Paired Ig-like receptor homologs in birds and mammals share a common ancestor with mammalian Fc receptors

Dennis, Glynn; Kubagawa, Hiromi; Cooper, Max D.

doi:10.1073/pnas.230442897

Cited by 77 publications

(69 citation statements)

References 58 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Initially, the CHIR genes have been isolated by using homology searches with mouse PIR-B probes in the chicken EST database (20). Reciprocally mouse PIR-B itself was cloned in an attempt to find a homologue of the human Fc␣RI (CD89) (21).…”

Section: Discussionmentioning

confidence: 99%

The chicken leukocyte receptor complex encodes a primordial, activating, high-affinity IgY Fc receptor

Viertlboeck

Schweinsberg

Hanczaruk

et al. 2007

Proc. Natl. Acad. Sci. U.S.A.

View full text Add to dashboard Cite

show abstract

Section: Discussionmentioning

confidence: 99%

The chicken leukocyte receptor complex encodes a primordial, activating, high-affinity IgY Fc receptor

Viertlboeck

Schweinsberg

Hanczaruk

et al. 2007

Proc. Natl. Acad. Sci. U.S.A.

View full text Add to dashboard Cite

show abstract

“…Design, Construction, and Expression of bFc␥2R MutantsBovine Fc␥2R is a member of the Ig gene superfamily of proteins and is closely related to several human members of this family, including the KIRs, Ig-like transcripts, and the human Fc␣R (CD89) (14). Several three-dimensional structures of KIR proteins have now been described, thus identifying the secondary structure composition of the Ig domains.…”

Section: Panel F)mentioning

confidence: 99%

“…The genes of the LRC are only slightly less closely related genetically to the other mammalian FcRs than they are to each other. Moreover, available crystal data suggest that proteins encoded in the LRC are structurally quite similar to FcRs (Fc␥RII, III, and Fc⑀RI) (14). However, despite this high degree of homology, the location of the ligand binding sites within these molecules varies considerably.…”

Section: Fig 2 Alignment Of the Protein Sequences Of Bfc␥2r And P58mentioning

confidence: 99%

“…In addition, there is a novel type of Fc␥R specific for bIgG2, termed bFc␥2R (13). This FcR is genetically more closely related to a novel family of human proteins that includes Fc␣RI (CD89) and the KIR, monocyte/ macrophage Ig-like receptor, and Ig-like transcripts/LIR families of receptors, which all probably arose by a series of duplication events from a single ancestral gene (14).…”

mentioning

confidence: 99%

See 1 more Smart Citation

Identification of Residues within the Extracellular Domain 1 of Bovine Fcγ2R Essential for Binding Bovine IgG2

Morton

Howard²,

Storset

et al. 2001

Journal of Biological Chemistry

View full text Add to dashboard Cite

Neutrophils and monocytes in cattle express a novel class of immunoglobulin Fc receptor, specific for bovine IgG2 (bIgG2), termed bFc␥2R. In cows, the ability of neutrophils to kill immunoglobulin-opsonized microorganisms appears to depend largely on this subclass, whose interaction with bFc␥2R initiates the killing process. bFc␥2R is a transmembrane glycoprotein consisting of two extracellular immunoglobulin-like domains, followed by a 19-amino acid membrane-spanning region and a short cytoplasmic tail. Although related to other mammalian Fc␥Rs, bFc␥2R belongs to a novel gene family that includes the human killer cell inhibitory receptor and Fc␣RI (CD89) proteins. We have shown previously (Morton, H. C., van Zandbergen, G., van Kooten, C., Howard, C. J., van de Winkel, J. G., and Brandtzaeg, P. (1999) J. Exp. Med. 189, 1715-1722) that like these proteins (and unlike other Fc␥Rs), bFc␥2R binds bIgG2 via the membrane-distal extracellular domain 1 (EC1). In this present study, we introduced mutations into the predicted loop regions of the EC1 domain and assayed the resulting bFc␥2R mutants for their ability to bind bIgG2. Our results indicated that the bIgG2 binding site lies within the predicted F-G loop region of the EC1 domain. Furthermore, single amino acid mutational analysis of this region identified Phe-82 and Trp-87 as being critical for bIgG2 binding.

