Document 1
DOCN 000365079
AN   94378593.
AU   Roberts-P-L. Walker-C-P. Feldman-P-A.
IN   Bio Products Laboratory, Elstree, UK.
TI   Removal and inactivation of enveloped and non-enveloped viruses during
the purification of a high-purity factor IX by metal chelate affinity
chromatography.
SO   Vox-Sang.  1994.  67 Suppl 1().  P 69-71.
JT   Vox Sang.
PT   JOURNAL-ARTICLE.
LG   Eng.
AB   Virus reduction during the copper chelate affinity chromatography stage
used during the purification of a new high-purity factor IX (BPLs 9MC)
has been investigated.  Virus reduction for the enveloped virus Sindbis
was 6.5 log, a value which included approximately 2 log of inactivation
due to the use of an acidic wash buffer (pH 4.4) during chromatography.
In the case of the non-enveloped hepatitis-A-like poliovirus, which is
acid-resistant, the virus reduction value was 4.0 log and was exclusively
due to physical virus removal during the chromatographic process.
Author-abstract.
MJ   CHROMATOGRAPHY-AFFINITY.  DRUG-CONTAMINATION: prevention-and-control.
FACTOR-IX: isolation-and-purification.  POLIOVIRUSES.  SINDBIS-VIRUS.
MN   CHELATING-AGENTS.  CHROMATOGRAPHY-AFFINITY: methods.  COPPER.  HUMAN.
PLASMA: microbiology.  VIRAL-ENVELOPE-PROTEINS.
RN   0 -- Chelating-Agents.  0 -- Viral-Envelope-Proteins.  7440-50-8 --
Copper.  9001-28-9 -- Factor-IX.
SB   M.
YR   94.
IS   0042-9007.  XLI.
CY   SWITZERLAND.
IM   9412.
ND   941019.
        Document 2
DOCN 000365016
AN   94378530.
AU   Lee-H. Ricker-P-D. Brown-D-T.
IN   Department of Microbiology, University of Texas at Austin 78713-7640.
TI   The configuration of Sindbis virus envelope proteins is stabilized by the
nucleocapsid protein.
SO   Virology.  1994 Oct.  204(1).  P 471-4.
JT   Virology.
PT   JOURNAL-ARTICLE.
LG   Eng.
AB   We have previously provided evidence that a strong and precise
interaction of the Sindbis virus nucleocapsid with the cytoplasmic tail
of E2 is critical for the function of the mature virion and that changes
in this association may affect infectivity (21).  In this study, we
examined the effects of temperature-sensitive defects in capsid protein
on virus infectivity and glycoprotein function.  The two Sindbis virus
mutants chosen were ts2 and Ser180/Gly183, which contain amino acid
substitutions in their capsid proteins.  Heating these mutants to 60
degrees C results in a loss of infectivity significantly greater than the
loss observed in wild type viruses.  Viral glycoprotein-mediated fusion
from without using heat-treated virions occurs normally with wild type
viruses but is lost in the mutants.  These results suggest that defects
in the capsid protein can induce a loss of infectivity through secondary
conformational changes in the virus envelope glycoproteins and that the
function of the virus envelope is dependent upon specific capsid-E2
interactions.  Author-abstract.
MJ   CAPSID: metabolism.  SINDBIS-VIRUS: chemistry.  VIRAL-ENVELOPE-PROTEINS:
metabolism.
MN   ANIMAL.  CAPSID: chemistry.  CELL-FUSION.  CELL-LINE.
CROSS-LINKING-REAGENTS.  HAMSTERS.  HEAT.  MUTATION: physiology.
PROTEIN-CONFORMATION.  SUCCINIMIDES.  SUPPORT-NON-U-S-GOV'T.
SUPPORT-U-S-GOV'T-P-H-S. VIRAL-ENVELOPE-PROTEINS: chemistry, physiology.
RN   0 -- glycoprotein-E2-Sindbis-virus.  0 -- Capsid.  0 --
Cross-Linking-Reagents.  0 -- Succinimides.  0 --
Viral-Envelope-Proteins.  112241-19-7 --
4-succinimidyloxycarbonyl-alpha-methyl-alpha-2-pyridyldithio-toluene.
SB   M. X.
YR   94.
IS   0042-6822.  XEA.
CY   UNITED STATES.
IM   9412.
ND   941020.
NO   AI 14710 AI NIAID.