Related Experiment Video
Updated: Jul 7, 2026

Biomimetic Materials to Characterize Bacteria-host Interactions
Published on: November 16, 2015
Functional mapping of an oligomeric autotransporter adhesin of Aggregatibacter actinomycetemcomitans
Chunxiao Yu1, Teresa Ruiz, Christopher Lenox
1Department of Microbiology and Molecular Genetics, University of Vermont, Burlington, VT 05405, USA.
Abstract:
Extracellular matrix protein adhesin A (EmaA) is a 202-kDa nonfimbrial adhesin, which mediates the adhesion of the oral pathogen Aggregatibacter actinomycetemcomitans to collagen. EmaA oligomers form surface antenna-like protrusions consisting of a long helical rod with an ellipsoidal ending. The functional analysis of in-frame emaA deletion mutants has located the collagen binding activity to the amino terminus of the protein corresponding to amino acids 70 to 386. The level of collagen binding of this deletion mutant was comparable to the emaA mutant strain. Transmission electron microscopy studies indicate that the first 330 amino acids of the mature protein form the ellipsoidal ending of the EmaA protrusions, where the activity resides. Amino acid substitution analysis within this sequence has identified a critical amino acid, which is essential for the formation of the ellipsoidal ending and for collagen binding activity.
More Related Videos
Related Concept Videos
Surface Appendages of Archaea
Actin Polymerization and Cell Motility
Actin cytoskeleton dynamics can produce pushing, pulling, and resistance forces that help the cell to migrate.
Adherens Junctions
Adherens Junctions are Dynamic
The endothelial cells...
Protein Translocation Machinery on the ER Membrane
Sec61 protein conducting channel
In eukaryotes, the translocon complex comprises a core heterotrimeric translocator channel called the Sec61 complex. This channel includes three transmembrane proteins, Sec61α, Sec61β, and Sec61γ, and is the largest subunit of the translocon complex.
Intracellular Signaling Affects Focal Adhesions
Some...
Tail-anchoring of Proteins in the ER Membrane

