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Infection and Immunity, October 2005, p. 6237-6248, Vol. 73, No. 10
0019-9567/05/$08.00+0     doi:10.1128/IAI.73.10.6237-6248.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

Inhibition of Cell Surface Export of Group A Streptococcal Anchorless Surface Dehydrogenase Affects Bacterial Adherence and Antiphagocytic Properties

Laboratory of Bacterial Pathogenesis, Public Health Research Institute at The International Center for Public Health, 225 Warren Street, Newark, New Jersey 07103-3535

Received 2 May 2005/ Returned for modification 13 June 2005/ Accepted 12 July 2005

Surface dehydrogenase (SDH) is an anchorless, multifunctional protein displayed on the surfaces of group A Streptococcus (GAS) organisms. SDH is encoded by a single gene, sdh (gap or plr) that is essential for bacterial survival. Hence, the resulting nonfeasibility of creating a knockout mutant is a major limiting factor in studying its role in GAS pathogenesis. An insertion mutagenesis strategy was devised in which a nucleotide sequence encoding a hydrophobic tail of 12 amino acids (³³⁷IVLVGLVMLLLS³⁴⁸) was added at the 3' end of the sdh gene, successfully creating a viable mutant strain (M1-SDH_HBtail). In this mutant strain, the SDH_HBtail protein was not secreted in the medium but was retained in the cytoplasm and to some extent trapped within the cell wall. Hence, SDH_HBtail was not displayed on the GAS surface. The mutant strain, M1-SDH_HBtail, grew at the same rate as the wild-type strain. The SDH_HBtail protein displayed the same GAPDH activity as the wild-type SDH protein. Although the whole-cell extracts of the wild-type and mutant strains showed similar GAPDH activities, cell wall extracts of the mutant strain showed 5.5-fold less GAPDH activity than the wild-type strain. The mutant strain, M1-SDH_HBtail, bound significantly less human plasminogen, adhered poorly to human pharyngeal cells, and lost its innate antiphagocytic activity. These results indicate that the prevention of the cell surface export of SDH affects the virulence properties of GAS. The anchorless SDH protein, thus, is an important virulence factor.

Editor: J. N. Weiser

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