This Article Full Text Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Reprints and Permissions Copyright Information Books from ASM Press MicrobeWorld Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Rivera Starr, C. Articles by Engleberg, N. C. Search for Related Content PubMed PubMed Citation Articles by Rivera Starr, C. Articles by Engleberg, N. C.

 Previous Article  |  Next Article 

Infection and Immunity, January 2006, p. 40-48, Vol. 74, No. 1
0019-9567/06/$08.00+0     doi:10.1128/IAI.74.1.40-48.2006
Copyright © 2006, American Society for Microbiology. All Rights Reserved.

Role of Hyaluronidase in Subcutaneous Spread and Growth of Group A Streptococcus

Clarise Rivera Starr¹ and N. Cary Engleberg^1,2*

Departments of Microbiology and Immunology,¹ Internal Medicine, University of Michigan Medical School, Ann Arbor, Michigan 48109²

Received 28 April 2005/ Returned for modification 23 July 2005/ Accepted 15 August 2005

Group A streptococcus (GAS) depends on a hyaluronic acid (HA) capsule to evade phagocytosis and to interact with epithelial cells. Paradoxically, GAS also produces hyaluronidase (Hyl), an enzyme that cleaves HA. A common assumption is that Hyl digests structurally identical HA in human tissue to promote bacterial spread. We inactivated the gene encoding extracellular hyaluronidase, hylA, in a clinical Hyl⁺ isolate. Hyl⁺ and an isogenic Hyl^– mutant were injected subcutaneously into mice with or without high-molecular-weight dextran blue. The Hyl^– strain produced small lesions with dye concentrated in close proximity. The Hyl⁺ strain produced identical lesions, but the dye diffused subcutaneously. However, Hyl⁺ bacteria were not isolated from unaffected skin stained by dye diffusion. Thus, Hyl digests tissue HA and facilitates spread of large molecules but is not sufficient to cause subcutaneous diffusion of bacteria or to affect lesion size. GAS capsule expression was assayed periodically during broth culture and was reduced in Hyl⁺ strains relative to Hyl^– strains at the onset and the end of active capsule synthesis but not during peak synthesis in mid-exponential phase. Thus, Hyl is not sufficiently active to remove capsule during peak synthesis. To demonstrate a possible nutritional role for Hyl, GAS was shown to grow with N-acetylglucosamine but not D-glucuronic acid (both components of HA) as a sole carbon source. However, only Hyl⁺ strains could grow utilizing HA as a sole carbon source, suggesting that Hyl may permit the organism to utilize host HA or its own capsule as an energy source.

---

* Corresponding author. Mailing address: University of Michigan Medical School, Department of Internal Medicine, 3116 TC, Ann Arbor, MI 48109-0378. Phone: (734) 936-5205. Fax: (734) 936-2737. E-mail: cengleb{at}umich.edu.

Editor: J. T. Barbieri

---

Infection and Immunity, January 2006, p. 40-48, Vol. 74, No. 1
0019-9567/06/$08.00+0     doi:10.1128/IAI.74.1.40-48.2006
Copyright © 2006, American Society for Microbiology. All Rights Reserved.

This article has been cited by other articles:

• Feng, Y., Li, M., Zhang, H., Zheng, B., Han, H., Wang, C., Yan, J., Tang, J., Gao, G. F. (2008). Functional Definition and Global Regulation of Zur, a Zinc Uptake Regulator in a Streptococcus suis Serotype 2 Strain Causing Streptococcal Toxic Shock Syndrome. J. Bacteriol. 190: 7567-7578 [Abstract] [Full Text]  
• Pecharki, D., Petersen, F. C., Scheie, A. Aa. (2008). Role of hyaluronidase in Streptococcus intermedius biofilm. Microbiology 154: 932-938 [Abstract] [Full Text]  
• Mishra, P., Akhtar, Md. S., Bhakuni, V. (2006). Unusual Structural Features of the Bacteriophage-associated Hyaluronate Lyase (hylp2). J. Biol. Chem. 281: 7143-7150 [Abstract] [Full Text]