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Scientists identify lab-made proteins that neutralize multiple strains of seasonal and pandemic flu
Date:2/22/2009

of the influenza virus to which their monoclonal antibodies bind. The hidden part of the influenza virus is in the neck below the peanut-shaped head of the hemagglutinin (HA) protein. HA and neuraminidase are the two main surface proteins on the influenza virus.

The scientists also identified a new mechanism of antibody action against influenza: Once the antibody binds, the virus cannot change its shape, a step required before it can fuse with and enter the cell it is attempting to infect.

Dr. Marasco, Jianhua Sui, M.D., Ph.D., and other Dana-Farber colleagues began their study with avian flu viruses. They scanned tens of billions of monoclonal antibodies produced in bacterial viruses, or bacteriophages, and found 10 antibodies active against the four major strains of H5N1 avian influenza viruses. Encouraged by these findings, they collaborated with Ruben O. Donis, Ph.D., of the CDC Influenza Division, and found that three of these monoclonal antibodies had broader neutralization capabilities when tested in cell cultures and in mice against representative strains of other known influenza A viruses.

Influenza A viruses can include any one of the 16 known subtypes of HA proteins, which fall into two groups, Group 1 and Group 2. Their monoclonal antibodies neutralized all testable viruses containing the 10 Group 1 HAs--which include the seasonal H1 viruses, the H1 virus that caused the 1918 pandemic and the highly pathogenic avian H5 subtypes--but none of the viruses containing the six Group 2 HAs.

Simultaneously, Dr. Marasco's group teamed up with Robert C. Liddington, Ph.D., professor and chair of the Infectious and Inflammatory Disease Center at Burnham, to determine the atomic structure of one of their monoclonal antibodies bound to the H5N1 HA. Their detailed picture shows one arm of the antibody inserted into a genetically stable pocket in the neck of the HA protein, an interaction that blocks the shape change required for
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Contact: Laurie K. Doepel
doepel@nih.gov
301-402-1663
NIH/National Institute of Allergy and Infectious Diseases
Source:Eurekalert

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