ArticleJournal of virology2005
Expression and characterization of a soluble, active form of the jaagsiekte sheep retrovirus receptor, Hyal2.
Article in Journal of virology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 22 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
22 citing papers in PubMed, 46 citations in OpenAlex.
- Genetic Deficiencies of Hyaluronan Degradation.Cells · 2024Review
- TMEM2: A missing link in hyaluronan catabolism identified?Matrix biology : journal of the International Society for Matrix Biology · 2019Review
- Endothelial Glycocalyx as a Shield Against Diabetic Vascular Complications: Involvement of Hyaluronan and Hyaluronidases.Arteriosclerosis, thrombosis, and vascular biology · 2018Review
- A mammalian homolog of the zebrafish transmembrane protein 2 (TMEM2) is the long-sought-after cell-surface hyaluronidase.The Journal of biological chemistry · 2017Article
- Hyaluronidase-1 Is Mainly Functional in the Upper Granular Layer, Close to the Epidermal Barrier.The Journal of investigative dermatology · 2015Article
- CD44 knock-down in bovine and human chondrocytes results in release of bound HYAL2.Matrix biology : journal of the International Society for Matrix Biology · 2015Article
- Hyaluronidase 2: a novel germ cell hyaluronidase with epididymal expression and functional roles in mammalian sperm.Biology of reproduction · 2014Article
- Emerging roles for hyaluronidase in cancer metastasis and therapy.Advances in cancer research · 2014Review
- Experimental transmission of enzootic nasal adenocarcinoma in sheep.Veterinary research · 2013Article
- The soluble form of the EIAV receptor encoded by an alternative splicing variant inhibits EIAV infection of target cells.PloS one · 2013Article
- Receptor binding and low pH coactivate oncogenic retrovirus envelope-mediated fusion.Journal of virology · 2009Article
- Enzootic nasal tumor virus envelope requires a very acidic pH for fusion activation and infection.Journal of virology · 2008Article
- Hyaluronidase 2 and its intriguing role as a cell-entry receptor for oncogenic sheep retroviruses.Seminars in cancer biology · 2008Review
- Fusogenicity of Jaagsiekte sheep retrovirus envelope protein is dependent on low pH and is enhanced by cytoplasmic tail truncations.Journal of virology · 2008Article
- Isoenzyme-specific differences in the degradation of hyaluronic acid by mammalian-type hyaluronidases.Glycoconjugate journal · 2008Article
- Evaluation of the 3p21.3 tumour-suppressor gene cluster.Oncogene · 2007Review
- Ability of hyaluronidase 2 to degrade extracellular hyaluronan is not required for its function as a receptor for jaagsiekte sheep retrovirus.Journal of virology · 2007Article
- Review
- Mouse testicular hyaluronidase-like proteins SPAM1 and HYAL5 but not HYALP1 degrade hyaluronan.The Biochemical journal · 2007Article
- Expression and cellular localization of human hyaluronidase-2 in articular chondrocytes and cultured cell lines.Osteoarthritis and cartilage · 2006Article
Corrections and comments
- Erratum issued
- Erratum issued
Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Retrovirus entry into cells is mediated by specific interactions between virus envelope glycoproteins and cell surface receptors. Many of these receptors contain multiple membrane-spanning regions, making their purification and study difficult. The jaagsiekte sheep retrovirus (JSRV) receptor, hyaluronidase 2 (Hyal2), is a glycosylphosphatidylinositol (GPI)-anchored molecule containing no peptide transmembrane regions, making it an attractive candidate for study of retrovirus entry. Further, the hyaluronidase activity reported for human Hyal2, combined with its broad expression pattern, may point to a critical function of Hyal2 in the turnover of hyaluronan, a major extracellular matrix component. Here we describe the properties of a soluble form of human Hyal2 (sHyal2) purified from a baculoviral expression system. sHyal2 is a 54-kDa monomer with weak hyaluronidase activity compared to that of the known hyaluronidase Spam1. In contrast to a previous report indicating that Hyal2 cleaved hyaluronan to a limit product of 20 kDa and was active only at acidic pH, we find that sHyal2 is capable of further degradation of hyaluronan and is active over a broad pH range, consistent with Hyal2 being active at the cell surface where it is normally localized. Interaction of sHyal2 with the JSRV envelope glycoprotein was analyzed by viral inhibition assays, showing >90% inhibition of transduction at 28 nM sHyal2, and by surface plasmon resonance, revealing a remarkably tight specific interaction with a dissociation constant (KD) of 32 +/- 1 pM. In contrast to results obtained with avian retroviruses, purified receptor was not capable of promoting transduction of cells that do not express the virus receptor.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.