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Infection and Immunity, July 2006, p. 4200-4213, Vol. 74, No. 7
0019-9567/06/$08.00+0     doi:10.1128/IAI.00493-06
Copyright © 2006, American Society for Microbiology. All Rights Reserved.

Identification and Characterization of an Antigen I/II Family Protein Produced by Group A Streptococcus

Shizhen Zhang,1 Nicole M. Green,1,2 Izabela Sitkiewicz,1 Rance B. LeFebvre,2 and James M. Musser1*

Center for Molecular and Translational Human Infectious Diseases Research, The Methodist Hospital Research Institute, and Department of Pathology, The Methodist Hospital, Houston, Texas 77030,1 Department of Pathology, Microbiology, and Immunology, University of California at Davis, Davis, California 956162

Received 27 March 2006/ Returned for modification 14 April 2006/ Accepted 24 April 2006

Group A Streptococcus (GAS) is a gram-positive human bacterial pathogen that causes infections ranging in severity from pharyngitis to life-threatening invasive disease, such as necrotizing fasciitis. Serotype M28 strains are consistently isolated from invasive infections, particularly puerperal sepsis, a severe infection that occurs during or after childbirth. We recently sequenced the genome of a serotype M28 GAS strain and discovered a novel 37.4-kb foreign genetic element designated region of difference 2 (RD2). RD2 is similar in gene content and organization to genomic islands found in group B streptococci (GBS), the major cause of neonatal infections. RD2 encodes seven proteins with conventional gram-positive secretion signal sequences, six of which have not been characterized. Herein, we report that one of these six proteins (M28_Spy1325; Spy1325) is a member of the antigen I/II family of cell surface-anchored molecules produced by oral streptococci. PCR and DNA sequence analysis found that Spy1325 is very well conserved in GAS strains of distinct M protein serotypes. As assessed by real-time TaqMan quantitative PCR, the Spy1325 gene was expressed in vitro, and Spy1325 protein was present in culture supernatants and on the GAS cell surface. Western immunoblotting and enzyme-linked immunosorbent assays indicated that Spy1325 was produced by GAS in infected mice and humans. Importantly, the immunization of mice with recombinant Spy1325 fragments conferred protection against GAS-mediated mortality. Similar to other antigen I/II proteins, recombinant Spy1325 bound purified human salivary agglutinin glycoprotein. Spy1325 may represent a shared virulence factor among GAS, GBS, and oral streptococci.

* Corresponding author. Mailing address: Center for Molecular and Translational Human Infectious Diseases Research, The Methodist Hospital Research Institute, The Methodist Hospital, B154, 6565 Fannin St., Houston, TX 77030. Phone: (713) 441-5890. Fax: (713) 790-6460. E-mail: jmmusser{at}tmh.tmc.edu.

Editor: D. L. Burns

Infection and Immunity, July 2006, p. 4200-4213, Vol. 74, No. 7
0019-9567/06/$08.00+0     doi:10.1128/IAI.00493-06
Copyright © 2006, American Society for Microbiology. All Rights Reserved.



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