ArticleInfection and immunity2007
Impact of the molecular form of immunoglobulin A on functional activity in defense against Streptococcus pneumoniae.
Article in Infection and immunity, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
26 citing papers in PubMed, 47 citations in OpenAlex.
- Salivary immune responses to the 7-valent pneumococcal conjugate vaccine in the first 2 years of life.PloS one · 2012Trial
- Innate immune responses in pneumonia.Pneumonia (Nathan Qld.) · 2023Review
- Role ofFrontiers in cellular and infection microbiology · 2023Review
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- Immune exclusion by naturally acquired secretory IgA against pneumococcal pilus-1.The Journal of clinical investigation · 2020Article
- IgA and FcαRI: Versatile Players in Homeostasis, Infection, and Autoimmunity.ImmunoTargets and therapy · 2020Review
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- Plasma therapy leads to an increase in functional IgA and IgM concentration in the blood and saliva of a patient with X-linked agammaglobulinemia.Journal of translational medicine · 2019Article
- Plant-derived secretory component forms secretory IgA with shiga toxin 1-specific dimeric IgA produced by mouse cells and whole plants.Plant cell reports · 2019Article
- A Capsular Polysaccharide-Specific Antibody Alters Streptococcus pneumoniae Gene Expression during Nasopharyngeal Colonization of Mice.Infection and immunity · 2018Article
- The Role of the Polymeric Immunoglobulin Receptor and Secretory Immunoglobulins during Mucosal Infection and Immunity.Viruses · 2018Review
- Bacterial-Host Interactions: Physiology and Pathophysiology of Respiratory Infection.Physiological reviews · 2018Review
- Streptococcus pneumoniae IgA1 protease: A metalloprotease that can catalyze in a split manner in vitro.Protein science : a publication of the Protein Society · 2017Article
- Novel Monoclonal Antibodies for Studies of Human and Rhesus Macaque Secretory Component and Human J-Chain.Monoclonal antibodies in immunodiagnosis and immunotherapy · 2016Article
- Article
- Antibody blocks acquisition of bacterial colonization through agglutination.Mucosal immunology · 2015Article
- Pneumococcal IgA1 protease subverts specific protection by human IgA1.Mucosal immunology · 2014Article
- Genome-wide association study identifies TNFSF13 as a susceptibility gene for IgA in a South Chinese population in smokers.Immunogenetics · 2012Article
Corrections and comments
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Authors and funding
6 authors at 5 institutions in 2 countries.
Funding
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.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.