scholarly journals Prolonged and preferential production of polymeric immunoglobulin A in response to Streptococcus pneumoniae capsular polysaccharides.

1996 ◽  
Vol 64 (10) ◽  
pp. 4339-4344 ◽  
Author(s):  
S Johnson ◽  
N L Opstad ◽  
J M Douglas ◽  
E N Janoff
Keyword(s):  
Streptococcus Pneumoniae ◽  
Immunoglobulin A ◽  
Capsular Polysaccharides

scholarly journals Impact of the Molecular Form of Immunoglobulin A on Functional Activity in Defense against Streptococcus pneumoniae

2007 ◽  
Vol 75 (4) ◽  
pp. 1801-1810 ◽  
Author(s):  
Claudine E. Fasching ◽  
Tracy Grossman ◽  
Blaise Corthésy ◽  
Andrew G. Plaut ◽  
Jeffrey N. Weiser ◽  
...  
Keyword(s):  
Streptococcus Pneumoniae ◽  
Molecular Form ◽  
Immunoglobulin A ◽  
Secretory Component ◽  
Secretory Iga ◽  
Molecular Forms ◽  
Capsular Polysaccharides ◽  
Iga1 Protease ◽  
Functional Inhibition ◽  
Function Relationship

ABSTRACT Antibodies of the immunoglobulin A (IgA) class react with capsular polysaccharides of Streptococcus pneumoniae and support complement-dependent opsonophagocytosis (OPC) of the organism by phagocytes. We characterized the biologic impact of the molecular forms of human monoclonal capsule-specific IgA (monomeric IgA [mIgA], polymeric IgA [pIgA], and secretory IgA [SIgA]) on OPC and susceptibility to cleavage by IgA1 protease. The efficiency of SIgA in support of OPC of S. pneumoniae was comparable to that of pIgA, and both forms exceeded that of mIgA by a fivefold margin. This structure-function relationship was associated with three factors. First, the avidities, or functional affinities, of both pIgA and SIgA for pneumococcal capsules exceeded those of mIgA. Second, both pIgA and SIgA required less complement to achieve similar levels of bacterial OPC than did mIgA, indicating that secretory component does not hinder the effect of complement. Third, both pIgA and SIgA mediated agglutination of the organism, whereas mIgA did not. All three forms of capsule-specific IgA showed comparable susceptibilities to cleavage and functional inhibition by bacterial IgA1 protease, demonstrating that secretory component does not prevent the proteolytic degradation of IgA1 by IgA1 protease. IgA1 cleavage results in formation of identical Fab fragments for each of the molecular forms, thereby abolishing the contribution of multivalence of pIgA and SIgA. In summary, the polymeric forms of IgA (both pIgA and SIgA) provide a substantial advantage in binding, agglutination, and OPC of the organism.

scholarly journals Assignment of Weight-Based Immunoglobulin G1 (IgG1) and IgG2 Units in Antipneumococcal Reference Serum Lot 89-S(F) for Pneumococcal Polysaccharide Serotypes 1, 4, 5, 7F, 9V, and 18C

2005 ◽  
Vol 12 (1) ◽  
pp. 218-223 ◽  
Author(s):  
Daniel J. Sikkema ◽  
Nancy A. Ziembiec ◽  
Thomas R. Jones ◽  
Stephen W. Hildreth ◽  
Dace V. Madore ◽  
...  
Keyword(s):  
Streptococcus Pneumoniae ◽  
Immune Responses ◽  
Conjugate Vaccine ◽  
Pneumococcal Conjugate Vaccine ◽  
Pneumococcal Disease ◽  
Pneumococcal Infection ◽  
Capsular Polysaccharides ◽  
Standardization Method ◽  
Igg2 Antibody ◽  
Reference Serum

