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Infection and Immunity, January 1999, p. 50-56, Vol. 67, No. 1
Department of Microbiology and Immunology,
Wake Forest University School of Medicine, Winston-Salem, North
Carolina
Received 22 June 1998/Returned for modification 11 September
1998/Accepted 6 October 1998
Streptococcus defectivus is one of the nutritionally
variant streptococci, a class of viridans group streptococci first
isolated from patients with endocarditis and otitis media. In previous studies, NVS-47, a clinical isolate of S. defectivus, was
shown to bind to the extracellular matrix. A high-molecular-weight
surface protein was identified and proposed to be responsible for
mediating this binding. In the present study, the gene encoding this
protein was identified by transposon mutagenesis and characterized. The gene (emb) was found to be larger than 14 kb and was
partially sequenced. It encodes a protein containing at least 50 repeats of 77 amino acids predicted to assume an alternating
coiled-coil conformation. The domain responsible for extracellular
matrix binding was mapped to the N terminus of the protein. From
sequence analysis, Emb is proposed to be the prototype of a new family of streptococcal fibrillar proteins.
0019-9567/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.
Characterization of emb, a Gene Encoding
the Major Adhesin of Streptococcus defectivus
and
*
Corresponding author. Mailing address: Wake Forest
University School of Medicine, Medical Center Blvd., Winston-Salem, NC 27157. Phone: (336) 716-2263. Fax: (336) 716-4204. E-mail:
ivr{at}wfubmc.edu.
Present address: Department of Microbiology, Public Health Research
Institute, New York, N.Y.
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