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Displaying record number 165

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MAb ID	10E7
HXB2 Location	Pol(92-102) DNA(2358..2390)	Pol Epitope Map
Author Location	Protease(38-45 HXB2)
Epitope	`MSLPGRWKPKM`	Epitope Alignment
Subtype	B
Ab Type
Neutralizing
Species (Isotype)	hamster(IgG)
Patient
Immunogen	vaccine
Keywords

Vaccine Details

Vaccine type	protein
Vaccine component	Protease

Notes

Showing 2 of 2 notes.

10E7: Similarity level of the 10E7 binding site pentapeptide WKPKM to the host proteome was low, with the low-similarity 5-mer occurring in the host proteome 0 times, indicating that this peptide can be used to elicit Abs for active/passive immunotherapy with low risk of cross-reaction with the host proteome. Kanduc2008
10E7: Immunodominant region of protease in Armenian hamster (but only weakly reactive in people, see: Bjorling1992) -- peptide MSLPGRWKP blocks protease binding Croix1993. Bjorling1992,Croix1993

References

Showing 3 of 3 references.

Croix1993 D. A. Croix, H. Y. Yeh, J. Sedlacek, R. B. Luftig, and P. D. Gottlieb. A Dominant Epitope of HIV-1 Protease Recognized by Hamster Monoclonal Antibodies. J. Acquir. Immune Defic. Syndr., 6:558-566, 1993. PubMed ID: 8496788. