Cloning and characterization of the bovine polymeric immunoglobulin receptor-encoding cDNA

Verbeet, Martin Ph.; Vermeer, Hendrika; Warmerdam, G.; Boer, H. H.; Lee, Sang He

doi:10.1016/0378-1119(95)00520-g

Cited by 32 publications

(13 citation statements)

References 21 publications

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“…DNA sequence information for pIgR is now available from several other species, including human (Eiffert et al, 1984;Davidson et al, 1988;Krajci et al, 1989Krajci et al, , 1992, mouse (Piskurich et al, 1995), cattle (Kulseth et al, 1995;Verbeet et al, 1995), rat (Banting et al, 1989), horse (Lewis et al, 2010), dog (Peters et al, 2003), pig (Kumura et al, 2000), possum (Adamski and Demmer, 1999), wallaby (Taylor et al, 2002), chicken (Wieland et al, 2004), frog (Braathen et al, 2007), and various fishes (Hamuro et al, 2007;Rombout et al, 2008;Feng et al, 2009;Xu et al, 2013). Further sequences have been revealed in genome sequencing projects.…”

Section: Pigr Genementioning

confidence: 94%

“…The amino acid sequences of pIgR have been determined or deduced for several species and are shown in Chapter 19 (Eiffert et al, 1984(Eiffert et al, , 1991Mostov et al, 1984;Banting et al, 1989;Kulseth et al, 1995;Verbeet et al, 1995;Piskurich et al, 1995;Adamski and Demmer, 1999;Kumura et al, 2000;Taylor et al, 2002;Peters et al, 2003;Wieland et al, 2004;Rombout et al, 2008;Braathen et al, 2007;Hamuro et al, 2007;Rombout et al, 2008;Feng et al, 2009;Lewis et al, 2010;Xu et al, 2013). In addition to the intrachain disulfide bonds that are thought to be buried within each domain, several of the domains have "extra" disulfide bonds.…”

Section: Primary Amino Acid Sequencementioning

confidence: 98%

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Mucosal Immunoglobulins

Woof

2015

Mucosal Immunology

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Section: Pigr Genementioning

confidence: 94%

Section: Primary Amino Acid Sequencementioning

confidence: 98%

Mucosal Immunoglobulins

Woof

2015

Mucosal Immunology

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“…In mammals and avian species, the mucosal Ig is transported by a polymeric Ig receptor (pIgR) 4 through the monolayer of epithelia into the mucosal secretions (1,2,(21)(22)(23)(24)(25). However, mammals and avian species do not express pIgR in the skin.…”

Section: A Teleost Polymeric Ig Receptor Exhibiting Two Ig-like Domaimentioning

confidence: 99%

A Teleost Polymeric Ig Receptor Exhibiting Two Ig-Like Domains Transports Tetrameric IgM into the Skin

Hamuro

Suetake

Saha³

et al. 2007

The Journal of Immunology

131

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The skin mucus IgM is an important molecule in the mucosal immune system of teleost skin. However, the transport mechanism associated with this molecule has yet to be clarified. In this study, we isolated a gene encoding a polymeric Ig receptor (pIgR) from a species of teleost fish, Takifugu rubripes (fugu). This gene is known to be an Ig transporter in the intestine of mammals. Our studies further demonstrated that fugu pIgR was expressed in the skin and that a fragment of pIgR bound to tetrameric IgM in the skin mucus. These results indicate that the skin pIgR transports tetrameric IgM into the skin mucus. The fugu pIgR exhibits a unique structure containing only two Ig-like domains corresponding to domain 1 and domain 4/5 of mammalian pIgR. This structure was sufficient for successful binding to tetrameric IgM. Teleost skin thus adopts the same Ig transport system as mammalian intestine via a unique pIgR.

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“…Alignment of the rat, mouse, human, rabbit and cattle predicted amino acid sequences demonstrated that pIgR is highly conserved both in amino acid sequence and structural organisation [82,103]. Subsequent alignment of the cytoplasmic tail of pIgR from cattle, men, rabbits, and rats reveals highly conserved areas that may reflect the importance of these regions for intracellular sorting of the receptor [5,50,103].…”

Section: Transport Of Piga Into the Mucosal Secretions By The Pigrmentioning

confidence: 99%

The IgA system: a comparison of structure and function in different species

2006

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-The predominant immunoglobulin isotype on most mucosal surfaces is secretory immunoglobulin A (SIgA), a polypeptide complex comprising two IgA monomers, the connecting J chain, and the secretory component. The molecular stability and strong anti-inflammatory properties make SIgA particularly well suited to provide protective immunity to the vulnerable mucosal surfaces by preventing invasion of inhaled and ingested pathogens. In contrast to SIgA, IgA in serum functions as an inflammatory antibody through interaction with FcαR on immune effector cells. Although IgA appears to share common features and protective functions in different species, significant variations exist within the IgA systems of different species. This review will give an overview of the basic concepts underlying mucosal IgA defence which will focus on the variations present among species in structure, antibody repertoire development, pIgR-mediated transport, colostral IgA content, hepatobiliary transport, and function with particular emphasis on the IgA system of the pig and dog. These interspecies variations emphasise the importance of elucidating and analysing the IgA system within the immune system of the species of interest rather than inferring roles from conclusions made in human and mouse studies.

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Cloning and characterization of the bovine polymeric immunoglobulin receptor-encoding cDNA

Cited by 32 publications

References 21 publications

Mucosal Immunoglobulins

Mucosal Immunoglobulins

A Teleost Polymeric Ig Receptor Exhibiting Two Ig-Like Domains Transports Tetrameric IgM into the Skin

The IgA system: a comparison of structure and function in different species

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