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Amino acid residues confer temperature sensitivity to influenza virus strains.

Vaccine Weekly

| May 07, 2003 | COPYRIGHT 2003 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

2003 MAY 7 - (NewsRx.com & NewsRx.net) -- Multiple amino acid residues conferred temperature sensitivity to human influenza virus vaccine strains (FluMist) derived from cold-adapted A/Ann Arbor/6/60.

"FluMist influenza A vaccine strains contain the PB1, PB2, PA, NP, M, and NS gene segments of ca A/AA/6/60, the master donor virus-A strain. These gene segments impart the characteristic cold-adapted (ca), attenuated (att), and temperature-sensitive (ts) phenotypes to the vaccine strains. A plasmid-based reverse genetics system was used to create a series of recombinant hybrids between the isogenic non-ts wt A/Ann Arbor/6/60 and MDV-A strains to characterize the genetic basis of the ts phenotype, a critical, genetically stable, biological trait that contributes to the attenuation and safety of FluMist vaccines," scientists in the United States report.

"PB1, PB2, and NP derived from MDV-A each expressed determinants of temperature sensitivity and the combination of all three gene segments was synergistic, resulting in expression of the characteristic MDV-A ts phenotype," stated Hong Jin and colleagues at MedImmune Vaccines, Inc. in San Diego. "Site-directed mutagenesis analysis mapped the MDV-A ts phenotype to the ...

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Source: HighBeam Research, Amino acid residues confer temperature sensitivity to influenza virus...

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