home
***
CD-ROM
|
disk
|
FTP
|
other
***
search
/
The Pier Shareware 6
/
The_Pier_Shareware_Number_6_(The_Pier_Exchange)_(1995).iso
/
026
/
med9408e.zip
/
M9480848.TXT
< prev
next >
Wrap
Text File
|
1994-09-05
|
2KB
|
37 lines
Document 0848
DOCN M9480848
TI Monoclonal antibodies to the MLV protease active site that crossreact
with the HIV protease.
DT 9410
AU Luftig RB; Calkins P; Yeh HY; Louisiana State University Medical Center,
New Orleans.
SO Abstr Gen Meet Am Soc Microbiol. 1994;94:485 (abstract no. T-16). Unique
Identifier : AIDSLINE ASM94/94313097
AB The retroviral proteases are essential for cleavage of gag and gag-pol
polyproteins during the virus assembly. Inhibitors that inactivate the
protease activity will reduce production of mature particles and, thus,
spread of diseases. In this study, we generated mouse monoclonal
antibodies specific to protease active site. A thyroglobulin-conjugated
20-mer peptide of the murine leukemia virus (MLV) protease active site
(Q-P-V-T-F-L-V-D-T-G-A-Q-H-S-V-L-T-Q-N-P) was used to immunize BALB/c
mice. About 40 hybridomas were generated by fusion of spleen cells with
a mouse myeloma cell line. A peptide ELISA assay confirmed that the mAbs
reacted to the original 20-mer peptide. Further, using immunoblot
analysis, we found 13 hybridomas where the mAbs reacted with MLV
protease expressed in E. coli, as well with HIV protease. Currently, we
are mapping the common epitope using short peptides (6- to 8-mer). The
significance of these results may provide another avenue for developing
inhibitors that bind specifically to the catalytic site.
DE Amino Acid Sequence Animal *Antibodies, Monoclonal Antigenic
Determinants/*ANALYSIS Binding Sites Cloning, Molecular Cross
Reactions Enzyme-Linked Immunosorbent Assay/METHODS Escherichia coli
Hybridomas/ENZYMOLOGY HIV Protease/*IMMUNOLOGY/METABOLISM Leukemia
Viruses, Murine/*ENZYMOLOGY Mice Mice, Inbred BALB C/IMMUNOLOGY
Molecular Sequence Data Peptide
Peptidohydrolases/*IMMUNOLOGY/METABOLISM Recombinant
Proteins/IMMUNOLOGY MEETING ABSTRACT
SOURCE: National Library of Medicine. NOTICE: This material may be
protected by Copyright Law (Title 17, U.S.Code).