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Related post: PERIOD COVERED
October 1, 1989 to September 30, Buy Eskalith 1990
TITLE OF PROJECT (80 characters or less. Title must fit on one line between the borders)
Expression of Selected Dengue E Protein Sequences by Recombinant Vaccinia Viruses
PRINCIPAL INVESTIGATOR (Ust other professional personnel below the Pnncipal Invesogator ) (Name, title, laboratory, and institute affiliation)
PI: Michael Bray, M.D. Senior Staff Fellow LID, NTAID
Others: Lewis Markoff, M.D. Medical Officer LID, MAID
Ching-Juh Lai, Ph.D. Head, MVB Section LID, NIAID
Robert M. Chanock, M.D. Chief LID, NIAID
COOPERATING UNITS (if any)
LVD, NIAID, NIH (B. Moss)
LAB/BRANCH
Laboratory of Infectious Diseases
SECTION
Molecular Viral Biology Section
INSTITUTE AND LOCATION
NIAID, NIH, Bethesda, MP 20892
TOTAL MAN-YEARS:
0.7
PROFESSIONAL:
0.4
0.3
CHECK APPROPRIATE BOX(ES)
□ (a) Human subjects □ (b) Human tissues lj3 (c) Neither
□ (a1) Minors
□ (a2) Interviews
SUMMARY OF WORK (Use standard unreduced type. Do not exceed the space provided.)
Recombinant vaccinia viruses expressing dengue type 4 virus (D4) and dengue type 2
virus (D2) proteins from cloned DNA were constructed for evaluation in experimental
immunoprophylaxis. Previously we showed that mice immunized with recombinant vaccinia
viruses which expressed the D4 pre-M and E glycoproteins, or E alone, were protected against
homotypic dengue virus encephalitis. However, an attempt ,to prevent dengue viremia in rhesus
monkeys by immunization with a vaccinia virus recombinant expressing pre-M, E and non-
structural protein NS1 was unsuccessful. Mice immunized with an E recombinant developed a
low level of neutralizing antibodies, but antibodies were not detectable by radio-
immunoprecipitation. Recently, recombinants expressing pre-M and E of the S- 1 candidate live
vaccine strain of D2 virus induced solid protection in mice against challenge with 100 LD 50 of
D2 strain New Guinea C. A recombinant expressing D2 E alone induced only partial protection
against D2 challenge, in contrast to complete homotypic protection provided by a D4 E
recombinant. A recombinant which expressed the N-terminal 79% of D2 E, that is secreted into
the medium, induced a strong antibody response to E in immunized mice and provided solid
protection against homotypic virus challenge equivalent to that provided by vD2 pM-E. Prior
infection with a vaccinia recombinant expressing apparently authentic E did not prime the antibody
response to subsequent Eskalith 450 Mg immunization with dengue virus or baculovirus expressed E. An analysis
of vaccinia recombinants that expressed E fusion proteins, in which the N-terminal half consisted
of D4 E and the C-terminal half of D2 E, or vice-versa failed to identify the region of the E
molecule responsible for eliciting a type specific protective immune response.
1 1-44
PHS 6040 (Rev. 1/W) SPO ll*iil
PROJECT NUMBER
DEPARTMENT OF HEALTH AND HUMAN SERVICES - PUBLIC HEALTH SERVICE ■
NOTICE OF INTRAMURAL RESEARCH PROJECT ! Z01 AI 00500-04 LID
PERIOD COVERED
October 1, 1989 to September 30, 1990
TITLE OF PROJECT (80 characters or less. Title must lit on one line between the borders)
Processing and Immunogenicity of Dengue Type 4 Virus Nonstructural Protein NS 1
PRINCIPAL INVESTIGATOR (Ust other professional personnel below the Principal Investigator.) (Name, title, laboratory, and institute Eskalith Cr affiliation)
PI: Barry Falgout, Ph.D. Staff Fellow LID, NIAID
Others: Ching-Juh Lai, Ph.D. Head, MVB Section LID, NIAID
Michael Bray, M.D. Senior Staff Fellow LID,NIAID
COOPERATING UNITS (if any)
Rochester General Hospital (Schlesinger)
LAB/BRANCH
Laboratory of Infectious Diseases
SECTION
Molecular Viral Biology Section
INSTITUTE AND LOCATION
NIAID, Eskalith Er NTH, Bethesda, MD 20892
TOTAL MAN- YEARS:
0.6
PROFESSIONAL:
0.4
0.2
CHECK APPROPRIATE BOX(ES)
13 (a) Human subjects □ (b) Human tissues □ (c) Neither
□ (a1) Minors
□ (a2) Interviews
SUMMARY OF WORK (Use standard unreduced type. Do not exceed the space provided.)
We studied the processing of dengue virus nonstructural protein NS1 by in vitro
transcription/translation, and in vivo as expressed by recombinant vaccinia virus. In vitro, the full
length NS1-NS2A precursor was made, and was translocated into dog pancreas microsomal
membranes and glycosylated, but NS 1/NS2A cleavage did not occur. In vivo, brefeldin A blocked
secretion of NS1 but did not inhibit NS1/NS2A cleavage. Jaken together, these results suggest
that NS 1/NS2A cleavage occurs in the Golgi, or in a compartment between the ER and the Golgi.
We constructed vaccinia recombinant viruses expressing chimeric preM-NSl(3/8)-NS2A proteins,
containing only the 3 or 8 C-terminal amino acid residues of NS1. We observed that the chimera
with Eskalith Cr 450 8 residues of NS1 was cleaved at the NS1-NS2A junction. Thus, the only portion of NS1
required for NS 1/NS2A cleavage is the region containing the 8 C-terminal amino acids. Results
with analogous NS5-NSl(3/8)-NS2A chimeras showed that these proteins were partially cleaved
to about the same extent. These results suggest, that the cleavage efficiency and NS1 target size
are both reduced when the NS1-NS2A junction is not translocated into the ER.
1 1-45
PHS 6040 (Rev. 1/84) Lithium Eskalith cf*° »14-»H
PROJECT NUMBER
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