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. 2006 Jul;61(1):126-41.
doi: 10.1111/j.1365-2958.2006.05225.x.

"V体育平台登录" Identification of novel genomic islands coding for antigenic pilus-like structures in Streptococcus agalactiae

Roberto Rosini  1 , Cira Daniela Rinaudo, Marco Soriani, Peter Lauer, Marirosa Mora, Domenico Maione, Annarita Taddei, Isabella Santi, Claudia Ghezzo, Cecilia Brettoni, Scilla Buccato, Immaculada Margarit, Guido Grandi, John L Telford
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Free article

Identification of novel genomic islands coding for antigenic pilus-like structures in Streptococcus agalactiae

Roberto Rosini et al. Mol Microbiol. 2006 Jul.
Free article

Abstract

We have recently reported the presence of covalently linked pilus-like structures in the human pathogen, Group B Streptococcus (GBS). The pilus operon codes for three proteins which contain the conserved amino acid motif, LPXTG, associated with cell wall-anchored proteins together with two genes coding for sortase enzymes. Analysis of the eight sequenced genomes of GBS has led to the identification of a second, related genomic island of which there are two variants, each containing genes coding for proteins with LPXTG motifs and sortases. Here we show that both variant islands also code for pilus-like structures. Furthermore, we provide a thorough description and characterization of the genomic organization of the islands and the role of each protein in the assembly of the pili. For each pilus, polymerization of one of the three component proteins is essential for incorporation of the other two proteins into the pilus structure. In addition, two sortases are required for complete pilus assembly, each with specificity for one of the pilus components. A component protein of one of the newly identified pili is also a previously identified protective antigen and a second component of this pilus is shown to confer protection against GBS challenge VSports手机版. We propose that pilus-like structures are important virulence factors and potential vaccine candidates. .

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