Jacalin, the human IgA1 and IgD precipitating lectin, also binds IgA2 of both allotypes

Aucouturier, Pièrre; Duarte, Françoise; Mihaesco, Edith; Pineau, Nathalie; Preud’homme, Jean-Louis

doi:10.1016/0022-1759(88)90331-6

Cited by 43 publications

(19 citation statements)

References 24 publications

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“…As serum lgAs are composed of IgA-1 and IgA-2, it was necessary to confirm that jacalin also recognizes IgA-2 in our assay. It appears that jacalin does bind to serum and colostral IgA-2 in an ELISA, in agreement with Aucouturier et al (11). Reactivity of myeloma IgA-2 to jacalin was assessed by the jacalin index, as compared with standard IgA purified by jacalin.…”

Section: Iganmentioning

confidence: 61%

Impairment of jacalin binding to serum IgA in IgA nephropathy

André¹,

Pogamp²,

Chevet³

1990

Clinical Laboratory Analysis

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A test was set up to analyze the direct binding of serum IgA to the lectin jacalin. Under the testing conditions, jacalin bound to both IgA subclasses and reacted similarly with monomeric and polymeric IgA. A jacalin index was defined to quantify serum IgA binding to this lectin. The jacalin index appeared significantly lower in IgA nephropathy than in controls. This may be related to abnormal IgA glycosylation, which could explain, at least in part, the mesangial deposition responsible for the renal disease.

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Section: Iganmentioning

confidence: 61%

Impairment of jacalin binding to serum IgA in IgA nephropathy

André¹,

Pogamp²,

Chevet³

1990

Clinical Laboratory Analysis

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“…Thus, the levels of IgG and IgM could not be determined by ELISA using jacal in-coated microplates. There was no significant rela tionship between the degree of histologic changes and the levels of serum IgA measured by ELISA using jacalincoated microplates in patients with IgA nephropathy in this study [data not shown], Jacalin was bound with both IgAl and IgA2 as de scribed by Andre et al [4] and Aucouturier et al [10], Reactivity of serum IgAl and IgA2 with jacalin was also observed in the present study [data not shown]. There was a significant difference in the capacity of serum IgA bind ing to jacalin between the results of Andre et al [4], Mes tecky et al [9] and those in our report.…”

Section: Single Radial Immunodiffusion For Quantitative Detection O Fmentioning

confidence: 76%

Binding Capacity of Serum IgA to Jacalin in Patients with IgA Nephropathy Using Jacalin-Coated Microplates

Tomino

Ohmuro

Takahashi

et al. 1995

Nephron

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Binding capacity of serum IgA to jacalin in 22 patients with IgA nephropathy, 14 patients with diffuse mesangial proliferative glomerulonephritis (non-IgA nephropathy) and 20 age-matched healthy adults was examined by enzyme-linked immunoassay (ELISA) using jacalin-coated microplates. In contrast to previous findings, the binding capacity of serum IgA to jacalin in patients with IgA nephropathy measured by ELISA using jacalin-coated microplates was significantly higher than that in healthy adults. The ratio of serum IgA levels measured by this method to those obtained by single radial immunodiffusion was significantly increased in patients with IgA nephropathy. It appeared that the capacity of serum IgA binding to jacalin was marked in these patients. It is concluded that the binding capacity of serum IgA to jacalin is not ubiquitously impaired in all patients with IgA nephropathy.

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“…Most publications do not distinguish between IgA1 and IgA2, and many also do not differentiate between monomeric, dimeric, or polymeric forms [33][34][35][36][37][38][39]. Furthermore, some studies only report on serum IgA responses, whereas others exclusively focus on IgA in mucosal fluids.…”

Section: Methods To Isolate Various Forms Of Human Igamentioning

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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Jacalin, the human IgA1 and IgD precipitating lectin, also binds IgA2 of both allotypes

Cited by 43 publications

References 24 publications

Impairment of jacalin binding to serum IgA in IgA nephropathy

Impairment of jacalin binding to serum IgA in IgA nephropathy

Binding Capacity of Serum IgA to Jacalin in Patients with IgA Nephropathy Using Jacalin-Coated Microplates

Are anti-HIV IgAs good guys or bad guys?

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