Skip to main page content
U.S. flag

An official website of the United States government

Dot gov

The .gov means it’s official.
Federal government websites often end in .gov or .mil. Before sharing sensitive information, make sure you’re on a federal government site.

Https

The site is secure.
The https:// ensures that you are connecting to the official website and that any information you provide is encrypted and transmitted securely.

Access keys NCBI Homepage MyNCBI Homepage Main Content Main Navigation
. 2008 Feb;39(2):202-207.
doi: 10.1016/j.mejo.2006.11.007.

Landscape Phage as a Molecular Recognition Interface for Detection Devices

Valery A Petrenko

Landscape Phage as a Molecular Recognition Interface for Detection Devices

Valery A Petrenko. Microelectronics J. 2008 Feb.

Abstract

Filamentous phages are thread-shaped bacterial viruses. Their outer coat is a tube formed by thousands equal copies of the major coat protein pVIII. Libraries of random peptides fused to pVIII domains were used for selection of phages probes specific for a panel of test antigens and biological threat agents. Because the viral carrier in the phage borne bio-selective probes is infective, they can be cloned individually and propagated indefinitely without needs of their chemical synthesis or reconstructing. As a new bioselective material, landscape phages combine unique characteristics of affinity reagents and self assembling proteins. Biorecognition layers formed by the phage-derived probes bind biological agents with high affinity and specificity and generate detectable signals in analytical platforms. The performance of phage-derived materials as biorecognition interface was illustrated by detection of Bacillus anthracis spores and Salmonella typhimurium cells. With further refinement, the phage-derived analytical platforms for detecting and monitoring of numerous threat agents may be developed, since phage interface against any bacteria, virus or toxin may be readily selected from the landscape phage libraries. As an interface in the field-use detectors, they may be superior to antibodies, since they are inexpensive, highly specific and strong binders, resistant to high temperatures and environmental stresses.

PubMed Disclaimer

Figures

Fig. 1
Fig. 1
Electron micrograph of filamentous phage. The aminoterminus of pIII proteins are visible and pointed by arrow (cortesy of Irina Davidovich, Gregory Kishchenko and and Lee Makowski).
Fig. 2
Fig. 2
A. Alpha-helical domain of the fusion major coat protein pVIII. B. Space-filling model of the phage (about 1% of its length). White area in A and B depicts the foreign random peptides attached to amino acid Asp-4 or Asp-5 of pVIII in the landscape libraries [11] (for simplicity they are presented in alpha-helical conformation, although they can adapt any conformation); yellow area pictures amino acids 12-19 randomized in the α-library [14]. Numbers 1-4 point different areas of the same pVIII subunit starting from the N-terminal foreign peptide. About half of amino acids are exposed, while another half is buried in the capsid (shown as red in A). The model was built by Dr. Alexey M. Eroshkin using Marvin's phage model [8].
Fig. 2
Fig. 2
A. Alpha-helical domain of the fusion major coat protein pVIII. B. Space-filling model of the phage (about 1% of its length). White area in A and B depicts the foreign random peptides attached to amino acid Asp-4 or Asp-5 of pVIII in the landscape libraries [11] (for simplicity they are presented in alpha-helical conformation, although they can adapt any conformation); yellow area pictures amino acids 12-19 randomized in the α-library [14]. Numbers 1-4 point different areas of the same pVIII subunit starting from the N-terminal foreign peptide. About half of amino acids are exposed, while another half is buried in the capsid (shown as red in A). The model was built by Dr. Alexey M. Eroshkin using Marvin's phage model [8].
Fig. 3
Fig. 3
TEM micrograph of bacteria-phage complex. Phage is labeled with gold nanoparticles (arrows). Adapted from [19].
Fig. 4
Fig. 4
Scanning electron micrograph of S. typhimurium binding to phage immobilized to the surface of a sensor by physical adsorption. Magnification 3000×; bar = 5μm. Adapted from [21].
See this image and copyright information in PMC

Similar articles

See all similar articles

Cited by

See all "Cited by" articles

References

    1. Cunningham AJ. Introduction to Bioanalytical Sensors. New york: John Wiley & Sons, Inc.; 1998. p. 418.
    1. Gizeli E, Lowe CR, editors. Biomolecular sensors. Taylor & Francis; London, New York: 2002. p. 322.
    1. Goodchild S, Love T, Hopkins N, Mayers C. Engineering antibodies for biosensor technologies. Adv Appl Microbiol. 2006;58:185–226. - PubMed
    1. Cooper J, Cass T, editors. Biosensors. Second. University Press; Oxford, New York: 2004. p. 251.
    1. Rider TH, Petrovick MS, Nargi FE, Harper JD, Schwoebel ED, Mathews RH, Blanchard DJ, Bortolin LT, Young AM, Chen J, Hollis MA. A B cell-based sensor for rapid identification of pathogens. Science. 2003;301(5630):213–215. - PubMed

LinkOut - more resources