Immunoglobulin A

Bakema, Jantine E.; Egmond, Marjolein van

doi:10.4161/mabs.3.4.16092

Cited by 84 publications

(51 citation statements)

References 138 publications

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“…A number of studies have reported that the IgA Ab may have more advantages than IgG antibodies for inhibiting tumor growth and infectious diseases via mediation of immune cell targeting (40). For example, IgA antibodies are far more effective than IgG anti-tumor antibodies in recruiting neutrophils for destruction of lymphoma and solid tumor targets (41–43).…”

Section: Discussionmentioning

confidence: 99%

Impact of IgA Constant Domain on HIV-1 Neutralizing Function of Monoclonal Antibody F425A1g8

Duval

Lewis

et al. 2013

The Journal of Immunology

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With the majority of HIV infections resulting from mucosal transmission, induction of an effective mucosal immune response is thought to be pivotal in preventing transmission. HIV-specific IgA, but not IgG, has been detected in genital tract, seminal fluid, urethral swabs, urine and vaginal wash samples of HIV-negative sex workers and HIV-status discordant couples. Purified mucosal and plasma IgA from some individuals with highly exposed, persistently sero-negative (HEPS) can neutralize infection and present cross-clade neutralization activity though present at low levels. We generated a CD4i human monoclonal antibody (mAb) F425A1g8 and characterized the impact of its isotype variants on HIV neutralizing activity. The result showed that, in contrast to little neutralization by the F425A1g8 IgG1 in the absence of sCD4, the IgA1 variant of the antibody (Ab) displayed significant independent neutralization activity against a range of HIV clade B isolates in the absence of sCD4. The studies of the neutralizing function of IgA isotypes, and the functional relationship between different antigenic epitopes and IgA antibodies, may also suggest strategies for the intervention of virus transmission and spread within the mucosa of host, as well as serve to inform the design of vaccine strategies that may be more effective at preventing mucosal transmission. This research clearly suggests that IgA isotype because of its unique molecular structure may play an important role in HIV neutralization.

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Section: Discussionmentioning

confidence: 99%

Impact of IgA Constant Domain on HIV-1 Neutralizing Function of Monoclonal Antibody F425A1g8

Duval

Lewis

et al. 2013

The Journal of Immunology

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“…The therapeutic antibody field is currently dominated by IgG-based mAbs. The advantages of opening up this arena to include IgA-based mAbs are becoming increasingly apparent, piquing interest in both academia and industry [79,[131][132][133]. One advantage is the new prospects it offers in terms of intellectual property, in what is already a complex landscape [134].…”

Section: Advantages Of Iga-based Therapeuticsmentioning

confidence: 99%

IgA: Structure, Function, and Developability

2019

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Immunoglobulin A (IgA) plays a key role in defending mucosal surfaces against attack by infectious microorganisms. Such sites present a major site of susceptibility due to their vast surface area and their constant exposure to ingested and inhaled material. The importance of IgA to effective immune defence is signalled by the fact that more IgA is produced than all the other immunoglobulin classes combined. Indeed, IgA is not just the most prevalent antibody class at mucosal sites, but is also present at significant concentrations in serum. The unique structural features of the IgA heavy chain allow IgA to polymerise, resulting in mainly dimeric forms, along with some higher polymers, in secretions. Both serum IgA, which is principally monomeric, and secretory forms of IgA are capable of neutralising and removing pathogens through a range of mechanisms, including triggering the IgA Fc receptor known as FcαRI or CD89 on phagocytes. The effectiveness of these elimination processes is highlighted by the fact that various pathogens have evolved mechanisms to thwart such IgA-mediated clearance. As the structure–function relationships governing the varied capabilities of this immunoglobulin class come into increasingly clear focus, and means to circumvent any inherent limitations are developed, IgA-based monoclonal antibodies are set to emerge as new and potent options in the therapeutic arena.

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“…Antibody-dependent enhancement of viral infections are major hurdles in the development of effective vaccines. This enhancement is likely facilitated by the Fc domain of IgG but not for its isotype variant IgA 18 . The avidity of mucosal IgA, in comparison with IgG, due to the multimeric structure, enhances the antibody binding with antigens.…”

Section: Introductionmentioning

confidence: 99%

IgA MAb blocks SARS-CoV-2 Spike-ACE2 interaction providing mucosal immunity

Ejemel¹,

Qi²,

Hou

et al. 2020

Preprint

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SummaryCOVID-19 caused by SARS-CoV-2 has become a global pandemic requiring the development of interventions for the prevention or treatment to curtail mortality and morbidity. No vaccine to boost mucosal immunity or as a therapeutic has yet been developed to SARS-CoV-2. In this study we discover and characterize a cross-reactive human IgA monoclonal antibody, MAb362. MAb362 binds to both SARS-CoV and SARS-CoV-2 spike proteins and competitively blocks hACE2 receptor binding, by completely overlapping the hACE2 structural binding epitope. Furthermore, MAb362 IgA neutralizes both pseudotyped SARS-CoV and SARS-CoV-2 in human epithelial cells expressing hACE2. SARS-CoV-2 specific IgA antibodies, such as MAb362, may provide effective immunity against SARS-CoV-2 by inducing mucosal immunity within the respiratory system, a potentially critical feature of an effective vaccine.

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Immunoglobulin A

Cited by 84 publications

References 138 publications

Impact of IgA Constant Domain on HIV-1 Neutralizing Function of Monoclonal Antibody F425A1g8

Impact of IgA Constant Domain on HIV-1 Neutralizing Function of Monoclonal Antibody F425A1g8

IgA: Structure, Function, and Developability

IgA MAb blocks SARS-CoV-2 Spike-ACE2 interaction providing mucosal immunity

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