This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Vigdorovich, V.
Right arrow Articles by Strong, R. K.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Vigdorovich, V.
Right arrow Articles by Strong, R. K.

 Previous Article  |  Next Article 

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.



This article has been cited by other articles:

  • Jadin, L., Wu, X., Ding, H., Frost, G. I., Onclinx, C., Triggs-Raine, B., Flamion, B. (2008). Skeletal and hematological anomalies in HYAL2-deficient mice: a second type of mucopolysaccharidosis IX?. FASEB J. 22: 4316-4326 [Abstract] [Full Text]  
  • Orimoto, A. M., Dumaresq-Doiron, K., Jiang, J.-Y., Tanphaichitr, N., Tsang, B. K., Carmona, E. (2008). Mammalian Hyaluronidase Induces Ovarian Granulosa Cell Apoptosis and Is Involved in Follicular Atresia. Endocrinology 149: 5835-5847 [Abstract] [Full Text]  
  • Monzon, M. E., Manzanares, D., Schmid, N., Casalino-Matsuda, S. M., Forteza, R. M. (2008). Hyaluronidase Expression and Activity Is Regulated by Pro-Inflammatory Cytokines in Human Airway Epithelial Cells. Am. J. Respir. Cell Mol. Bio. 39: 289-295 [Abstract] [Full Text]  
  • Cote, M., Zheng, Y.-M., Albritton, L. M., Liu, S.-L. (2008). Fusogenicity of Jaagsiekte Sheep Retrovirus Envelope Protein Is Dependent on Low pH and Is Enhanced by Cytoplasmic Tail Truncations. J. Virol. 82: 2543-2554 [Abstract] [Full Text]  


Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»