News, Analysis, Trends, Management Innovations for
Clinical Laboratories and Pathology Groups

Hosted by Robert Michel

News, Analysis, Trends, Management Innovations for
Clinical Laboratories and Pathology Groups

Hosted by Robert Michel

Sign In

University of Illinois Scientists Use Structural DNA to Make Tiny ‘Hand’ That ‘Grabs’ COVID-19 Coronavirus

Study shows clinical laboratories may one day use nanorobotic tests to help prevent spread of viral infections, cancer, and other diseases

Scientists from the University of Illinois Urbana-Champaign (U of I) have developed a tiny robotic “hand” made from structural DNA that “grabs” viruses—including the COVID-19 coronavirus—potentially preventing them from infecting cells. Such a nano-robotic antiviral technology could be used by anatomic pathologists and clinical laboratory managers in the future as a point-of-care type of test.

This is yet another example of out-of-the-box thinking by developers of diagnostic technology. Led by Xing Wang, PhD, professor of bioengineering and of chemistry at the U of I, the scientists dubbed their DNA device the NanoGripper.

Similar to a piece of origami (Japanese art of folded paper), the so-called hand has “four bendable fingers and a palm, all in one nanostructure folded from a single piece of DNA,” according to a U of I news release. The scientists found in their study that the hand was capable of doing a rapid test to identify the (COVID-19) virus and “prevented the viral spike proteins from infecting the cells,” Gizmodo reported.

“We are using DNA for its structural properties. It is strong, flexible, and programmable. Yet even in the DNA origami field, this is novel in terms of the design principle. We fold one long strand of DNA back and forth to make all of the elements, both the static and moving pieces, in one step,” said Wang in the news release. 

The scientists published their findings in the journal Science Robotics titled, “Bioinspired Designer DNA NanoGripper for Virus Sensing and Potential Inhibition.” 

“It would be very difficult to apply it after a person is infected, but there’s a way we could use it as a preventive therapeutic,” said Xing Wang, PhD (above), associate professor, bioengineering and chemistry, University of Illinois Urbana-Champaign, in a news release. “We could make an anti-viral nasal spray compound. The nose is the hot spot for respiratory viruses, like COVID or influenza. A nasal spray with the NanoGripper could prevent inhaled viruses from interacting with the cells in the nose.” Clinical laboratories may one day perform antiviral testing that uses U of I’s NanoGripper technology. (Photo copyright: University of Illinois.)

How a DNA Nanorobot Grabs a Virus

The U of I researchers wanted to leverage what has been discovered about DNA as a “material for constructing versatile nanorobots for biomedical applications,” they wrote in Science Robotics. However, previous studies had not achieved the current origami design of a nanoscale mechanism, the authors added.

With robotic precision and its DNA structure, the researchers’ NanoGripper moves and enables fingers to bend for “customized interactions with target molecules,” Interesting Engineering reported, adding that the technology also:

  • Employed DNA aptamers on the fingers which act as “molecular locks” to find and bind to specific targets.
  • In a demonstration, wrapped its fingers around the target spike protein of the COVID-19 coronavirus, essentially “disabling its ability to infect cells.”

The NanoGripper binds to the virus with the help of “pattern-recognition-enabled multivalent interaction,” Wang told The Pathologist.

“The aptamers are arranged into a spatial pattern that specifically matches that of the trimeric spike protein on the virus outer surface. Such pattern recognition-enabled multivalent interaction—a principle developed by my group—has induced ultrahigh NanoGripper virus-binding avidity, resulting in enhanced virus diagnosis sensitivity,” Wang said.

Taken from the U of I news release, the image above shows how “Inspired by the gripping power of the human hand and bird claws, the researchers designed the NanoGripper with four bendable fingers and a palm, all in one nanostructure folded from a single piece of DNA. Each finger has three joints, like a human finger, and the angle and degree of bending are determined by the design on the DNA scaffold.” Such nano-robotic technology could become a new clinical laboratory test for diagnosing viral infections, or even a preventative treatment if caught prior to infection. (Photo and caption copyright: University of Illinois.)

Developing a Test for COVID-19

The scientists discovered that when equipped with a photonic crystal sensor, NanoGripper detected the SARS-CoV-2 coronavirus in 30 minutes with sensitivity equal to RTqPCR tests, Gizmodo reported.

“The NanoGripper functions as a highly sensitive biosensor that selectively detects intact SARS-CoV-2 virions in human saliva with a limit of detection of 100 copies per milliliter, providing a sensitivity equal to that of reverse transcription quantitative polymerase chain reaction [RTqPCR],” the authors wrote in Science Robotics.

In fact, the NanoGripper test is reportedly faster and easier than RTqPCR testing, which requires sophisticated instruments.

“Our test is very fast and simple since we detect the intact virus directly,” said study collaborator Brian Cunningham, PhD, professor, electrical and computer engineering and bioengineering at U of I, in the news release.

“When the virus is held in the NanoGripper’s hand, a fluorescent molecule is triggered to release light when illuminated by an LED or laser,” he said, adding, “When a large number of fluorescent molecules are concentrated upon a single virus, it becomes bright enough in our detection system to count each virus individually.”

More Research and Applications

Gizmodo compared the NanoGripper to a “true Swiss army knife,” able to change and detect other viruses such as HIV and influenza (Flu).

The U of I researchers have already studied the NanoGripper’s ability to detect hepatitis B and plan to publish findings soon, Wang told The Pathologist. He also noted it’s possible the NanoGripper “can be integrated with a lateral flow assay paper strip platform for development of a rapid, sensitive, and inexpensive at home or point-of-care virus detection.”

