Research & Development World

  • R&D World Home
  • Topics
    • Aerospace
    • Automotive
    • Biotech
    • Careers
    • Chemistry
    • Environment
    • Energy
    • Life Science
    • Material Science
    • R&D Management
    • Physics
  • Technology
    • 3D Printing
    • A.I./Robotics
    • Software
    • Battery Technology
    • Controlled Environments
      • Cleanrooms
      • Graphene
      • Lasers
      • Regulations/Standards
      • Sensors
    • Imaging
    • Nanotechnology
    • Scientific Computing
      • Big Data
      • HPC/Supercomputing
      • Informatics
      • Security
    • Semiconductors
  • R&D Market Pulse
  • R&D 100
    • Call for Nominations: The 2025 R&D 100 Awards
    • R&D 100 Awards Event
    • R&D 100 Submissions
    • Winner Archive
    • Explore the 2024 R&D 100 award winners and finalists
  • Resources
    • Research Reports
    • Digital Issues
    • R&D Index
    • Subscribe
    • Video
    • Webinars
  • Global Funding Forecast
  • Top Labs
  • Advertise
  • SUBSCRIBE

Insights into protein folding may lead to better flu vaccine

By R&D Editors | July 26, 2012

FluVaccineA
new method for looking at how proteins fold inside mammal cells could
one day lead to better flu vaccines, among other practical applications,
say Cornell researchers.

The
method, described online in the Proceedings of the National Academy of
Sciences
July 16, allows researchers to take snapshots of the cell’s
protein-making machinery—called ribosomes—in various stages of protein
production. The scientists then pieced together the snapshots to
reconstruct how proteins fold during their synthesis.

Proteins
are made up of long chains of amino acids called polypeptides, and
folding gives each protein its characteristic structure, which
determines its function. Though researchers have used synthetic and
purified proteins to study protein folding, this study looks at proteins
from their inception, providing a truer picture for how partially
synthesized polypeptides can fold in cells.

Proteins
fold so quickly—in microseconds—that it has been a longtime mystery
just how polypeptide chains fold to create the protein’s structure.

“The
speed is very fast, so it’s very hard to capture certain steps, but our
approach can look at protein folding at the same time as it is being
synthesized by the ribosomes,” said Shu-Bing Qian, assistant professor
of nutritional sciences and the corresponding author on the paper. Yan
Han, a postdoctoral associate in Qian’s lab, is the paper’s first
author.

In
a nutshell, messenger RNA (mRNA) carries the coding information for
proteins from the DNA to ribosomes, which translate those codes into
chains of amino acids that make up proteins. Previously, other
researchers had developed a technique to localize the exact position of
the ribosomes on the mRNA. Qian and colleagues further advanced this
technique to selectively enrich only a certain portion of the
protein-making machinery, basically taking snapshots of different stages
of the protein synthesis process.

“Like
a magnifier, we enrich a small pool from the bigger ocean and then
paint a picture from early to late stages of the process,” Qian said.

In
the paper, the researchers also describe applying this technique to
better understanding a protein called hemagglutinin (HA), located on the
surface of the influenza A virus; HA’s structure (folding) allows it to
infect the cell.

Flu
vaccines are based on antibodies that recognize such proteins as HA.
But viruses have high mutation rates to escape antibody detection.
Often, flu vaccines lose their effectiveness because surface proteins on
the virus mutate. HA, for example, has the highest mutation rate of the
flu virus’ surface proteins.

The researchers proved that their technique can identify how the folding process changes when HA mutates.

“If people know the folding picture of how a mutation changes, it will be helpful for designing a better vaccine,” Qian said.

“Folding
is a very fundamental issue in biology,” Qian added. “It’s been a
long-term mystery how the cell achieves this folding successfully, with
such speed and with such a great success rate.”

Monitoring cotranslational protein folding in mammalian cells at codon resolution

Source: Cornell University

Related Articles Read More >

professional photo of wooly mammoth in nature --ar 2:1 --personalize sq85hce --v 6.1 Job ID: 47185eaa-b213-4624-8bee-44f9e882feaa
Why science ethicists are sounding skepticism and alarm on ‘de-extinction’
ALAFIA system speeds complex molecular simulations for University of Miami drug research
3d rendered illustration of the anatomy of a cancer cell
Funding flows to obesity, oncology and immunology: 2024 sales data show where science is paying off
Health-related innovation in Morocco highlighted by resident inventor patenting activity
rd newsletter
EXPAND YOUR KNOWLEDGE AND STAY CONNECTED
Get the latest info on technologies, trends, and strategies in Research & Development.
RD 25 Power Index

R&D World Digital Issues

Fall 2024 issue

Browse the most current issue of R&D World and back issues in an easy to use high quality format. Clip, share and download with the leading R&D magazine today.

Research & Development World
  • Subscribe to R&D World Magazine
  • Enews Sign Up
  • Contact Us
  • About Us
  • Drug Discovery & Development
  • Pharmaceutical Processing
  • Global Funding Forecast

Copyright © 2025 WTWH Media LLC. All Rights Reserved. The material on this site may not be reproduced, distributed, transmitted, cached or otherwise used, except with the prior written permission of WTWH Media
Privacy Policy | Advertising | About Us

Search R&D World

  • R&D World Home
  • Topics
    • Aerospace
    • Automotive
    • Biotech
    • Careers
    • Chemistry
    • Environment
    • Energy
    • Life Science
    • Material Science
    • R&D Management
    • Physics
  • Technology
    • 3D Printing
    • A.I./Robotics
    • Software
    • Battery Technology
    • Controlled Environments
      • Cleanrooms
      • Graphene
      • Lasers
      • Regulations/Standards
      • Sensors
    • Imaging
    • Nanotechnology
    • Scientific Computing
      • Big Data
      • HPC/Supercomputing
      • Informatics
      • Security
    • Semiconductors
  • R&D Market Pulse
  • R&D 100
    • Call for Nominations: The 2025 R&D 100 Awards
    • R&D 100 Awards Event
    • R&D 100 Submissions
    • Winner Archive
    • Explore the 2024 R&D 100 award winners and finalists
  • Resources
    • Research Reports
    • Digital Issues
    • R&D Index
    • Subscribe
    • Video
    • Webinars
  • Global Funding Forecast
  • Top Labs
  • Advertise
  • SUBSCRIBE