» Articles » PMID: 10698802

Staphylococcal Surface Display of Metal-binding Polyhistidyl Peptides

Overview
Date 2000 Mar 4
PMID 10698802
Citations 17
Authors
Affiliations
Soon will be listed here.
Abstract

Recombinant Staphylococcus xylosus and Staphylococcus carnosus strains were generated with surface-exposed chimeric proteins containing polyhistidyl peptides designed for binding to divalent metal ions. Surface accessibility of the chimeric surface proteins was demonstrated and the chimeric surface proteins were found to be functional in terms of metal binding, since the recombinant staphylococcal cells were shown to have gained Ni(2+)- and Cd(2+)-binding capacity, suggesting that such bacteria could find use in bioremediation of heavy metals. This is, to our knowledge, the first time that recombinant, surface-exposed metal-binding peptides have been expressed on gram-positive bacteria. Potential environmental or biosensor applications for such recombinant staphylococci as biosorbents are discussed.

Citing Articles

Bacillus subtilis surface display technology: applications in bioprocessing and sustainable manufacturing.

Bahrulolum H, Ahmadian G Biotechnol Biofuels Bioprod. 2025; 18(1):34.

PMID: 40089785 DOI: 10.1186/s13068-025-02635-4.


Enhanced biosorption of cadmium ions on immobilized surface-engineered yeast using cadmium-binding peptides.

Wang S, Sun Y, Wang S, Fan C, Wang D, Liu F Front Microbiol. 2024; 15:1496843.

PMID: 39619698 PMC: 11604839. DOI: 10.3389/fmicb.2024.1496843.


Engineered Yeast Displaying Specific Norovirus-Binding Nanobodies for the Concentration and Detection of Human Norovirus in Food Matrix.

Zhao X, Rahman M, Xu Z, Kasputis T, He Y, Yuan L J Agric Food Chem. 2023; 71(22):8665-8672.

PMID: 37227100 PMC: 10332245. DOI: 10.1021/acs.jafc.3c01946.


Recent advances in bacterial biosensing and bioremediation of cadmium pollution: a mini-review.

Hui C, Guo Y, Liu L, Yi J World J Microbiol Biotechnol. 2021; 38(1):9.

PMID: 34850291 DOI: 10.1007/s11274-021-03198-w.


A Novel Cu(II)-Binding Peptide Identified by Phage Display Inhibits Cu-Mediated Aβ Aggregation.

Zhang X, Zhang X, Zhong M, Zhao P, Guo C, Li Y Int J Mol Sci. 2021; 22(13).

PMID: 34202166 PMC: 8269028. DOI: 10.3390/ijms22136842.


References
1.
Sousa C, Kotrba P, Ruml T, Cebolla A, de Lorenzo V . Metalloadsorption by Escherichia coli cells displaying yeast and mammalian metallothioneins anchored to the outer membrane protein LamB. J Bacteriol. 1998; 180(9):2280-4. PMC: 107165. DOI: 10.1128/JB.180.9.2280-2284.1998. View

2.
Patwardhan A, Goud G, Koepsel R, Ataai M . Selection of optimum affinity tags from a phage-displayed peptide library. Application to immobilized copper(II) affinity chromatography. J Chromatogr A. 1997; 787(1-2):91-100. DOI: 10.1016/s0021-9673(97)00580-3. View

3.
Mejare M, Ljung S, Bulow L . Selection of cadmium specific hexapeptides and their expression as OmpA fusion proteins in Escherichia coli. Protein Eng. 1998; 11(6):489-94. DOI: 10.1093/protein/11.6.489. View

4.
Pazirandeh M, Wells B, RYAN R . Development of bacterium-based heavy metal biosorbents: enhanced uptake of cadmium and mercury by Escherichia coli expressing a metal binding motif. Appl Environ Microbiol. 1998; 64(10):4068-72. PMC: 106604. DOI: 10.1128/AEM.64.10.4068-4072.1998. View

5.
Malik P, Terry T, Bellintani F, Perham R . Factors limiting display of foreign peptides on the major coat protein of filamentous bacteriophage capsids and a potential role for leader peptidase. FEBS Lett. 1998; 436(2):263-6. DOI: 10.1016/s0014-5793(98)01140-5. View