ABSTRACT Weight-based assignments for immunoglobulin G1 (IgG1) and IgG2 subclass antibodies to Streptococcus pneumoniae capsular polysaccharides (PnPs) in antipneumococcal standard reference serum lot 89-S (lot 89-S), also known as lot 89-SF, have been determined for serotypes 1, 4, 5, 7F, 9V, and 18C. This extends the usefulness of lot 89-S beyond the IgG1 and IgG2 subclass assignments for serotypes 3, 6B, 14, 19F, and 23F made previously (A. Soininen, H. Kayhty, I. Seppala, and T. Wuorimaa, Clin. Diagn. Lab. Immunol. 5:561-566, 1998) to cover 11 major serotypes associated with the highest percentage of pneumococcal disease worldwide. A method of equivalence of absorbances in enzyme immunosorbent assays was used to determine the IgG1 and IgG2 antibody concentrations for the additional serotypes in lot 89-S, based on the subclass values previously assigned for PnPs serotypes 6B, 14, and 23F. This cross-standardization method assures consistency with previous antibody assignments in that reference serum. The newly assigned subclass values for serotype 9V, and previously assigned values for serotype 14, were used to quantitate PnPs antibodies in sera from adult and pediatric subjects immunized with a pneumococcal conjugate vaccine. There was a predominance of IgG1 anti-PnPs antibodies in pediatric sera and IgG2 anti-PnPs antibodies in the adult sera. The IgG1 and IgG2 subclass assignments for the 11 PnPs serotypes in antipneumococcal standard reference serum lot 89-S are useful for quantitating and characterizing immune responses to pneumococcal infection and vaccination regimens.

Development of experimental carbohydrate-conjugate vaccines composed of Streptococcus pneumoniae capsular polysaccharides and the universal helper T-lymphocyte epitope (PADRE®)

Vaccine ◽  
2004 ◽  
Vol 22 (19) ◽  
pp. 2362-2367 ◽  
Author(s):  
Jeff Alexander ◽  
Marie-France del Guercio ◽  
Barbara Frame ◽  
Ajesh Maewal ◽  
Alessandro Sette ◽  
...  
Keyword(s):  
Streptococcus Pneumoniae ◽  
T Lymphocyte ◽  
Capsular Polysaccharides ◽  
Conjugate Vaccines

scholarly journals Serum immunoglobulins and anti-pneumococcal antibody levels in patients with bronchiectasis of unknown aetiology

2020 ◽  
Vol 19 (2) ◽  
pp. 200-207
Author(s):  
Mustafa Norhazlin ◽  
Asrul Abdul Wahab ◽  
Mohd Faisal Abdul Hamid ◽  
Hamzaini Abdul Hamid ◽  
Husyairi Harunarashid
Keyword(s):  
Streptococcus Pneumoniae ◽  
Specific Antibody ◽  
Capsular Polysaccharide ◽  
Medical Science ◽  
Asian Population ◽  
Immunoglobulin Therapy ◽  
Female Gender ◽  
Total Serum ◽  
Capsular Polysaccharides ◽  
Serum Immunoglobulins

Background: Bronchiectasis is a chronic condition which can result in significant physical and social morbidity. The exact prevalence in Malaysia is unknown although several studies have shown a higher prevalence in the Asian population. Several causative factors have been identified but there are many patients with unknown aetiologies. This study looks into the level of serum immunoglobulins and antipenumococcal antibody in bronchiectasis patients where they were not part of prior routine investigations. Methodology: Four hundred fifteen bronchiectasis patients were screened and 26 patients who fulfilled the inclusion and exclusion criteria were enrolled for this study. The serum immunoglobulins (IgG, IgA and IgM) concentrations were measured using nephelometry and interpreted according to age-matched reference range. The integrity of antibody production against specific antibody to capsular polysaccharides of Streptococcus pneumoniae were assessed using ELISA method and the level of ≥ 10mg/L is considered as reactive. Results: The twenty six bronchiectasis patients have the mean age of 62 years and a predilection of female gender. Majority of patients presented with typical bronchiectasis symptoms which were further supported by radiological findings. One of 26 patients (4%) had low total serum IgG level. The vaccinated group has higher anti-pneumococcal capsular polysaccharide antibody level (median: 224.2 mg/L) compared to the unvaccinated group (median: 100.4 mg/L). However there is no statistical difference between the anti-PCP levels of both groups (p> 0.05). All of the selected patients had reactive specific antibody to capsular polysaccharides of Streptococcus pneumoniae regardless of the vaccination status, which may reflect the natural acquisition of anti-pneumococcal immunity. Conclusion: Although immunoglobulin deficiency is an uncommon aetiological cause of bronchiectasis, the immunoglobulin parameters can be helpful in selecting patients who should receive the appropriate treatment of immunoglobulin therapy for the prevention of subsequent complications and better quality of life. Bangladesh Journal of Medical Science Vol.19(2) 2020 p.200-207

