Vibrio cholerae biofilms use modular adhesins with glycan-targeting and nonspecific surface binding domains for colonization

Xin Huang, Thomas Nero, Ranjuna Weerasekera, Katherine H. Matej, Alex Hinbest, Zhaowei Jiang, Rebecca F. Lee, Longjun Wu, Cecilia Chak, Japinder Nijjer, Isabella Gibaldi, Hang Yang, Nathan Gamble, Wai-Leung Ng, Stacy A. Malaker, Kaelyn Sumigray, Rich Olson () and Jing Yan ()
Additional contact information
Xin Huang: Cellular and Developmental Biology, Yale University
Thomas Nero: Cellular and Developmental Biology, Yale University
Ranjuna Weerasekera: Molecular Biophysics Program, Wesleyan University
Katherine H. Matej: Cellular and Developmental Biology, Yale University
Alex Hinbest: Molecular Biophysics Program, Wesleyan University
Zhaowei Jiang: Cellular and Developmental Biology, Yale University
Rebecca F. Lee: Yale School of Medicine
Longjun Wu: Yale University
Cecilia Chak: Cellular and Developmental Biology, Yale University
Japinder Nijjer: Cellular and Developmental Biology, Yale University
Isabella Gibaldi: Molecular Biophysics Program, Wesleyan University
Hang Yang: Molecular Biophysics Program, Wesleyan University
Nathan Gamble: Molecular Biophysics Program, Wesleyan University
Wai-Leung Ng: Tufts University School of Medicine
Stacy A. Malaker: Yale University
Kaelyn Sumigray: Yale School of Medicine
Rich Olson: Molecular Biophysics Program, Wesleyan University
Jing Yan: Cellular and Developmental Biology, Yale University

Nature Communications, 2023, vol. 14, issue 1, 1-14

Abstract: Abstract Bacterial biofilms are formed on environmental surfaces and host tissues, and facilitate host colonization and antibiotic resistance by human pathogens. Bacteria often express multiple adhesive proteins (adhesins), but it is often unclear whether adhesins have specialized or redundant roles. Here, we show how the model biofilm-forming organism Vibrio cholerae uses two adhesins with overlapping but distinct functions to achieve robust adhesion to diverse surfaces. Both biofilm-specific adhesins Bap1 and RbmC function as a “double-sided tape”: they share a β-propeller domain that binds to the biofilm matrix exopolysaccharide, but have distinct environment-facing domains. Bap1 adheres to lipids and abiotic surfaces, while RbmC mainly mediates binding to host surfaces. Furthermore, both adhesins contribute to adhesion in an enteroid monolayer colonization model. We expect that similar modular domains may be utilized by other pathogens, and this line of research can potentially lead to new biofilm-removal strategies and biofilm-inspired adhesives.

Date: 2023
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DOI: 10.1038/s41467-023-37660-0

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