Rich Olson
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View article: <i>Vibrio cholerae</i> interaction with predatory bacteria on chitin suggests an alternative mode of biofilm formation in marine snow conditions
<i>Vibrio cholerae</i> interaction with predatory bacteria on chitin suggests an alternative mode of biofilm formation in marine snow conditions Open
Vibrio cholerae is a ubiquitous marine microbe that solubilizes and consumes chitin in the marine water column. In both the marine environment and the intestinal track, V. cholerae forms biofilms; a key question regarding the lifestyle of …
View article: Conformations and sequence determinants in the lipid binding of an adhesive peptide derived from <i>Vibrio cholerae</i> biofilm
Conformations and sequence determinants in the lipid binding of an adhesive peptide derived from <i>Vibrio cholerae</i> biofilm Open
Surface adhesion is critical to the survival of pathogenic bacteria both in natural niches and during infections, often via forming matrix-embedded communities called biofilms. We previously identified a 57-amino acid peptide (Bap1-57aa) a…
View article: Comprehensive genomic and evolutionary analysis of biofilm matrix clusters and proteins in the <i>Vibrio</i> genus
Comprehensive genomic and evolutionary analysis of biofilm matrix clusters and proteins in the <i>Vibrio</i> genus Open
Vibrio cholerae pathogens cause cholera, an acute diarrheal disease resulting in significant morbidity and mortality worldwide. Biofilms in vibrios enhance their survival in natural ecosystems and facilitate transmission during cholera out…
View article: Vibrio cholerae RbmB is an α-1,4-polysaccharide lyase with biofilm-disrupting activity against Vibrio polysaccharide (VPS)
Vibrio cholerae RbmB is an α-1,4-polysaccharide lyase with biofilm-disrupting activity against Vibrio polysaccharide (VPS) Open
Many pathogenic bacteria form biofilms as a protective measure against environmental and host hazards. The underlying structure of the biofilm matrix consists of secreted macromolecules, often including exopolysaccharides. To escape the bi…
View article: Surface remodeling and inversion of cell-matrix interactions underlies community recognition and dispersal in<i>Vibrio cholerae</i>biofilms
Surface remodeling and inversion of cell-matrix interactions underlies community recognition and dispersal in<i>Vibrio cholerae</i>biofilms Open
Biofilms are ubiquitous surface-associated bacterial communities embedded in an extracellular matrix. While it is commonly assumed that biofilm-dwelling cells are glued together by the matrix, how the cell-matrix interaction depends on the…
View article: <i>Vibrio cholerae</i>RbmB is an α−1,4-polysaccharide lyase with biofilm-dispersal activity against Vibrio Polysaccharide (VPS)
<i>Vibrio cholerae</i>RbmB is an α−1,4-polysaccharide lyase with biofilm-dispersal activity against Vibrio Polysaccharide (VPS) Open
Many pathogenic bacteria form biofilms as a protective measure against environmental and host hazards. The underlying structure of the biofilm matrix consists of secreted macromolecules, usually including exopolysaccharides. To escape the …
View article: Comprehensive Genomic and Evolutionary Analysis of Biofilm Matrix Clusters and Proteins in the Vibrio Genus
Comprehensive Genomic and Evolutionary Analysis of Biofilm Matrix Clusters and Proteins in the Vibrio Genus Open
Vibrio cholerae pathogens cause cholera, an acute diarrheal disease resulting in significant morbidity and mortality worldwide. Biofilms in vibrios enhance their survival in natural ecosystems and facilitate transmission during cholera out…
View article: Social evolution of shared biofilm matrix components
Social evolution of shared biofilm matrix components Open
Biofilm formation is an important and ubiquitous mode of growth among bacteria. Central to the evolutionary advantage of biofilm formation is cell–cell and cell–surface adhesion achieved by a variety of factors, some of which are diffusibl…
View article: Social evolution of shared biofilm matrix components
Social evolution of shared biofilm matrix components Open
Biofilm formation is an important and ubiquitous mode of growth among bacteria. Central to the evolutionary advantage of biofilm formation is cell-cell and cell-surface adhesion achieved by a variety of factors, some of which are diffusibl…
View article: Searching for the Secret of Stickiness: How Biofilms Adhere to Surfaces
Searching for the Secret of Stickiness: How Biofilms Adhere to Surfaces Open
Bacterial biofilms are communities of cells enclosed in an extracellular polymeric matrix in which cells adhere to each other and to foreign surfaces. The development of a biofilm is a dynamic process that involves multiple steps, includin…
View article: Protein yoga: Conformational versatility of the Hemolysin II C‐terminal domain detailed by NMR structures for multiple states
Protein yoga: Conformational versatility of the Hemolysin II C‐terminal domain detailed by NMR structures for multiple states Open
The C‐terminal domain of Bacillus cereus hemolysin II (HlyIIC), stabilizes the trans‐membrane‐pore formed by the HlyII toxin and may aid in target cell recognition. Initial efforts to determine the NMR structure of HlyIIC were hampered by …
View article: Structural basis of mammalian glycan targeting by Vibrio cholerae cytolysin and biofilm proteins
Structural basis of mammalian glycan targeting by Vibrio cholerae cytolysin and biofilm proteins Open
Vibrio cholerae is an aquatic gram-negative microbe responsible for cholera, a pandemic disease causing life-threatening diarrheal outbreaks in populations with limited access to health care. Like most pathogenic bacteria, V. cholerae secr…
View article: Conserved SecA Signal Peptide-Binding Site Revealed by Engineered Protein Chimeras and Förster Resonance Energy Transfer
Conserved SecA Signal Peptide-Binding Site Revealed by Engineered Protein Chimeras and Förster Resonance Energy Transfer Open
Signal peptides are critical for the initiation of protein transport in bacteria by virtue of their recognition by the SecA ATPase motor protein followed by their transfer to the lateral gate region of the SecYEG protein-conducting channel…