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ARS Home » Midwest Area » Ames, Iowa » National Animal Disease Center » Food Safety and Enteric Pathogens Research » Research » Publications at this Location » Publication #67971
Title: STRUCTURE/FUNCTION STUDIES OF THE CAPSID PROTEIN OF CALICIVIRUSES: DOMAIN SWAPS BETWEEN DIFFERENT FELINE CALICIVIRUS STRAINS

Author
item Neill, John
item SOSNOVTSEV, S - NATL INSTITUTES OF HEALTH
item GREEN, K - NATL INSTITUTES OF HEALTH

Submitted to: American Society for Virology Meeting
Publication Type: Abstract Only
Publication Acceptance Date: 7/17/1996
Publication Date: N/A
Citation: N/A

Interpretive Summary:

Technical Abstract: The caliciviruses are a family of viruses which are recently drawing more attention and data is now becoming available detailing their geneology and molecular biology. However, little is known concerning the function(s) of specific calicivirus proteins and the domains within these proteins. This is especially true of the single capsid protein. The capsid protein of the eanimal caliciviruses has been divided into 6 distinct regions (A-F) based on the degree of conservation of the amino acid sequences. Regions B and D are highly conserved, regions A and F shows a moderate degree of conservation and regions C and E are hypervariable. To examine the function of the B, C, D, E, and F regions, sequences encoding these domains from the FCV strains CFI, KCD, and NADC were used to replace the homologous sequences in the FCV Urbana infectious clone. The effect of the replacement sequences on antigenicity and viability of recombinant FCV was examined.