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Updated: Aug 18, 2026

In Vitro Assay of Bacterial Adhesion onto Mammalian Epithelial Cells
Published on: May 16, 2011
Characterization of emb, a gene encoding the major adhesin of Streptococcus defectivus
1Department of Microbiology and Immunology, Wake Forest University School of Medicine, Winston-Salem, North Carolina, USA.
Abstract:
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.
Insights
Streptococcus defectivus possesses a large surface protein, Emb, responsible for binding to the extracellular matrix. This protein, encoded by the emb gene, may represent a new family of streptococcal fibrillar proteins.
Area of Science:
- Microbiology
- Molecular Biology
- Protein Science
Background:
- Streptococcus defectivus belongs to nutritionally variant streptococci (NVS), linked to endocarditis and otitis media.
- Previous research indicated NVS-47, an S. defectivus isolate, binds to the extracellular matrix via a high-molecular-weight surface protein.
Purpose of the Study:
- To identify and characterize the gene encoding the extracellular matrix-binding protein in S. defectivus.
- To elucidate the structure and function of this novel surface protein.
Main Methods:
- Transposon mutagenesis was employed to identify the relevant gene.
- Partial gene sequencing of the identified gene (emb) was performed.
- Bioinformatic analysis predicted protein structure and identified functional domains.
Main Results:
- The gene emb, encoding a protein over 14 kb, was identified.
- The Emb protein contains at least 50 repeats of 77 amino acids, predicted to form a coiled-coil structure.
- Extracellular matrix binding activity was localized to the N-terminal domain of the Emb protein.
Conclusions:
- Emb is a novel, large, fibrillar surface protein of Streptococcus defectivus.
- The N-terminus of Emb mediates extracellular matrix binding.
- Emb is proposed as the prototype for a new family of streptococcal fibrillar proteins.
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