There is “power in soft nanorobotics,” said Wang, who envisions potential for the NanoGripper beyond viruses to include programming the fingers to detect cancer markers and enabling the grippers to deliver treatment to target cells. 

Clinical pathologists and laboratory managers may want to follow this research coming out of the University of Illinois Urbana-Champaign. Once put through additional clinical studies, such nanorobotic diagnostic technology might eventually be used at the point-of-care to help prevent viral infection and spread of disease.                         

—Donna Marie Pocius

Related Information:

Nanorobot Hand Made of DNA Grabs Viruses for Diagnostics and Blocks Cell Entry

Scientists Built a Tiny DNA “Hand” That Grabs Viruses to Stop Infections

Bioinspired Designer DNA NanoGripper for Virus Sensing and Potential Inhibition

Tiny Four-Fingered DNA Robot Hand Grabs COVID Virus, Shields Cells from Infection

Folded DNA “Hand” Grips Virus Particles in a Rapid Detection System in Liquid Samples

Two University of North Carolina School of Medicine Laboratories Develop Technique for Seeing How Proteins Change Shape In Vivo

UNC’s novel way to visualize the human proteome could lead to improved clinical laboratory tests along with the development of new therapies

Diagnostic testing based on proteomics is considered to be a field with immense potential in diagnostics and therapeutics. News of a research breakthrough into how scientists can visualize protein activity within cells will be of major interest to the pathologists, PhDs, and medical laboratory scientists who specialize in clinical laboratory testing involving proteins.

Proteins are essential to all life and to the growth, maintenance, and repair of the human body. So, a thorough understanding of how they function within living cells would be essential to informed medical decision-making as well. And yet, how proteins go about doing their work is not well understood.

That may soon change. Scientists at the University of North Carolina (UNC) School of Medicine have developed an imaging method that could provide new insights into how proteins alter their shapes within living cells. And those insights may lead to the development of new therapies and medical treatments.

Dubbed “binder-tag” by the UNC scientists, their new technique “allows researchers to pinpoint and track proteins that are in a desired shape or ‘conformation,’ and to do so in real time inside living cells,” according to a UNC Health news release.

Two labs in the UNC School of Medicine’s Department of Pharmacology collaborated to develop the binder-tag technique:

The scientists published their findings in the journal Cell, titled, “Biosensors Based on Peptide Exposure Show Single Molecule Conformations in Live Cells.”

Klaus Hahn PhD
 
“No one has been able to develop a method that can do, in such a generalizable way, what this method does. So, I think it could have a very big impact,” said lead author of the UNC study Klaus Hahn PhD (above), in the news release. “With this method we can see, for example, how microenvironmental differences across a cell affect, often profoundly, what a protein is doing,” he added. This research may enlarge scientists’ understanding of how the human proteome works and could lead to new medical laboratory tests and therapeutic drugs. (Photo copyright: UNC School of Medicine.)
 

How Binder-Tag Works

During their study, the UNC scientists developed binder-tag “movies” that allow viewers to see how the binder-tag technique enables the tracking of active molecules in living cells.

According to Cosmos:

  • The technique involves two parts: a fluorescent binder and a molecular tag that is attached to the proteins of interest.
  • When inactive, the tag is hidden inside the protein, but when the protein is ready for action it changes shape and exposes the tag.
  • The binder then joins with the exposed tag and fluoresces. This new fluorescence can easily be tracked within the cell.
  • Nothing else in the cell can bind to the binder or tag, so they only light up when in contact on the active protein.
  • This type of visualization will help researchers understand the dynamics of a protein in a cell.

“The method is compatible with a wide range of beacons, including much more efficient ones than the interacting beacon pairs required for ordinary FRET [fluorescence resonance energy transfer]. Binder-tag can even be used to build FRET sensors more easily. Moreover, the binder-tag molecules were chosen so that nothing in cells can react with them and interfere with their imaging role,” Hahn said in the news release.

“Only upon exposure can the peptide specifically interact with a reporter protein (the binder). Thus, simple fluorescence localization reflects protein conformation. Through direct excitation of bright dyes, the trajectory and conformation of individual proteins can be followed,” the UNC researchers wrote in Cell. “The simplicity of binder-tag can provide access to diverse proteins.”  

The UNC researchers’ binder-tag technique is a way to overcome the dire challenge of seeing tiny and hard-working proteins, Cosmos noted. Typical light microscopy does not enable a view of molecules at work. This paves the way for the new binder-tag technique, UNC pointed out.

“With this method, we can see, for example, how microenvironmental differences across a cell affect—and often profoundly—what a protein is doing,” Hahn said. “For a lot of protein-related diseases, scientists haven’t been able to understand why proteins start to do the wrong thing. The tools for obtaining that understanding just haven’t been available.”

More Proteins to Study

More research is needed before the binder-tag method can be used in diagnostics. Meanwhile, the UNC scientists intend to show how binder-tag can be applied to other protein structures and functions. 

“The human proteome has between 80,000 and 400,000 proteins, but not all at one time. They are expressed by 20,000 to 25,000 human genes. So, the human proteome has great promise for use in diagnostics, understanding disease, and developing therapies,” said Robert Michel, Editor-in-Chief of Dark Daily and its sister publication The Dark Report.

Medical scientists and diagnostics professionals will want to stay tuned to discover more about the tiny—though mighty—protein’s contributions to understanding diseases and patient treatment.     

Donna Marie Pocius

Related Information:

Biosensors Based on Peptide Exposure Show Single Molecule Conformations in Live Cells

Powerful Technique Allows Scientists to Study How Proteins Change Shape Inside Cells

Watching Proteins Dance

Binder-Tag: A Versatile Approach to Probe and Control the Conformational Changes of Individual Molecules in Living Cells

;