AccessMyLibrary provides FREE access to over 30 million articles from top publications available through your library.

Recent findings from Y.R. Kong and co-authors highlight research in anthrax.

Bioterrorism Week

| June 29, 2009 | COPYRIGHT 2009 NewsRX. This material is published under license from the publisher through the Gale Group, Farmington Hills, Michigan.  All inquiries regarding rights should be directed to the Gale Group. (Hide copyright information)Copyright

"PA-binding domain of LF (LFn) or PA-binding domain of EF (EFn) is the anthrax protective antigen (PA) binding domain of anthrax lethal factor ( LF) or edema factor (EF). Here we show the development of a novel anthrax toxin inhibitor, fusion protein of N-terminal 27 amino acids deletion of LFn (Delta 27LFn) and EFn," investigators in Beijing, People's Republic of China report (see also Anthrax).

"In a cell model of intoxication, fusion protein of Delta 27LFn and EFn (Delta 27LFn-EFn) was a 62-fold more potent toxin inhibitor than LFn or EFn, and this increased activity corresponded to a 39-fold higher PA-binding affinity by Biacore analysis. More importantly, Delta 27LFn-EFn could protect the highly susceptible Fischer 344 rats from anthrax lethal toxin challenge," wrote Y.R. Kong and colleagues.

The researchers concluded: "This work suggested that Delta 27LFn-EFn has the potential as a ...

Related articles from newspapers, magazines, journals, and more
For more facts and information, see all results

Source: HighBeam Research, Recent findings from Y.R. Kong and co-authors highlight research in...

©2009 Gale, a part of Cengage Learning. All rights reserved.
About us | FAQs | Contact us | Privacy policy | Terms and conditions
Other Gale sites: Encyclopedia.com | HighBeam Research | Acquire Content | Books & Authors | Goliath | MovieRetriever | Smart QandA