Interactions of bacteriophage T4 adhesin with selected lipopolysaccharides studied using atomic force microscopy

Scientific Reports
Ewa BrzozowskaJoanna Niedziółka-Jönsson

Abstract

The interaction between the T4 bacteriophage gp37 adhesin and the bacterial lipopolysaccharide (LPS) is a well-studied system, however, the affinity and strength of the interaction haven't been analyzed so far. Here, we use atomic force microscopy to determine the strength of the interaction between the adhesin and its receptor, namely LPS taken from a wild strain of E. coli B. As negative controls we used LPSs of E. coli O111:B and Hafnia alvei. To study the interaction an AFM tip modified with the gp37 adhesin was used to scan surfaces of mica covered with one of the three different LPSs. Using the correlation between the surface topography images and the tip-surface interaction we could verify the binding between the specific LPS and the tip in contrast to the very weak interaction between the tip and the non-binding LPSs. Using force spectroscopy we could then measure the binding strength by pulling on the AFM tip until it lifted off from the surface. The force necessary to break the interaction between gp37 and LPS from E. coli B, LPS from E. coli O111:B and LPS from H. alvei were measured to be 70 ± 29 pN, 46 ± 13 pN and 45 ± 14 pN, respectively. The latter values are likely partially due to non-specific interaction betwe...Continue Reading

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Citations

Mar 29, 2019·Angewandte Chemie·Ralph Wieneke, Robert Tampé
Jan 12, 2021·Biosensors & Bioelectronics·Wajid HussainShenqi Wang

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Methods Mentioned

BETA
AFM
Surface Plasmon Resonance
bio-layer interferometry
bio-layer
atomic force spectroscopy
biosensor

Software Mentioned

Octet
ImageJ

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