scholarly journals WciGO-Acetyltransferase Functionality Differentiates Pneumococcal Serotypes 35C and 42

2017 ◽  
Vol 55 (9) ◽  
pp. 2775-2784 ◽  
Author(s):  
K. Aaron Geno ◽  
C. Allen Bush ◽  
Mengnan Wang ◽  
Cheng Jin ◽  
Moon H. Nahm ◽  
...  
Keyword(s):  
Streptococcus Pneumoniae ◽  
Nucleotide Sequence ◽  
Chromosomal Region ◽  
Capsular Polysaccharides ◽  
Pneumococcal Serotypes ◽  
Subsequent Reaction ◽  
Content Type ◽  
Comprehensive View ◽  
Opsonophagocytic Killing ◽  
Dependent Mechanism

ABSTRACTStreptococcus pneumoniaeexpresses capsular polysaccharides (CPSs) to protect itself from opsonophagocytic killing. The genes responsible for capsules synthesized by the Wzy-dependent mechanism, which accounts for 96 of the 98 known pneumococcal capsule types, are in a chromosomal region known as thecpslocus. The nucleotide sequence in this region has been determined for all serotypes. In contrast, not all CPS structures have been defined. The structure of the serotype 35C polysaccharide was recently reported, but the presence ofO-acetyltransferase genes in the serotype 35Ccpslocus suggested that it could be incomplete, as the reported structure contains no O-acetylation. In addition, the genetic distinction of serotype 35C from the closely related serotype 42 was unclear, as their reportedcpsloci are nearly identical. To clarify these discrepancies, we obtained serotype 35C and 42 clinical and reference isolates and studied their serological and genetic properties, as well as the structures of CPSs purified from reference isolates. We demonstrated that theO-acetyltransferase WciG was functional in serotype 35C but nonfunctional in serotype 42 due to a deletion inwciG. Serotype 35C was O-acetylated at the 5- and 6-positions of 3-β-galactofuranose, as well as the 2-position of 6-β-galactofuranose. However, serotype 42 has only O-acetylation at 3-β-galactofuranose, an observation consistent with its loss of WciG functionality, which is associated with O-acetylation at the 2-position and subsequent reaction with typing antiserum 35a. These findings provide a comprehensive view of the genetic, biochemical structural, and serological bases of serotypes 35C and 42.

scholarly journals Production of Capsular Polysaccharide ofStreptococcus pneumoniae Type 14 and Its Purification by Affinity Chromatography

2001 ◽  
Vol 67 (2) ◽  
pp. 969-971 ◽  
Author(s):  
Norma Suárez ◽  
Laura Franco Fraguas ◽  
Esther Texeira ◽  
Hugo Massaldi ◽  
Francisco Batista-Viera ◽  
...  
Keyword(s):  
Streptococcus Pneumoniae ◽  
Affinity Chromatography ◽  
Efficient Method ◽  
Capsular Polysaccharide ◽  
Capsular Polysaccharides ◽  
Affinity Adsorbent ◽  
Soybean Lectin

ABSTRACT We describe a rapid and efficient method for producing the capsular polysaccharide of Streptococcus pneumoniae by fermentation on tryptic soy broth and purification of this compound by using immobilized soybean lectin as an affinity adsorbent. In principle, the same strategy can be used to produce purified capsular polysaccharides from other streptococcal serotypes by selecting the appropriate lectin adsorbents.

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