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Adherence of Bacteria to Plant Surfaces Measured in the Laboratory

Adherence of Bacteria to Plant Surfaces Measured in the Laboratory

Published on: June 19, 2018

Pb2+ tolerance by Frankia sp. strain EAN1pec involves surface-binding.

Teal Furnholm¹, Medhat Rehan^1,2,3, Jessica Wishart^1,4

¹Department of Cellular, Molecular, and Biomedical Sciences, University of New Hampshire, Durham, NH, USA.

Microbiology (Reading, England)

|February 1, 2017

Summary

This summary is machine-generated.

Frankia sp. strain EAN1pec exhibits remarkable lead resistance through surface modifications and protein expression changes. This bacterium utilizes multiple mechanisms, including metal transporters and chaperones, to cope with heavy metal stress.

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Area of Science:

Microbiology
Environmental Science
Biochemistry

Background:

Frankia strains are known for lead resistance.
Understanding the specific mechanisms in Frankia sp. strain EAN1pec is crucial.

Purpose of the Study:

To investigate the lead resistance mechanisms in Frankia sp. strain EAN1pec.
To identify proteins and pathways involved in heavy metal tolerance.

Main Methods:

Scanning electron microscopy (SEM), energy dispersive X-ray spectroscopy (EDAX), and Fourier transforming infrared spectroscopy (FTIR) were used for surface analysis.
Shotgun proteomics (labeled and unlabeled) analyzed protein expression changes under lead and zinc stress.
Bioinformatic analysis identified potential transcription factor binding sites.

Main Results:

Frankia sp. strain EAN1pec binds significant amounts of Pb+2 through surface modifications.
Pb+2 induced changes in exopolysaccharides, stringent response, and the phosphate (pho) regulon.
Upregulation of metal transporters, chaperones, and enzymes involved in metal precipitation were observed.
A novel transcription factor (DUF156) binding site was identified in multiple organisms.

Conclusions:

Frankia sp. strain EAN1pec employs a multi-faceted resistance mechanism against lead (Pb+2).
The identified mechanisms involve surface binding, metal transport, precipitation, and cellular stress responses.
The discovery of the DUF156 binding site has broader implications across different kingdoms.