title: Ability of hyaluronidase 2 to degrade extracellular hyaluronan is not required for its function as a receptor for jaagsiekte sheep retrovirus.
abstract: Jaagsiekte sheep retrovirus (JSRV) uses hyaluronidase 2 (Hyal2) as a cell entry receptor. By making inactivating mutations to the catalytic residues of human Hyal2, we found that hyaluronidase activity was dispensable for its receptor function. The affinities of the JSRV envelope glycoprotein for Hyal2 and the Hyal2 mutant were similar, and hyaluronan did not block either high-affinity interaction or virus infection. While generating the Hyal2 mutant, we discovered that our previous analysis of the hyaluronidase activity of Hyal2 was affected by a contaminating hyaluronan lyase, which we have identified as the occlusion-derived baculovirus E66 protein of the recombinant baculovirus used to produce Hyal2. We now report that purified human Hyal2 is a weak acid-active hyaluronidase.
authors.affiliation: Fred Hutchinson Cancer Research Center, 1100 Fairview Avenue N., Seattle, WA 98109-1024, USA.
authors.forename: Vladimir
authors.initials: V
authors.lastname: Vigdorovich
authors.forename: A Dusty
authors.initials: AD
authors.lastname: Miller
authors.forename: Roland K
authors.initials: RK
authors.lastname: Strong
mesh_terms: D000143:Acids; D000818:Animals; D016367:Baculoviridae / Q000502:physiology; D002460:Cell Line; D015971:Gene Expression Regulation, Enzymologic; D005822:Genetic Vectors / Q000235:genetics; D006820:Hyaluronic Acid / Q000378:metabolism*; D006821:Hyaluronoglucosaminidase / Q000235:genetics / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D007074:Immunoglobulin G / Q000276:immunology; D022141:Jaagsiekte sheep retrovirus / Q000235:genetics / Q000378:metabolism*; D007700:Kinetics; D009154:Mutation / Q000235:genetics; D011485:Protein Binding; D011991:Receptors, Virus / Q000378:metabolism; D012995:Solubility
chemical_list: D000143:Acids; D007074:Immunoglobulin G; D011991:Receptors, Virus; D006820:Hyaluronic Acid; D006821:Hyaluronoglucosaminidase