This Article 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 Fenno, J C Articles by Fives-Taylor, P Search for Related Content PubMed PubMed Citation Articles by Fenno, J C Articles by Fives-Taylor, P

 Previous Article  |  Next Article 

Infect Immun. 1989 November; 57(11): 3527-3533

Nucleotide sequence analysis of a type 1 fimbrial gene of Streptococcus sanguis FW213.

Department of Microbiology and Molecular Genetics, College of Medicine, University of Vermont, Burlington 05405.

ABSTRACT

A structural gene for type 1 fimbriae of Streptococcus sanguis FW213 was located within a 6-kilobase fragment cloned in Escherichia coli. A 1.6-kilobase internal fragment contains an open reading frame of 927 bases coding for an immunoreactive peptide of 34,349 daltons, which corresponds in size with an observed cytoplasmic form of fimbrial peptide (P. M. Fives-Taylor, F. L. Macrina, T. J. Pritchard, and S. J. Peene, Infect. Immun. 55:123-128, 1987). Disruption of the reading frame by insertional mutagenesis results in loss of immunoreactivity. Consensus sequences for initiation of transcription and translation were identified 5' to the coding region. Transcription terminator-like sequences were found downstream of the coding region. The deduced amino acid sequence of the cloned fimbrial peptide shows a strongly hydrophobic signal sequence at the amino terminus. The carboxyl-terminal region does not include a hydrophobic membrane anchor sequence such as has been reported for other gram-positive surface structures. A hydrophobic region of 12 to 14 amino acids downstream from the putative signal sequence cleavage site exhibits homology with the Streptococcus pyogenes type 6 M protein repetitive region A (S. K. Hollingshead, V. A. Fischetti, and J. R. Scott, J. Biol. Chem., 261:1677-1686, 1986). Functional homology at the level of protein secondary structure with Actinomyces viscosus T14V type 1 fimbriae (M. K. Yeung, B. M. Chassy, and J. O. Cisar, J. Bacteriol., 169:1678-1683, 1987) is proposed.

This article has been cited by other articles:

• Elsner, A., Kreikemeyer, B., Braun-Kiewnick, A., Spellerberg, B., Buttaro, B. A., Podbielski, A. (2002). Involvement of Lsp, a Member of the LraI-Lipoprotein Family in Streptococcus pyogenes, in Eukaryotic Cell Adhesion and Internalization. Infect. Immun. 70: 4859-4869 [Abstract] [Full Text]  
• Tseng, H.-J., McEwan, A. G., Paton, J. C., Jennings, M. P. (2002). Virulence of Streptococcus pneumoniae: PsaA Mutants Are Hypersensitive to Oxidative Stress. Infect. Immun. 70: 1635-1639 [Abstract] [Full Text]  
• GILLESPIE, S.H., BALAKRISHNAN, I. (2000). Pathogenesis of pneumococcal infection. J Med Microbiol 49: 1057-1067 [Abstract] [Full Text]  
• Harrington, D. J., Greated, J. S., Chanter, N., Sutcliffe, I. C. (2000). Identification of Lipoprotein Homologues of Pneumococcal PsaA in the Equine Pathogens Streptococcus equi and Streptococcus zooepidemicus. Infect. Immun. 68: 6048-6051 [Abstract] [Full Text]  
• Loo, C. Y., Corliss, D. A., Ganeshkumar, N. (2000). Streptococcus gordonii Biofilm Formation: Identification of Genes that Code for Biofilm Phenotypes. J. Bacteriol. 182: 1374-1382 [Abstract] [Full Text]  
• Mintz, K. P., Fives-Taylor, P. M. (1999). Identification of Genes Coding for Exported Proteins of Actinobacillus actinomycetemcomitans. Infect. Immun. 67: 6217-6220 [Abstract] [Full Text]  
• Froeliger, E. H., Oetjen, J., Bond, J. P., Fives-Taylor, P. (1999). Streptococcus parasanguis pepO Encodes an Endopeptidase with Structure and Activity Similar to Those of Enzymes That Modulate Peptide Receptor Signaling in Eukaryotic Cells. Infect. Immun. 67: 5206-5214 [Abstract] [Full Text]  
• Spellerberg, B., Rozdzinski, E., Martin, S., Weber-Heynemann, J., Schnitzler, N., Lutticken, R., Podbielski, A. (1999). Lmb, a Protein with Similarities to the LraI Adhesin Family, Mediates Attachment of Streptococcus agalactiae to Human Laminin. Infect. Immun. 67: 871-878 [Abstract] [Full Text]  
• Lu, D., Boyd, B., Lingwood, C. A. (1997). Identification of the Key Protein for Zinc Uptake in Hemophilus influenzae. J. Biol. Chem. 272: 29033-29038 [Abstract] [Full Text]