Journal
BIOCHEMISTRY
Volume 45, Issue 1, Pages 324-330Publisher
AMER CHEMICAL SOC
DOI: 10.1021/bi050675k
Keywords
-
Categories
Funding
- Intramural NIH HHS Funding Source: Medline
Ask authors/readers for more resources
We have induced a polyclonal IgG that degrades the HIV-1 surface antigen, glycoprotein gp120, by taking advantage of the susceptibility of SJL mice to a peptide-induced autoimmune disorder, experimental autoimmune encephalomyelitis (EAE). Specific pathogen-free SJL mice were immunized with structural fragments of gp120, fused in-frame with encephalitogenic peptide MBP85-101. It has resulted in a pronounced disease-associated immune response against antigens. A dramatic increase of gp120 degradation level by purified polyclonal IgG from immunized versus nonimmunized mice has been demonstrated by a newly developed fluorescence-based assay. This activity was inhibited by anti-mouse immunoglobulin antibodies as well as by Ser- and His-reactive covalent inhibitors. A dominant proteolysis site in recombinant gp120 incubated with purified polyclonal IgG from immunized mice was shown by SDS-PAGE. The SELDI-based mass spectrometry revealed that these antibodies exhibited significant specificity toward the Pro(484)-Leu(485) peptide bond. The sequence surrounding this site is present in nearly half of the HIV-1 variants. This novel strategy can be generalized for creating a catalytic vaccine against viral pathogens.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available