Mucosal Immunoglobulins

Woof, Jenny M.

doi:10.1016/b978-0-12-415847-4.00017-3

Cited by 33 publications

(26 citation statements)

References 385 publications

(539 reference statements)

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“…In addition, IgA has been shown to facilitate the uptake of luminal Ag across the intestinal epithelium, enhancing Ag-presentation and priming of Ag-specific immunity. 8,9,[80][81][82] Since the gut is a complex system with 3 main interacting components, the intestinal epithelium, the microbiota and the immune system, alterations in IgA production leads to changes in the composition of the intestinal microbiota and altered intestinal barrier function. Mucosal IgA has been shown to play an important role in containing potentially invasive commensal bacteria, suggesting that IgA exerts protective effects at the level of barrier function in the gut.…”

Section: Functions Of Igamentioning

confidence: 99%

“…pIgA binds the polymeric Ig receptor (pIgR) at the basolateral side of intestinal epithelial cells (IEC), and the complex is shuttled to the apical membrane where pIgR is cleaved to release secretory IgA (SIgA) as a hybrid molecule comprising pIgA and the secretory component provided by the pIgR. [7][8][9] Although mucosae are the primary inductive sites for IgA C PC, in adults, about 80% of serum PC and 40% of bone marrow (BM) PC are IgA C , suggesting a substantial contribution of IgA C PC to the long-lived PC reservoir. 10 Development of intestinal IgA depends largely on commensal colonization as GF mice have much lower numbers of IgA C PC.…”

Section: Locations Of Iga C Plasma Cell Generationmentioning

confidence: 99%

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Re-thinking the functions of IgA⁺plasma cells

Gommerman

Rojas

Fritz³

2014

Gut Microbes

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Section: Functions Of Igamentioning

confidence: 99%

Section: Locations Of Iga C Plasma Cell Generationmentioning

confidence: 99%

Re-thinking the functions of IgA⁺plasma cells

Gommerman

Rojas

Fritz³

2014

Gut Microbes

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“…These polymeric IgA forms are associated with the extracellular portion of the polymeric Ig receptor, generating a complex (receptor + polymeric IgA) called S-IgA (9). S-IgA primarily corresponds to dimeric IgA, although low levels of some larger polymeric forms, particularly tetramers, are also present (9)(10)(11)(12)(13)(14)(15). Polymeric S-IgA has been shown (both in vitro and in experimental animal models) to be more effective than monomeric IgA or IgG for the neutralization of influenza viruses (16)(17)(18)(19).…”

mentioning

confidence: 99%

Relationship of the quaternary structure of human secretory IgA to neutralization of influenza virus

Suzuki

Kawaguchi

Ainai

et al. 2015

Proc. Natl. Acad. Sci. U.S.A.

116

103

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Secretory IgA (S-IgA) antibodies, the major contributors to humoral mucosal immunity to influenza virus infection, are polymeric Igs present in many external secretions. In the present study, the quaternary structures of human S-IgA induced in nasal mucosa after administration of intranasal inactivated influenza vaccines were characterized in relation to neutralization potency against influenza A viruses. Human nasal IgA antibodies have been shown to contain at least five quaternary structures. Direct and real-time visualization of S-IgA using high-speed atomic force microscopy (AFM) demonstrated that trimeric and tetrameric S-IgA had six and eight antigen-binding sites, respectively, and that these structures exhibited large-scale asynchronous conformational changes while capturing influenza HA antigens in solution. Furthermore, trimeric, tetrameric, and larger polymeric structures, which are minor fractions in human nasal IgA, displayed increased neutralizing potency against influenza A viruses compared with dimeric S-IgA, suggesting that the larger polymeric than dimeric forms of S-IgA play some important roles in protection against influenza A virus infection in the human upper respiratory tract.

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“…Monomeric IgA is also one of the major immunoglobulin classes present in serum, second only to IgG. In humans, the production of IgA per day is greater than that of the other classes of immunoglobulins combined [1]. Despite this, the ability of IgA -both systemic and mucosal -to modulate the risks of HIV infection remains relatively understudied.…”

Section: Introductionmentioning

confidence: 99%

Are anti-HIV IgAs good guys or bad guys?

Zhou

Ruprecht

2014

Retrovirology

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An estimated 90% of all HIV transmissions occur mucosally. Immunoglobulin A (IgA) molecules are important components of mucosal fluids. In a vaccine efficacy study, in which virosomes displaying HIV gp41 antigens protected most rhesus monkeys (RMs) against simian-human immunodeficiency virus (SHIV), protection correlated with vaginal IgA capable of blocking HIV transcytosis in vitro. Furthermore, vaginal IgG exhibiting virus neutralization and/or antibody-dependent cellular cytotoxicity (ADCC) correlated with prevention of systemic infection. In contrast, plasma IgG had neither neutralizing nor ADCC activity. More recently, a passive mucosal immunization study provided the first direct proof that dimeric IgAs (dIgAs) can prevent SHIV acquisition in RMs challenged mucosally. This study compared dimeric IgA1 (dIgA1), dIgA2, or IgG1 versions of a human neutralizing monoclonal antibody (nmAb) targeting a conserved HIV Env epitope. While the nmAb neutralization profiles were identical in vitro, dIgA1 was significantly more protective in vivo than dIgA2. Protection was linked to a new mechanism: virion capture. Protection also correlated with inhibition of transcytosis of cell-free virus in vitro. While both of these primate model studies demonstrated protective effects of mucosal IgAs, the RV144 clinical trial identified plasma IgA responses to HIV Env as risk factors for increased HIV acquisition. In a secondary analysis of RV144, plasma IgA decreased the in vitro ADCC activity of vaccine-induced, Env-specific IgG with the same epitope specificity. Here we review the current literature regarding the potential of IgA -systemic as well as mucosal -in modulating virus acquisition and address the question whether anti-HIV IgA responses could help or harm the host.

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Mucosal Immunoglobulins

Cited by 33 publications

References 385 publications

Re-thinking the functions of IgA⁺plasma cells

Re-thinking the functions of IgA⁺plasma cells

Relationship of the quaternary structure of human secretory IgA to neutralization of influenza virus

Are anti-HIV IgAs good guys or bad guys?

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Mucosal Immunoglobulins

Cited by 33 publications

References 385 publications

Re-thinking the functions of IgA+plasma cells

Re-thinking the functions of IgA+plasma cells

Relationship of the quaternary structure of human secretory IgA to neutralization of influenza virus

Are anti-HIV IgAs good guys or bad guys?

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Re-thinking the functions of IgA⁺plasma cells

Re-thinking the functions of IgA⁺plasma cells