show abstract

“…3). Dennis et al (2000) have originally suggested that Fc and LRC sequences share a common ancestor. These authors have pointed out that, despite the low degree of sequence similarity, the tertiary structures of the Ig-like domains encoded by the FcγRIIB (D2 of group FcII in Fig.…”

mentioning

confidence: 99%

Origin and evolution of the Ig-like domains present in mammalian leukocyte receptors: insights from chicken, frog, and fish homologues

2005

View full text Add to dashboard Cite

In mammals many natural killer (NK) cell receptors, encoded by the leukocyte receptor complex (LRC), regulate the cytotoxic activity of NK cells and provide protection against virus-infected and tumor cells. To investigate the origin of the Ig-like domains encoded by the LRC genes, a subset of C2-type Ig-like domain sequences was compiled from mammals, birds, amphibians, and fish. Phylogenetic analysis of these sequences generated seven monophyletic groups in mammals (MI, MII, and FcI, FcIIa, FcIIb, FcIII, FcIV), two in chicken (CI, CII), four in frog (FI-FIV), and five in zebrafish (ZI-ZV). The analysis of the major groups supported the following order of divergence: ZI [or a common ancestor of ZI and F (a cluster composed of the FcIII and FIII groups)], F, CII (or a common ancestor of CII and MII), MII, and MI-CI. The relationships of the remaining groups were unclear, since the phylogenetic positions of these groups were not supported by high bootstrap values. Two main conclusions can be drawn from this analysis. First, the two groups of mammalian LRC sequences must diverged before the separation of the avian and mammalian lineages. Second, the mammalian LRC sequences are most closely related to the Fc receptor sequences and these two groups diverged before the separation of birds and mammals. KeywordsLeukocyte receptor complex; Chicken Ig-like receptors; Fc receptors; Ig-like domain groupsThe mammalian natural killer (NK) cell receptors fall into two categories, one category belonging to the immunoglobulin superfamily (IgSF) and the other to the C-type lectin superfamily. The Ig-like receptors occupy a genomic region called the leukocyte receptor complex (LRC; Trowsdale et al. 2001). In mammals, the LRC contains several gene families including the killer cell Ig-like receptors (KIR), the leukocyte Ig-like receptors (LILR), and the paired Ig-like receptors (PIR), which form species-specific evolutionary clusters (Martin et al. 2002). Singleton genes have been identified in the LRC of humans, artiodactyls, and rodents (Hoelsbrekken et al. 2003;Maruoka et al. 2004;Morton et al. 2004). The presence of the LRC in all mammals so far studied suggests that this region formed before the mammalian radiation. Evolution of the LRC genes has thus far been studied mainly in mammalian species for which gene sequences have been available (Volz et al. 2001;Hughes 2002;Martin et al. 2002). Here we investigate the origin of Ig-like domains encoded by the mammalian LRC genes using recently generated homologous sequences from chicken, frog, and fish. . BLAST searching was conducted by using high expected E-values (E=10) to ensure that most sequences homologous to the mammalian LRC genes would be retrieved. The resulting BLAST hits were sorted according to the E-value and the coverage of the query sequence. Only hits covering at least 85 amino acid residues (the minimum length of the C2-type Ig-like domain; Klein and Hořejší 1997) were used for further analysis. Gene structures were predicted by using GenomeScan (Yeh et ...

show abstract

Paired Ig-like receptor homologs in birds and mammals share a common ancestor with mammalian Fc receptors

Cited by 77 publications

References 58 publications

The chicken leukocyte receptor complex encodes a primordial, activating, high-affinity IgY Fc receptor

The chicken leukocyte receptor complex encodes a primordial, activating, high-affinity IgY Fc receptor

Identification of Residues within the Extracellular Domain 1 of Bovine Fcγ2R Essential for Binding Bovine IgG2

Origin and evolution of the Ig-like domains present in mammalian leukocyte receptors: insights from chicken, frog, and fish homologues

Contact Info

Product

Resources

About