The 2009 pandemic H1N1 neuraminidase N1 lacks the 150-cavity in its active site

[tetano]

Nat Struct Mol Biol. 2010 Sep 19. [Epub ahead of print]
The 2009 pandemic H1N1 neuraminidase N1 lacks the 150-cavity in its active site.

Li Q, Qi J, Zhang W, Vavricka CJ, Shi Y, Wei J, Feng E, Shen J, Chen J, Liu D, He J, Yan J, Liu H, Jiang H, Teng M, Li X, Gao GF.

[1] CAS Key Laboratory of Pathogenic Microbiology and Immunology, Institute of Microbiology, Chinese Academy of Sciences (CAS), Beijing, China. [2] College of Life Sciences, University of Science and Technology of China, Hefei, China. [3] These authors contributed equally to this work.
Abstract

Influenza A virus neuraminidase can be classified into groups 1 and 2 on the basis of its primary structure. The main structural feature of group 1 neuraminidase is an extra cavity in the active site, the 150-cavity. Here we present the crystal structure of neuraminidase from the 2009 pandemic H1N1 influenza strain. In contrast to other characterized N1 neuraminidases, which are all members of group 1, 2009 H1N1 neuraminidase does not have a 150-cavity.

PMID: 20852645 [PubMed - as supplied by publisher]

http://www.ncbi.nlm.nih.gov/pubmed/20852645

 

[tetano]

Re: The 2009 pandemic H1N1 neuraminidase N1 lacks the 150-cavity in its active site

Chinese scientists revealed: why young people are vulnerable


Abstract: Recently, Chinese Academy of Sciences Institute of Microbiology high fu discussion group on the 2009 influenza A H1N1 influenza virus hemagglutinin surface protein of two important (HA) and neuraminidase (NA) of a breakthrough reveals why young A flow of the virus susceptible, while the elderly have more resistance to the biological reasons. Recently, the Chinese Academy of Sciences Institute of Microbiology high fu discussion group on the 2009 influenza A H1N1 influenza virus hemagglutinin surface protein of two important (HA) and neuraminidase (NA) of a breakthrough, revealed why the young people a Flow virus susceptible, while the elderly have more resistance to the biological reasons.
Fu and other selected high in March 2009 outbreak in Mexico, a flow of a typical strain of the virus HA and NA was studied by X-ray diffraction analysis of their crystal structure. Analysis of the HA structure, with the 1918 pandemic influenza HA, the overall height of the structure and antigen-bit similar to seasonal influenza vary widely speculated that a flow of the HA could be influenza serum 1918 and. This view explains why a flow of young people susceptible to the virus, while the elderly have more resistance. Gao Fu said: "The 1918 flu virus may last for a long period of time, during which time the person born on or before, if infected, it will produce immunity and immune memory. "
In addition, the researchers also found that a flow of HA compared with seasonal flu and the 1918HA, one more glycosylation sites. The site may interfere with antibody recognition, leading to reduced virulence, low toxicity and immunity to maintain dynamic balance of forces in order to ensure a large number of amplification in the host body.
High-fu said, A-type influenza virus NA 9 subtypes, can be divided into two groups. Among them, Group 1 NA three-dimensional structure of the main features of the formation of a cavity in a particular area, known as the 150 - hole. According to this particular 150 - hole can be designed and synthesized some new NA inhibitors. A stream is a typical virus NA Group 1, but its crystal structure analysis found no 150 - hole, which indicated that for the 150 - a flow hole of the drugs on the efficiency of the virus weakened or even invalid. This will guide the design of drugs.
According to reports, the research project is in the Chinese Academy of Sciences influenza pandemic emergency start-up projects and the Ministry of Science and pandemic influenza 973 projects completed under the joint auspices. Research published online in the September 19 issue of "Nature" magazine sub s "Nature - Structural and Molecular Biology." (YUAN Zhi-yong)

http://www.ebiotrade.com/newsf/2010-9/2010926143647286.htm