Related Experiment Video
Updated: Aug 13, 2026

Aip1p Dynamics Are Altered by the R256H Mutation in Actin
Published on: July 30, 2014
Mutants of Actinomyces viscosus T14V lacking type 1, type 2, or both types of fimbriae
J O Cisar1, A E Vatter, W B Clark
1Laboratory of Microbial Ecology, National Institute of Dental Research, Bethesda, Maryland 20892.
Abstract:
Mutants of Actinomyces viscosus T14V lacking type 1 or type 2 fimbriae or both were selected by their failure to react with rabbit antibodies against either or both fimbrial antigens. Immunospecific double labeling with iron dextran and ferritin-conjugated antibodies showed two types of fimbriae on individual cells of the parent organism, a single type on mutant strains with type 1+2- and type 1-2+ fimbriae and no labeled or unlabeled fimbriae on a type 1-2- fimbria-deficient strain. The mutational loss of one fimbrial antigen did not appear to affect expression of the other, since bacteria with one or two types of fimbriae bound similar amounts of a monoclonal antibody directed against the fimbrial antigen present on both bacterial phenotypes. The strong adsorption of strains with type 1+2+ or 1+2- fimbriae to saliva-treated hydroxyapatite and weak adsorption of those with type 1-2+ or no fimbriae was consistent with the known involvement of type 1 fimbriae in this attachment process. Similarly, the A. viscosus lectin was clearly associated with the expression of type 2 fimbriae, since only the strains with type 1+2+ or 1-2+ fimbriae participated in lactose-sensitive coaggregations with Streptococcus sanguis 34. Further studies using the fimbria-deficient mutant strains showed that aggregation of A. viscosus T14V in the presence of sialidase-treated human saliva involved both types of fimbriae, whereas neither type was required for the lactose-resistant coaggregation of the organism with certain streptococcal strains.
Insights
Actinomyces viscosus T14V has two fimbrial types involved in adhesion. Type 1 fimbriae mediate hydroxyapatite binding, while type 2 fimbriae are linked to lectin activity and coaggregation with Streptococcus sanguis.
Area of Science:
- Microbiology
- Bacterial Adhesion
- Molecular Biology
Background:
- Actinomyces viscosus T14V possesses fimbriae, which are hair-like appendages crucial for bacterial adhesion and colonization.
- Understanding the specific roles of different fimbrial types is essential for elucidating host-microbe interactions.
Purpose of the Study:
- To characterize the distinct functions of type 1 and type 2 fimbriae in Actinomyces viscosus T14V.
- To investigate the involvement of these fimbriae in adhesion to hydroxyapatite and coaggregation with other bacteria.
Main Methods:
- Generation and characterization of fimbria-deficient mutants of Actinomyces viscosus T14V using antibody-based selection.
- Immunospecific double labeling with iron dextran and ferritin-conjugated antibodies to visualize fimbriae.
- Assays for bacterial adsorption to saliva-treated hydroxyapatite and coaggregation with Streptococcus sanguis.
Main Results:
- Mutants lacking type 1 or type 2 fimbriae were successfully isolated, confirming the presence of two distinct fimbrial types.
- Type 1 fimbriae were essential for strong adsorption to saliva-treated hydroxyapatite.
- Type 2 fimbriae were associated with the Actinomyces viscosus lectin and mediated lactose-sensitive coaggregation with Streptococcus sanguis.
Conclusions:
- Actinomyces viscosus T14V expresses two antigenically distinct fimbrial types, type 1 and type 2.
- Type 1 fimbriae play a primary role in adherence to hydroxyapatite, while type 2 fimbriae are involved in specific coaggregation mechanisms.
- Both fimbrial types contribute to the aggregation of Actinomyces viscosus T14V in the presence of human saliva.
Related Concept Videos
Cytoskeletal Proteins in Bacteria
Introduction to Actin
Generation of Straight or Branched Actin Filaments
Arp2/3 Complex
Arp2/3 complex is a seven-subunit complex consisting of two proteins similar to actin- Arp2 and Arp3, and five other subunits that help keep Arp2 and Arp3 inactive. When required, the complex is...
Actin Filament Depolymerization
In F-actin, the ADF/cofilin proteins...
Actin Polymerization and Cell Motility
Actin cytoskeleton dynamics can produce pushing, pulling, and resistance forces that help the cell to migrate.
Fimbriae, Pili, and Axial Filaments

