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Gene Review

scav-1  -  Protein SCAV-1

Caenorhabditis elegans

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Disease relevance of glycoprotein


High impact information on glycoprotein

  • We have previously reported the purification of the prototypic es transporter from human erythrocytes and have shown that this glycoprotein of apparent M, 55,000 is immunologically related to nucleoside transporters from several other species and tissues, including human placenta [6].
  • Wnt proteins are secreted, cysteine-rich glycoprotein ligands with numerous roles during animal development [7].
  • The soluble, 170 kDa glycoprotein occurs throughout Drosophila embryos, in microsomes of highly secretory Drosophila Kc cells and in small amounts in cell culture media [8].
  • Identification of the major soluble cuticular glycoprotein of lymphatic filarial nematode parasites (gp29) as a secretory homolog of glutathione peroxidase [9].
  • An extracellular matrix-associated glycoprotein expressed in a variety of tissues during embryogenesis and repair, SPARC contains modular domains that can function independently to bind cells and matrix components [10].

Biological context of glycoprotein

  • We have previously demonstrated that one such molecule, the phosphorylcholine-containing glycoprotein ES-62, acts to bias the immune response toward an anti-inflammatory/Th2 phenotype that is conducive to both worm survival and host health [11].
  • In this review we discuss the immunomodulatory effects of the phosphorylcholine-containing filarial nematode-secreted glycoprotein ES-62 and describe the intracellular signal transduction pathways it targets to achieve these effects [12].
  • Previous studies have shown that the secreted phosphorylcholine-containing glycoprotein of filarial nematodes, ES-62, is only present in the post-infective life-cycle stages, but that the mRNA is transcribed throughout the worm's life-cycle [13].
  • Linked to parasite-specific glycoprotein glycans or glycolipids, it is assumed to be responsible for a variety of immunological effects, including invasion mechanisms and long-term persistence of parasites within the host [14].
  • These findings have prompted the hypothesis that there could be additional glycoprotein hormones in vertebrate genomes [15].

Anatomical context of glycoprotein


Associations of glycoprotein with chemical compounds


Physical interactions of glycoprotein


Other interactions of glycoprotein

  • Molecular cloning and demonstration of an aminopeptidase activity in a filarial nematode glycoprotein [27].
  • Chemical degradation of one particular epitope recognized by monoclonal antibody PP1/117, and designated ep117, occurred after treatment with NaOH, periodate or Proteinase K, suggesting that an O-linked glycoprotein may be involved [28].
  • A glycoprotein analogous to viral fusion proteins has been identified on the surface of guinea pig sperm (PH-30/fertilin) and is implicated in sperm-egg fusion. adm-1 is the first reported invertebrate gene related to PH-30 and a family of proteins containing snake venom disintegrin- and metalloprotease-like domains [29].
  • This article is an attempt to provide, in an easily accessible format, a compilation of genes and cDNAs that have been sequenced and deposited in GenBank that encode transferase enzymes involved in eukaryotic glycoprotein or glycolipid biosynthesis [30].
  • Western- and lectin-blotting of the shed coat material demonstrated 2 prominent entities; a 90 kDa glycoprotein, which bound Datura stramonium agglutinin and was resistant to N- and O-glycanase treatment and a 47-60 kDa set of protein(s) [31].

Analytical, diagnostic and therapeutic context of glycoprotein

  • The T. spiralis beta-N-acetyl-D-hexosaminidase is a glycoprotein based on its binding to lentil-lectin Sepharose affinity column and its specific binding of concanavalin A on Western blots [32].
  • ES-62 is a PC-containing glycoprotein, which is secreted by the rodent filarial nematode Acanthocheilonema viteae and which provides a model system for the dissection of the mechanisms of immune evasion induced by related PC-containing glycoproteins expressed by human filarial nematodes [33].
  • Sequence alignments showed that the TM region of the nematode receptor has 30% identity and 50% similarity to the same region in mammalian glycoprotein hormone receptors [34].
  • Using pairwise sequence analysis of the complete human genome, we have identified two novel glycoprotein hormone subunit-related genes [35].


