Sequence analyses of fimbriae subunit FimA proteins on <it>Actinomyces naeslundii </it>genospecies 1 and 2 and <it>Actinomyces odontolyticus </it>with variant carbohydrate binding specificities

• Main Authors: Persson Karina, Birve Anna, Öhman Ulla, Hallberg Kristina, Drobni Mirva, Johansson Ingegerd, Strömberg Nicklas
• Format: Article
• Language: English
• Published: BMC 2006-05-01
• Series: BMC Microbiology
• Online Access: http://www.biomedcentral.com/1471-2180/6/43

<p>Abstract</p> <p>Background</p> <p><it>Actinomyces naeslundii </it>genospecies 1 and 2 express type-2 fimbriae (FimA subunit polymers) with variant Galβ binding specificities and <it>Actinomyces odontolyticus </it>a sialic acid specificity to colonize different oral surfaces. However, the fimbrial nature of the sialic acid binding property and sequence information about FimA proteins from multiple strains are lacking.</p> <p>Results</p> <p>Here we have sequenced <it>fimA </it>genes from strains of <it>A.naeslundii </it>genospecies 1 (n = 4) and genospecies 2 (n = 4), both of which harboured variant Galβ-dependent hemagglutination (HA) types, and from <it>A.odontolyticus </it>PK984 with a sialic acid-dependent HA pattern. Three unique subtypes of FimA proteins with 63.8–66.4% sequence identity were present in strains of <it>A. naeslundii </it>genospecies 1 and 2 and <it>A. odontolyticus</it>. The generally high FimA sequence identity (>97.2%) within a genospecies revealed species specific sequences or segments that coincided with binding specificity. All three FimA protein variants contained a signal peptide, pilin motif, E box, proline-rich segment and an LPXTG sorting motif among other conserved segments for secretion, assembly and sorting of fimbrial proteins. The highly conserved pilin, E box and LPXTG motifs are present in fimbriae proteins from other Gram-positive bacteria. Moreover, only strains of genospecies 1 were agglutinated with type-2 fimbriae antisera derived from <it>A. naeslundii </it>genospecies 1 strain 12104, emphasizing that the overall folding of FimA may generate different functionalities. Western blot analyses with FimA antisera revealed monomers and oligomers of FimA in whole cell protein extracts and a purified recombinant FimA preparation, indicating a sortase-independent oligomerization of FimA.</p> <p>Conclusion</p> <p>The genus <it>Actinomyces </it>involves a diversity of unique FimA proteins with conserved pilin, E box and LPXTG motifs, depending on subspecies and associated binding specificity. In addition, a sortase independent oligomerization of FimA subunit proteins in solution was indicated.</p>