confidence: 77%

Escherichia coli capsule bacteriophages. IV. Primary structure of the bacteriophage 29 receptor, the E. coli serotype 29 capsular polysaccharide

Choy¹,

Fehmel²,

Frank³

et al. 1975

J Virol

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Using periodate oxidation, methylation analysis, characterization of oligosaccharides obtained by Smith degradation or partial acid hydrolysis, as well as proton magnetic resonance, the primary structure of the Escherichia coli serotype 29 capsular polysaccharide (the receptor of E. coli K phage 29) was reinvestigated. The polymer was found to consist of hexasaccharide repeating units of the following structure: pyruvate (ketal) 4A6 D-Glcp ol4 2 D-Manp 2)-D-pa' 4 aa) 2)-D-Manp-(l c' 3)-D-Glcp-(-l4 3)-D-GlcUAp-(11-3)-D-Galp-(I1 Like the other Escherichia coli capsule bacteriophages (38, 41), phage 29 is specific for the host capsular polysaccharide, i.e., it does not adsorb to acapsular host mutants and generally not to related strains with capsules of different serotype and chemical structure. There is also a host capsule depolymerase activity associated with the particles of phage 29 (39)-small virions consisting of an isometric head with a base plate and a set of spikes (32, 41)-the active center of which is part of the virus spikes (4, 32). Within these organelles, the enzyme is part of subunits that contain polypeptides of about 57,000 daltons only (32). In the capsular glycan of the phage 29 host [E. coli Bi161/42 (24), 09:K29(A):H-, also the serological test strain for the E. coli K29 antigen (25) ] the virus particles catalyze the liberation of reducing glucose (39, 40). The primary structure of the E. coli K29 capsular polysaccharide has been investigated by Nhan et al. (30; L.

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Section: Discussionmentioning

confidence: 77%

Escherichia coli capsule bacteriophages. IV. Primary structure of the bacteriophage 29 receptor, the E. coli serotype 29 capsular polysaccharide

Choy¹,

Fehmel²,

Frank³

et al. 1975

J Virol

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“…The O-acetylation level is one of the critical determinants of immunogenicity in the Vi polysaccharide antigen. Removal of O-acetyl groups resulted in a lower vaccine immunogenicity [ 37 , 38 ].…”

Section: O-acetylation In Conjugate Vaccinesmentioning

confidence: 99%

Role of O-Acetylation in the Immunogenicity of Bacterial Polysaccharide Vaccines

Berti

Ricco²,

Rappuoli

2018

Molecules

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The incidence of infectious diseases caused by several bacterial pathogens such as Haemophilus influenzae type b, Streptococcus pneumoniae, and Neisseria meningitidis, has been dramatically reduced over the last 25 years through the use of glycoconjugate vaccines. The structures of the bacterial capsular polysaccharide (CPS) antigens, extracted and purified from microbial cultures and obtained with very high purity, show that many of them are decorated by O-acetyl groups. While these groups are often considered important for the structural identity of the polysaccharides, they play a major role in the functional immune response to some vaccines such as meningococcal serogroup A and Salmonella typhi Vi, but do not seem to be important for many others, such as meningococcal serogroups C, W, Y, and type III Group B Streptococcus. This review discusses the O-acetylation status of CPSs and its role in the immunological responses of these antigens.

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“…Although the secondary structure of the Vi antigen has not been established, some evidence that parallel polysaccharide chains may be linked together by ester bonds has been presented by G. Kiessling (Ph.D. Thesis, Univ. of Hamburg, EFFECT OF SONIC TREATMENT ON Vi ANTIGEN Germany, 1966) and Jarvis et al (10). Treatment by dilute acid or alkali may cause depolymerization largely by hydrolysis of such bonds.…”

Section: Effeci Of Sonic Treatment On VI Antigenmentioning

confidence: 99%

Physicochemical and Biological Properties of Sonically Treated Vi Antigen

1967

Self Cite

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Electrophoretically purified Vi antigen from Citrobacter freundii 5396/38 was depolymerized by sonic treatment. The treatment caused an 80% reduction in specific viscosity and a reduction in molecular weight from 1.6 x 106 to 3.9 X 104. The 0-acetyl and N-acetyl contents of the antigen and its infrared spectrum remained unchanged. The sonically treated antigen was only 1 % as effective as the original antigen in eliciting protection in mice against challenge with Salmonella typhi. Sonically treated antigen also elicited lower antibody titers after single injections in mice and rabbits. No loss in ability to precipitate antibody or to sensitize red blood cells for hemagglutination was observed.

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Physicochemical Properties of the Vi Antigen Before and After Mild Alkaline Hydrolysis

Cited by 15 publications

References 7 publications

Escherichia coli capsule bacteriophages. IV. Primary structure of the bacteriophage 29 receptor, the E. coli serotype 29 capsular polysaccharide

Escherichia coli capsule bacteriophages. IV. Primary structure of the bacteriophage 29 receptor, the E. coli serotype 29 capsular polysaccharide

Role of O-Acetylation in the Immunogenicity of Bacterial Polysaccharide Vaccines

Physicochemical and Biological Properties of Sonically Treated Vi Antigen

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