A paper written by Associate Professor of Molecular Biology and Biochemistry Rich Olson and his former students was designated as an “Editor’s Pick” by the Journal of Biological Chemistry. Only 2% of the approximately 6,600 papers published each year in the journal receive this designation.
Titled “The 1.9 Å crystal structure of the extracellular matrix protein Bap1 from Vibrio cholerae provides insights into bacterial biofilm adhesion,” the paper, published on Oct. 4, explores how bacteria “glues” itself to surfaces in the environment. The co-authors include Alison Biester ’19, Ethan Chupp ’18, Jianyi Lu ’17, Charlie Visudharomn ’17 and Katherine Kaus PhD ’18. Kaus, who is first author on the paper, is featured in a special profile on the JBC website.
Bacteria commonly form structures called biofilms, which are communities of living cells encapsulated by a three-dimensional matrix of secreted proteins, nucleic acids, and carbohydrates. Biofilms are a defense mechanism against environmental challenges and play a role in many pathogenic diseases.
Vibrio cholerae is a historically significant bacterium that causes the disease called cholera, which is still responsible for tens of thousands of annual deaths worldwide. The V. cholerae biofilm is primarily composed of a secreted carbohydrate called VPS and a number of matrix proteins secreted by the bacteria.
The Olson Lab’s recent work focuses on how several of these secreted matrix proteins form adhesive interactions on surfaces in the environment and on human or animal cells.
In this paper, the co-authors present the three-dimensional structure of the Bap1 biofilm matrix protein solved using a biophysical technique called X-ray crystallography.
“This structure gives us clues about how the Bap1 protein might function as a ‘glue’ to attach the biofilm to surfaces in the environment,” Olson said. “This structure also gives us insight into the function of a related matrix protein called RbmC, which we have previously shown to attach to sugar molecules found on mammalian cell surfaces.”
Together, these results show how the Bap1 and RbmC proteins likely play similar roles in forming interactions within the biofilm, but different roles in attaching the biofilm to diverse surfaces.
“Understanding how biofilms attach to surfaces provides insights into the disease mechanism and new strategies for developing therapeutics against deadly pathogens,” Olson said.