Immunology of the Fetus and Newborn

Weitkamp, Jörn-Hendrik; Lewis, David B.; Levy, Ofer

doi:10.1016/b978-0-323-40139-5.00036-x

Cited by 2 publications

(2 citation statements)

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“…These fetal IgM antibodies are predominantly polyreactive “natural” IgM antibodies that play a role in the innate defense against infectious pathogens [ 33 ]. Postnatal IgM concentrations increase rapidly within the first month of postnatal life likely due to increased exposure to foreign antigens, and then gradually level off [ 34 ]. Levels of prenatal IgM are approximately 5 mg/dL in infants at 28 weeks and 11 mg/dL at birth.…”

Section: Introduction To Immunoglobulin M (Igm)mentioning

confidence: 99%

Structure, Function, and Therapeutic Use of IgM Antibodies

et al. 2020

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Natural immunoglobulin M (IgM) antibodies are pentameric or hexameric macro-immunoglobulins and have been highly conserved during evolution. IgMs are initially expressed during B cell ontogeny and are the first antibodies secreted following exposure to foreign antigens. The IgM multimer has either 10 (pentamer) or 12 (hexamer) antigen binding domains consisting of paired µ heavy chains with four constant domains, each with a single variable domain, paired with a corresponding light chain. Although the antigen binding affinities of natural IgM antibodies are typically lower than IgG, their polyvalency allows for high avidity binding and efficient engagement of complement to induce complement-dependent cell lysis. The high avidity of IgM antibodies renders them particularly efficient at binding antigens present at low levels, and non-protein antigens, for example, carbohydrates or lipids present on microbial surfaces. Pentameric IgM antibodies also contain a joining (J) chain that stabilizes the pentameric structure and enables binding to several receptors. One such receptor, the polymeric immunoglobulin receptor (pIgR), is responsible for transcytosis from the vasculature to the mucosal surfaces of the lung and gastrointestinal tract. Several naturally occurring IgM antibodies have been explored as therapeutics in clinical trials, and a new class of molecules, engineered IgM antibodies with enhanced binding and/or additional functional properties are being evaluated in humans. Here, we review the considerable progress that has been made regarding the understanding of biology, structure, function, manufacturing, and therapeutic potential of IgM antibodies since their discovery more than 80 years ago.

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Section: Introduction To Immunoglobulin M (Igm)mentioning

confidence: 99%

Structure, Function, and Therapeutic Use of IgM Antibodies

et al. 2020

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“…The tolerogenic intrauterine milieu under the direction of innate and adaptive influences reduces autoreactivity to self-antigen while preserving necessary responses against rare external pathogens. 28 In the first months of life, waning levels of regulatory T cells and transplacentally acquired IgG in conjunction with increased exposures to potentially pathogenic microbes markedly alters the infant's maturing immunologic environment. These early months provide a critical window for susceptibility to allergic disease.…”

Section: Primary Preventionmentioning

confidence: 99%

Preventing allergies through the skin

Winslow

Keet

2022

Annals of Allergy, Asthma & Immunology

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Immunology of the Fetus and Newborn

Cited by 2 publications

References 296 publications

Structure, Function, and Therapeutic Use of IgM Antibodies

Structure, Function, and Therapeutic Use of IgM Antibodies

Preventing allergies through the skin

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