Polymorphisms of Immunoglobulins: Gm, Am and Km Typing

Lange, G. G. de; Leeuwen, A.M. van; Eede, P.H. van; Lincoln, P. J.; Engelfriet, C. P.

doi:10.1007/978-3-642-73330-7_14

Cited by 30 publications

(43 citation statements)

References 2 publications

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“…The main allelic forms for IgG1 are G1m (z,a), G1m (f), and G1m (f,a) [9,64,65]. The G1m (f) allele is only found in Caucasians, whereas the G1m (f,a) allele is common in Asians; other variants have also been described [9,66,67].…”

Section: Discussionmentioning

confidence: 99%

Selective subnormal IgG3 in 121 adult index patients with frequent or severe bacterial respiratory tract infections

Barton

Bertoli²,

Acton

2016

Cellular Immunology

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Section: Discussionmentioning

confidence: 99%

Selective subnormal IgG3 in 121 adult index patients with frequent or severe bacterial respiratory tract infections

Barton

Bertoli²,

Acton

2016

Cellular Immunology

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“…83,84 Four systems have been described for the constant heavy and k light chain genes of Igs, Gm, Am, Em and Km, with 24 allotypes. 85,86 Gm and Km allotypes are associated with amino acid substitutions in the constant regions-the former influencing IgG1, IgG2 and IgG3 subclass levels-and are inherited in the Mendelian manner. 87 The sizable gene family of human FcRs belongs to the large Ig supergene family.…”

Section: Igs and Fcrs Polymorphismsmentioning

confidence: 99%

Congenital toxoplasmosis: candidate host immune genes relevant for vertical transmission and pathogenesis

et al. 2010

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“…Recombinant anti-rhesus D (anti-RhD) mAb were constructed in IgG1, IgG2, IgG3, IgG4, IgA 1 , and IgA 2 versions (20,21). mAb constructs relied on those H-chain allotypes most prevalent in African populations: G1m(a,z), G2m(n ϩ ) and G3m(b) for IgG1, IgG2, and IgG3, respectively, and the A2m1 for IgA 2 (22).…”

Section: Monoclonal Absmentioning

confidence: 99%

A Novel Antibody-Dependent Cellular Cytotoxicity Mechanism Involved in Defense against Malaria Requires Costimulation of Monocytes FcγRII and FcγRIII

Jafarshad

Dziegiel

Lundquist

et al. 2007

The Journal of Immunology

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Clinical experiments have shown that the Ab-dependent cell-mediated inhibition of Plasmodium falciparum is a major mechanism controlling malaria parasitemia and thereby symptoms. In this study, we demonstrate that a single merozoite per monocyte (MN) is sufficient to trigger optimal antiparasitic activity. Using particulate Ag as pseudomerozoites, we show that only Ags, and no other parasite-derived factor, are required to trigger MN activation and that a single Ag is as potent as the complex combination of Ags constituting the merozoite surface. Moreover, we found that soluble Ags binding at least two Abs are as effective as the parasite at stimulating MN and that nonmalarial Ags are as efficient provided they are targeted by cytophilic Abs. Indeed, only cytophilic IgGs are potent and, in agreement with immunoepidemiological findings, IgG3 is superior to IgG1. Very low Ab concentrations (>700 pM), i.e., in the range of molecules having a hormonal effect, are effective, in contrast to Abs having a direct, neutralizing effect. Finally, Ab-dependent cell-mediated inhibition proved to require the synergistic activation of both FcγRIIa and FcγRIIIa which both distinguish it from other Ab-dependent cellular cytotoxicity and implies that all MN are not equally effective. These findings have both fundamental and practical implications, particularly for vaccine discovery.

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Polymorphisms of Immunoglobulins: Gm, Am and Km Typing

Cited by 30 publications

References 2 publications

Selective subnormal IgG3 in 121 adult index patients with frequent or severe bacterial respiratory tract infections

Selective subnormal IgG3 in 121 adult index patients with frequent or severe bacterial respiratory tract infections

Congenital toxoplasmosis: candidate host immune genes relevant for vertical transmission and pathogenesis

A Novel Antibody-Dependent Cellular Cytotoxicity Mechanism Involved in Defense against Malaria Requires Costimulation of Monocytes FcγRII and FcγRIII

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