  1. Primary structure of and immunoglobulin E response to the repeat subunit of gp15/400 from human lymphatic filarial parasites. Paxton, W.A., Yazdanbakhsh, M., Kurniawan, A., Partono, F., Maizels, R.M., Selkirk, M.E. Infect. Immun. (1993) [Pubmed]
  2. Characterisation of an immunodominant glycoprotein antigen of Onchocerca volvulus with homologues in other filarial nematodes and Caenorhabditis elegans. Tree, T.I., Gillespie, A.J., Shepley, K.J., Blaxter, M.L., Tuan, R.S., Bradley, J.E. Mol. Biochem. Parasitol. (1995) [Pubmed]
  3. Coordinated Muc2 and Muc3 mucin gene expression in Trichinella spiralis infection in wild-type and cytokine-deficient mice. Shekels, L.L., Anway, R.E., Lin, J., Kennedy, M.W., Garside, P., Lawrence, C.E., Ho, S.B. Dig. Dis. Sci. (2001) [Pubmed]
  4. The childhood muscular dystrophies: making order out of chaos. Tsao, C.Y., Mendell, J.R. Seminars in neurology. (1999) [Pubmed]
  5. Proteomics computational analyses suggest that the carboxyl terminal glycoproteins of Bunyaviruses are class II viral fusion protein (beta-penetrenes). Garry, C.E., Garry, R.F. Theoretical biology & medical modelling [electronic resource]. (2004) [Pubmed]
  6. Cloning of a human nucleoside transporter implicated in the cellular uptake of adenosine and chemotherapeutic drugs. Griffiths, M., Beaumont, N., Yao, S.Y., Sundaram, M., Boumah, C.E., Davies, A., Kwong, F.Y., Coe, I., Cass, C.E., Young, J.D., Baldwin, S.A. Nat. Med. (1997) [Pubmed]
  7. Wnt signalling in Caenorhabditis elegans: regulating repressors and polarizing the cytoskeleton. Thorpe, C.J., Schlesinger, A., Bowerman, B. Trends Cell Biol. (2000) [Pubmed]
  8. Drosophila UDP-glucose:glycoprotein glucosyltransferase: sequence and characterization of an enzyme that distinguishes between denatured and native proteins. Parker, C.G., Fessler, L.I., Nelson, R.E., Fessler, J.H. EMBO J. (1995) [Pubmed]
  9. Identification of the major soluble cuticular glycoprotein of lymphatic filarial nematode parasites (gp29) as a secretory homolog of glutathione peroxidase. Cookson, E., Blaxter, M.L., Selkirk, M.E. Proc. Natl. Acad. Sci. U.S.A. (1992) [Pubmed]
  10. The biology of SPARC, a protein that modulates cell-matrix interactions. Lane, T.F., Sage, E.H. FASEB J. (1994) [Pubmed]
  11. Immunomodulation via novel use of TLR4 by the filarial nematode phosphorylcholine-containing secreted product, ES-62. Goodridge, H.S., Marshall, F.A., Else, K.J., Houston, K.M., Egan, C., Al-Riyami, L., Liew, F.Y., Harnett, W., Harnett, M.M. J. Immunol. (2005) [Pubmed]
  12. Signalling mechanisms underlying subversion of the immune response by the filarial nematode secreted product ES-62. Goodridge, H.S., Stepek, G., Harnett, W., Harnett, M.M. Immunology (2005) [Pubmed]
  13. Stage-specific and species-specific differences in the production of the mRNA and protein for the filarial nematode secreted product, ES-62. Stepek, G., Houston, K.M., Goodridge, H.S., Devaney, E., Harnett, W. Parasitology (2004) [Pubmed]
  14. Phosphorylcholine substituents in nematodes: structures, occurrence and biological implications. Lochnit, G., Dennis, R.D., Geyer, R. Biol. Chem. (2000) [Pubmed]
  15. Conservation of the heterodimeric glycoprotein hormone subunit family proteins and the LGR signaling system from nematodes to humans. Park, J.I., Semyonov, J., Chang, C.L., Hsu, S.Y. Endocrine (2005) [Pubmed]
  16. A filarial nematode secreted product differentially modulates expression and activation of protein kinase C isoforms in B lymphocytes. Deehan, M.R., Harnett, M.M., Harnett, W. J. Immunol. (1997) [Pubmed]
  17. Subversion of immunological signalling by a filarial nematode phosphorylcholine-containing secreted product. Goodridge, H.S., Deehan, M.R., Harnett, W., Harnett, M.M. Cell. Signal. (2005) [Pubmed]
  18. Induction of signalling anergy via the T-cell receptor in cultured Jurkat T cells by pre-exposure to a filarial nematode secreted product. Harnett, M.M., Deehan, M.R., Williams, D.M., Harnett, W. Parasite Immunol. (1998) [Pubmed]
