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1988 PROGRAM 0 a 3
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71 H .
t; 72 59h Fourteenth Annual Symposmm on
A.M. RM. 4; (D 0
9:00 Registration and Coffee-Room 137, 12:15 Lunch, Faculty Club o 3 '3
Chemistry-Physics Building (See enclosed card) 8 g (3
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9:30 Welcome by Presrdent David P. Roselle, 1215 Prof. Eckard Wimmer, State Umversnty of u K: g; m r! n
University of Kentucky, Room 139, New York at Stony Brook 8 x2 Che ISt a d
Chemistry-Physics Building Genetic Manipulations of Capsid Protein 01 0
Synthesis and the Formation of Neutraliza- U1 MOIecular 3101093]
9:35 Introductory Remarks . . .
tron Epitopes of Pollovuus
9:40 Prof. Roland R. Rueckert, University of
Wisconsin 2:15 Break
Picornavirus Vaccines and Chemotherapy 2:30 Dr. Mark A. McKinlay, Sterling-Winthrop
Past, Present, and Future Research Institute bl h d ' th f
The picornaviruses include a number of structurally similar Antiviral Activity of Compounds Which ln- eSta 15 e In 8 memory 0
pathogens including poliovirus, human rhinoviruses (common hibit Picornavirus Uncoating Anna S. Naff
cold), hepatitis A virus, and foot and mouth disease virus; hence A series of orally active antiviral agents which suppress picor-
they are historically important targets for vaccine development and navirus replication through an inhibition of the virion uncoating
contiriue to be key models for development 0f vaccines and an} process has been discovered and developed at the Sterling ___-','
tivira 5, Determination of their gene sequences and mapping 0 Winthro R hl ~ ~ _ '
J p esearc nstitute in Rensselaer, New York. These an .
antigenic sites and drug-resistance mutations within the tiviral agents have been shown to insert themselves in 'a STRUCTURE AND FUNCTION
3-dimensional structure of these viruses has heightened enthusiasm hydrophobic pocket within the virus capsid protein VPl, and to OF
N degelOPmSEAOf SVEtdheth peptide vaccines, valccinesdfrom induce large conformational changes (up to 5.5 A) in the viriorl . '
recom inant v an esign 0 improve neutra izing 195v structure. These conformational changes are thought to stabilize
but success still hinges upon mastery of new research frontiers. the virion and prevent uncoating or disassembly and the subse- SMALL RNA VIRAL PATHOGENS
Some problems and opportunities presented by the special hIOlOQV quent release of the infectious RNA. Representatives of this class ________
Of these viruses Will be discussed. of antiviral agents have a broad spectrum of in vitro antiviral ac
10340 Break tivity against the nesrly 200 serotypes of human rhinovirIstes arid
enteroviruses whic cause diseases ranging in severity rom t e S eakers
1050 Prof. Michael 6' Rossmann, Purdue common cold to life threatening paralytic poliomyelitis and p
University neonatal sepsis. In addition to the potent in vitro activity, these
What Doesnthe Molecular Structure 09 agents are orally effective in preventing paralysis and death in mice MICHAEL G . ROSSM ANN
Viruses Te Us About Viral Functions. -  - - -
. . Infected wrth human-enterowruses. A representative of'thisclass MARK A. MCKINLAY
The structures of the protein shell of a number of srmple of antwrral agents, disoxaril (WIN 51711), 15 currently in clinical
icosahedral RNA plant and animal viruses are now known at trials to evaluate its ability to treat picornavirus infections in man. ' ROLAND R- RUECKERT
atomic resolution. In addition, components'of viral capsids such 3:30 Informal Discussion, Room 137' Chemistry- ECKARD WIMMER
as the haemagglutinin and neuraminidase spikes of influenza Virus Ph i B ild'
and the hexon unit of adenovirus are known in similar detail. These ys cs u . mg  . _
structures have provided a wealth of information on viral assembly, We encourage symposrum part1c1pants, especrally students, to
viral disassembly, the antigenic surface on viruses available to take thls opportunity to meet mm the speakers. ,
neutralizing antibodies, the host cell receptor attachment site, fusion
of viral particles with the host cell, processing of polyproteins during Monday MarCh 28 1988
maturation and the manner in which antiviral agents can interfere Department Of Chemistry
With the function of a Viral capsid. University Of Kentucky
Lexington, Kentucky 40506-0055