I and i antigens of human peripheral blood lymphocytes cocap with receptors for concanavalin A.

Feizi, Ten; Kapadia, Anupsheela; Yount, WJ

doi:10.1073/pnas.77.1.376

Cited by 22 publications

(5 citation statements)

References 23 publications

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“…These compounds should therefore bind JCV. The ‘i’ antigen is expressed on a high proportion of human peripheral lymphocytes (Feizi et al, 1980). Glycan profiling by mass spectrometry has identified long glycans consistent with the LSTc motif in the N -glycan fractions of several human tissues including kidney, lung, and spleen (www.functionalglycomics.org), but tissues of the entire CNS were not analyzed.…”

Section: Discussionmentioning

confidence: 99%

Structure-Function Analysis of the Human JC Polyomavirus Establishes the LSTc Pentasaccharide as a Functional Receptor Motif

Neu

Maginnis

Palma

et al. 2010

Cell Host & Microbe

176

317

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SUMMARY The human JC polyomavirus (JCV) causes a fatal demyelinating disease, Progressive Multifocal Leukoencephalopathy (PML), in immunocompromised individuals. Current treatment options for PML are inadequate. Sialylated oligosaccharides and the serotonin receptor are known to be necessary for JCV entry, but the molecular interactions underlying JCV attachment remain unknown. Using glycan array screening and viral infectivity assays, we identify a linear sialylated pentasaccharide with the sequence NeuNAc-α2,6-Gal-β1,4-GlcNAc-β1,3-Gal-β1,4-Glc (LSTc) present on host glycoproteins and glycolipids as a specific JCV recognition motif. The crystal structure of the JCV capsid protein VP1 was solved alone and in complex with LSTc. It reveals extensive interactions with the terminal sialic acid of the LSTc motif and specific recognition of an extended conformation of LSTc. Mutations in the JCV oligosaccharide binding sites abolish cell attachment, viral spread and infectivity, further validating the importance of this interaction. Our findings provide a powerful platform for the development of antiviral compounds.

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Section: Discussionmentioning

confidence: 99%

Structure-Function Analysis of the Human JC Polyomavirus Establishes the LSTc Pentasaccharide as a Functional Receptor Motif

Neu

Maginnis

Palma

et al. 2010

Cell Host & Microbe

176

317

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“…However, cells with the i type sequences are abundant in inflammatory tissues. For example, monocytes and lymphocytes are rich in sialylated sequences not only of I type but also of i type (6,15,21). Thus, massive amounts of immunogenic complexes may form in the inflamed respiratory tract containing the lipid-rich mycoplasma (a potential adjuvant) and I-and i-active host cells, including epithelium, lymphocytes, and accessory cells.…”

Section: Discussionmentioning

confidence: 99%

Interaction of Mycoplasma pneumoniae with erythrocyte glycolipids of I and i antigen types

Loomes¹,

Uemura²,

Feizi³

1985

Infect Immun

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The role of sialoglycolipids (gangliosides) as receptors for the human pathogen Mycoplasma pneumoniae was investigated by using purified gangliosides of known carbohydrate structures as inhibitors of the binding of 51Cr-labeled erythrocytes to sheet cultures of M. pneumoniae. We found that sialoglycolipids with long carbohydrate backbones of the poly-N-acetyllactosamine type were more potent inhibitors of M. pneumoniae binding than those with short carbohydrate chains. This is in accord with earlier inhibition data for glycoproteins and oligosaccharides. Thus, the inhibitory activity of a fraction of bovine erythrocyte gangliosides containing long backbone structures of I antigen type was approximately 200 times greater than that of the short chain gangliosides GM3 and GTlb. The binding of M. pneumoniae to erythrocytes of I and i antigen types was found to be comparable, indicating that M. pneumoniae in its adhesive specificity may not distinguish between the branched carbohydrate backbones of I type and the linear structures of i type. Thus, the production of autoantibodies to the backbone structures of I type rather than i type after infection with this agent may simply reflect a greater abundance of branched carbohydrate receptors of I type on the surface of host cells with which the mycoplasma forms immunogenic complexes.

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“…In support of this hypothesis, chick galaptin has been shown to be mitogenic for murine lympho cytes [23,24]; galaptin-like lectin from the electric eel was reported to have therapeutic effects in experimental myasthenia gravis in rabbits [25]; galaptin isolated from calf tis sues has been shown to have a high affinity for lactosamine-type structures [26,27]; leu cocytes from various sources bear lactos amine-type structures on their cell surface [28,29]; and galaptins are secreted by var ious tissues [30].…”

Section: Introductionmentioning

confidence: 90%

Galactoside-Binding Lectin in Human Tissues

Allen

Piver

et al. 1987

Tumor Biol

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Lactose-inhibitable lectin activity has been analyzed by hemagglutination assay in a variety of human tissues and cells obtained at surgery and autopsy. The lectin activity was detected in surgically removed melanoma, sarcoma, colon carcinoma, breast carcinoma, adjacent non-malignant tissues, non-malignant tissues obtained at autopsy and in cells isolated from malignant effusions. Although, on average, malignant tissue had a higher hemag-glutinating titer than non-malignant tissue, similar tissues from different individuals varied widely in their apparent lectin content. The lectin was isolated from lung by affinity chro-matography and was found to have a native molecular mass of 31,000 daltons and a subunit molecular mass of 14,000 daltons. Utilizing rabbit anti-lung lectin serum in an immunohis-tochemical assay, the lectin was found to be distributed throughout the cytoplasm of lung epithelial cells. Ouchterlony immunodiffusion analysis confirmed the presence of this lectin in a variety of tissues and in some body fluids. In vitro metabolic radiolabelling experiments showed that the presence of lectin in tissues was most likely due to endogenous synthesis rather than absorption from body fluids. Lectin isolated from several tissues was found to bind to human buffy coat cell receptors.

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I and i antigens of human peripheral blood lymphocytes cocap with receptors for concanavalin A.

Cited by 22 publications

References 23 publications

Structure-Function Analysis of the Human JC Polyomavirus Establishes the LSTc Pentasaccharide as a Functional Receptor Motif

Structure-Function Analysis of the Human JC Polyomavirus Establishes the LSTc Pentasaccharide as a Functional Receptor Motif

Interaction of Mycoplasma pneumoniae with erythrocyte glycolipids of I and i antigen types

Galactoside-Binding Lectin in Human Tissues

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