Research Papers

Adhesin-Specific Nanomechanical Cantilever Biosensors for Detection of Microorganisms

[+] Author and Article Information
Tzuen-Rong J. Tzeng

Department of Biological Sciences, Clemson University, 132 Long Hall, Clemson, SC 29634-0314tzuenrt@clemson.edu

Yunyan R. Cheng

Department of Biological Sciences, Clemson University, 132 Long Hall, Clemson, SC 29634-0314ycheng@clemson.edu

Reza Saeidpourazar

Department of Materials Science and Engineering, University of Illinois at Urbana-Champaign, Urbana, IL 61801rezas@illinois.edu

Siddharth S. Aphale

Department of Mechanical Engineering, Clemson University, Clemson, SC 29634

Nader Jalili

Piezoactive Systems Laboratory, Department of Mechanical and Industrial Engineering,  Northeastern University, Boston, MA 02115

J. Heat Transfer 133(1), 011012 (Sep 30, 2010) (5 pages) doi:10.1115/1.4002363 History: Received May 16, 2010; Revised July 15, 2010; Published September 30, 2010; Online September 30, 2010

Lectins (adhesins) on bacterial surfaces play important roles in infection by mediating bacterial adherence to host cell surfaces via their cognate receptors. We have explored the use of α-D-mannose receptors as capturing agents for the detection of Escherichia coli using a microcantilever and have demonstrated that E. coli ORN178, which expresses normal type-1 pili, can interact with microcantilevers functionalized with α-D-mannose and can cause shifts in its resonance frequencies. Although E. coli ORN208, which expresses abnormal pili, binds poorly to α-D-mannose on the nitrocellulose membrane of a FAST slide, it did cause a detectable shift in resonance frequency when interacting with the α-D-mannose functionalized microcantilevers.

Copyright © 2011 by American Society of Mechanical Engineers
Your Session has timed out. Please sign back in to continue.



Grahic Jump Location
Figure 1

Polytec MSA 400 setup: (a) utilized at Clemson University Smart Structures and NEMS Laboratory and (b) listed on the website of Polytec

Grahic Jump Location
Figure 2

Yeast agglutination test. Superimposed images obtained from phase contrast microscope and epifluorescent microscope demonstrating (a) the agglutination of yeast cells mediated by E. coli ORN178-GFP (FimH+) and (b) the absence of yeast cell agglutination with E. coli ORN208-GFP (FimH-).

Grahic Jump Location
Figure 3

Binding of (a) E. coli ORN178-GFP to immobilized α-D-mannose-PAA, (b) PBS to immobilized α-D-mannose-PAA, (c) E. coli ORN208-GFP to immobilized α-D-mannose-PAA, (d) E. coli ORN178-GFP to immobilized α-D-galactose-PAA, (e) E. coli ORN178-GFP, pre-exposed to free mannose, to immobilized α-D-mannose-PAA, and (f) E. coli O157:H7-GFP to immobilized α-D-mannose-PAA on Whatman FAST 16-pad slides

Grahic Jump Location
Figure 4

Binding of formaldehyde killed E. coli ORN178-GFP (FimH+) to (a) yeast and to (b) α-D-mannose-PAA

Grahic Jump Location
Figure 5

Binding results of (a) E. coli ORN178-GFP (FimH+) and (b) E. coli ORN208-GFP (FimH-) to α-D-mannose-PAA on a gold slide

Grahic Jump Location
Figure 6

Binding results of (a) E. coli ORN178-GFP (FimH+) and (b) E. coli ORN208-GFP (FimH-) to α-D-mannose-PAA on a gold microcantilever base



Some tools below are only available to our subscribers or users with an online account.

Related Content

Customize your page view by dragging and repositioning the boxes below.

Related Journal Articles
Related eBook Content
Topic Collections

Sorry! You do not have access to this content. For assistance or to subscribe, please contact us:

  • TELEPHONE: 1-800-843-2763 (Toll-free in the USA)
  • EMAIL: asmedigitalcollection@asme.org
Sign In