  19. In vivo exposure of murine dendritic cell and macrophage bone marrow progenitors to the phosphorylcholine-containing filarial nematode glycoprotein ES-62 polarizes their differentiation to an anti-inflammatory phenotype. Goodridge, H.S., Marshall, F.A., Wilson, E.H., Houston, K.M., Liew, F.Y., Harnett, M.M., Harnett, W. Immunology (2004) [Pubmed]
  20. Inhibitory effects of human neutrophil functions by the 45-kD glycoprotein derived from the parasitic nematode Trichinella spiralis. Bruschi, F., Carulli, G., Azzarà, A., Homan, W., Minnucci, S., Rizzuti-Gullaci, A., Sbrana, S., Angiolini, C. Int. Arch. Allergy Immunol. (2000) [Pubmed]
  21. ES-62, an immunomodulator secreted by filarial nematodes, suppresses clonal expansion and modifies effector function of heterologous antigen-specific T cells in vivo. Marshall, F.A., Grierson, A.M., Garside, P., Harnett, W., Harnett, M.M. J. Immunol. (2005) [Pubmed]
  22. Isolation of messenger RNA coding for eggshell protein of the DNA-eliminating nematode Ascaris lumbricoides. Zulauf, E., Gut, C. Eur. J. Biochem. (1978) [Pubmed]
  23. High levels of protection induced by a 40-mer synthetic peptide vaccine against the intestinal nematode parasite Trichinella spiralis. Robinson, K., Bellaby, T., Chan, W.C., Wakelin, D. Immunology (1995) [Pubmed]
  24. Mechanisms underlying the transfer of phosphorylcholine to filarial nematode glycoproteins--a possible role for choline kinase. Houston, K.M., Harnett, W. Parasitology (1999) [Pubmed]
  25. An adherens junction protein is a member of the family of lactose-binding lectins. Chiu, M.L., Parry, D.A., Feldman, S.R., Klapper, D.G., O'Keefe, E.J. J. Biol. Chem. (1994) [Pubmed]
  26. Genetic evidence for a dystrophin-glycoprotein complex (DGC) in Caenorhabditis elegans. Grisoni, K., Martin, E., Gieseler, K., Mariol, M.C., Ségalat, L. Gene (2002) [Pubmed]
  27. Molecular cloning and demonstration of an aminopeptidase activity in a filarial nematode glycoprotein. Harnett, W., Houston, K.M., Tate, R., Garate, T., Apfel, H., Adam, R., Haslam, S.M., Panico, M., Paxton, T., Dell, A., Morris, H., Brzeski, H. Mol. Biochem. Parasitol. (1999) [Pubmed]
  28. Diversity and partial characterization of putative virulence determinants in Pasteuria penetrans, the hyperparasitic bacterium of root-knot nematodes (Meloidogyne spp.). Davies, K.G., Redden, M. J. Appl. Microbiol. (1997) [Pubmed]
  29. ADM-1, a protein with metalloprotease- and disintegrin-like domains, is expressed in syncytial organs, sperm, and sheath cells of sensory organs in Caenorhabditis elegans. Podbilewicz, B. Mol. Biol. Cell (1996) [Pubmed]
  30. Molecular cloning of eukaryotic glycoprotein and glycolipid glycosyltransferases: a survey. Field, M.C., Wainwright, L.J. Glycobiology (1995) [Pubmed]
  31. The surface coat of infective larvae of Trichinella spiralis. Modha, J., Roberts, M.C., Robertson, W.M., Sweetman, G., Powell, K.A., Kennedy, M.W., Kusel, J.R. Parasitology (1999) [Pubmed]
  32. Purification, characterization, and immunochemical studies of beta-N-acetyl-D-hexosaminidase from the parasitic nematode Trichinella spiralis. Rhoads, M.L. Mol. Biochem. Parasitol. (1988) [Pubmed]
  33. Modulation of the host immune system by phosphorylcholine-containing glycoproteins secreted by parasitic filarial nematodes. Harnett, W., Harnett, M.M. Biochim. Biophys. Acta (2001) [Pubmed]
  34. The nematode leucine-rich repeat-containing, G protein-coupled receptor (LGR) protein homologous to vertebrate gonadotropin and thyrotropin receptors is constitutively active in mammalian cells. Kudo, M., Chen, T., Nakabayashi, K., Hsu, S.Y., Hsueh, A.J. Mol. Endocrinol. (2000) [Pubmed]
  35. Evolution of glycoprotein hormone subunit genes in bilateral metazoa: identification of two novel human glycoprotein hormone subunit family genes, GPA2 and GPB5. Hsu, S.Y., Nakabayashi, K., Bhalla, A. Mol. Endocrinol. (2002) [Pubmed]
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