Cloning and sequencing of a novel human gene which encodes a putative hydroxylase

Iriyama, Chisako; Matsuda, Satoru; Katsumata, Ryu; Hamaguchi, Michinari

doi:10.1007/s100380170081

Cited by 16 publications

(22 citation statements)

References 6 publications

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“…It was initially identified based on its ability to bind MAWD (MAPK activator with WD-repeats), a protein that may be involved in cell signaling pathways (Matsuda et al, 2000). Consistent with previous reports (Iriyama et al, 2001), we detected mRNA for MAWD-BP in all tissues tested, including synoviocytes, suggesting that this protein is ubiquitously expressed. However, it was not bound in vitro by all six antibiotic-refractory associated DRB molecules.…”

Section: Discussionsupporting

confidence: 92%

“…The most promising self-peptide appeared to be MAWD-BP 280−288 , which shares eight of the nine core amino acid residues with the spirochetal peptide. Little is known about this human protein (Iriyama et al, 2001). It was initially identified based on its ability to bind MAWD (MAPK activator with WD-repeats), a protein that may be involved in cell signaling pathways (Matsuda et al, 2000).…”

Section: Discussionmentioning

confidence: 99%

“…Though MAWD-BP and T-span7 were previously shown to be expressed in multiple tissues (Iriyama et al, 2001;Takagi et al, 1995), it was unknown whether either was expressed in joint tissue (e.g. synoviocytes), or whether MAWD-BP was expressed by any immune cells.…”

Section: Tissue Expression Of Candidate Autoantigensmentioning

confidence: 99%

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Human homologues of a Borrelia T cell epitope associated with antibiotic-refractory Lyme arthritis

Drouin

Glickstein

Kwok

et al. 2008

Molecular Immunology

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Antibiotic-refractory Lyme arthritis, which may result from infection-induced autoimmunity, is associated with HLA-DR molecules that bind an epitope of Borrelia burgdorferi (Bb) outer-surface protein A (OspA 165−173 ) and with T cell reactivity with this epitope. One potential mechanism to explain these associations is molecular mimicry between OspA 165−173 and a self-peptide. Here, we searched the published human genome for peptides with sequence homology with OspA 165−173 . The two peptides identified with the greatest sequence homology with the OspA epitope were MAWD-BP 276−288 , which had identity at eight of the nine core amino acid residues, and T-span7 58−70 , which had identity at six residues. MAWD-BP mRNA was expressed by synoviocytes, while T-span7 mRNA was not. However, neither peptide bound all of the HLA-DR molecules associated with antibiotic-refractory Lyme arthritis. Among 11 patients, nine had T cell reactivity with OspA 161−170 , six had responses to MAWD-BP 276−288 , and three had reactivity with T-span7 58−70 , but reactivity with the self-peptides was lower than that induced by the spirochetal epitope. Thus, there remains an association between OspA 165−173 and antibiotic-refractory Lyme arthritis, and infection-induced autoimmunity is an attractive hypothesis to explain this outcome. However, molecular mimicry due to sequence homology between OspA 165−173 and a human peptide seems unlikely to be the critical mechanism.

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Section: Discussionsupporting

confidence: 92%

Section: Discussionmentioning

confidence: 99%

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Human homologues of a Borrelia T cell epitope associated with antibiotic-refractory Lyme arthritis

Drouin

Glickstein

Kwok

et al. 2008

Molecular Immunology

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“…The immune response to these homologous peptides provides a species-dependent and regionspecific explanation for Borrelia-induced autoimmunity in post-Lyme arthritis, which is more prevalent in the United States than in Europe. [31][32][33] In a similar mode, infection-induced autoimmunity in Borrelia-associated early-onset morphea might be influenced by the genetic heterogeneity of B burgdorferi or depend on certain immunogenic factors that may vary between different Borrelia species or geographic Borrelia populations and thus explain regional differences in the geographical prevalence of this novel disease entity.…”

Section: Discussionmentioning

confidence: 94%

“Borrelia-associated early-onset morphea”: A particular type of scleroderma in childhood and adolescence with high titer antinuclear antibodies?

Prinz¹,

Kutasi²,

Weisenseel³

et al. 2009

Journal of the American Academy of Dermatology

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“…2D), suggesting that the unknown substrate is deprotonated by glutamic acid and reprotonated by cysteine. A second related sequence, MAWD-binding protein (MAWDBP) (30), is of human origin and was identified in a two-hybrid screen for binding partners of the WD-40 domains of MAWD (putative human mitogen-activated protein kinase activator with WD repeats), a protein that may be involved in breast cancer (31). MAWDBP shares 22% identity with PhzF, and its active site contains the basic cysteine residue, making it similar to YddE from E. coli.…”

Section: Resultsmentioning

confidence: 99%

Structure and function of the phenazine biosynthetic protein PhzF from Pseudomonas fluorescens

Blankenfeldt

Kuzin

Skarina

et al. 2004

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

124

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Phenazines produced by Pseudomonas and Streptomyces spp. are heterocyclic nitrogen-containing metabolites with antibiotic, antitumor, and antiparasitic activity. The antibiotic properties of pyocyanin, produced by Pseudomonas aeruginosa, were recognized in the 1890s, although this blue phenazine is now known to be a virulence factor in human disease. Despite their biological significance, the biosynthesis of phenazines is not fully understood. Here we present structural and functional studies of PhzF, an enzyme essential for phenazine synthesis in Pseudomonas spp. PhzF shares topology with diaminopimelate epimerase DapF but lacks the same catalytic residues. The structure of PhzF in complex with its substrate, trans-2,3-dihydro-3-hydroxyanthranilic acid, suggests that it is an isomerase using the conserved glutamate E45 to abstract a proton from C3 of the substrate. The proton is returned to C1 of the substrate after rearrangement of the double-bond system, yielding an enol that converts to the corresponding ketone. PhzF is a dimer that may be bifunctional, providing a shielded cavity for ketone dimerization via double Schiff-base formation to produce the phenazine scaffold. Our proposed mechanism is supported by mass and NMR spectroscopy. The results are discussed in the context of related structures and protein sequences of unknown biochemical function.active site residues ͉ catalytic activity ͉ x-ray structure

show abstract

Cloning and sequencing of a novel human gene which encodes a putative hydroxylase

Cited by 16 publications

References 6 publications

Human homologues of a Borrelia T cell epitope associated with antibiotic-refractory Lyme arthritis

Human homologues of a Borrelia T cell epitope associated with antibiotic-refractory Lyme arthritis

“Borrelia-associated early-onset morphea”: A particular type of scleroderma in childhood and adolescence with high titer antinuclear antibodies?

Structure and function of the phenazine biosynthetic protein PhzF from Pseudomonas fluorescens

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