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Journal of Virology, April 2007, p. 3124-3129, Vol. 81, No. 7
0022-538X/07/$08.00+0     doi:10.1128/JVI.02177-06
Copyright © 2007, American Society for Microbiology. All Rights Reserved.

Ability of Hyaluronidase 2 To Degrade Extracellular Hyaluronan Is Not Required for Its Function as a Receptor for Jaagsiekte Sheep Retrovirus{triangledown}

Vladimir Vigdorovich,1,2 A. Dusty Miller,1,3* and Roland K. Strong3

Division of Human Biology,1 Molecular and Cellular Biology Program,2 Division of Basic Sciences, Fred Hutchinson Cancer Research Center, Seattle, Washington 981093

Received 4 October 2006/ Accepted 6 January 2007

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.

* Corresponding author. Mailing address: Fred Hutchinson Cancer Research Center, 1100 Fairview Ave. N., Room C2-105, P.O. Box 19024, Seattle, WA 98109-1024. Phone: (206) 667-2890. Fax: (206) 667-6523. E-mail: dmiller{at}fhcrc.org.

{triangledown} Published ahead of print on 17 January 2007.

Journal of Virology, April 2007, p. 3124-3129, Vol. 81, No. 7
0022-538X/07/$08.00+0     doi:10.1128/JVI.02177-06
Copyright © 2007, American Society for Microbiology. All Rights Reserved.



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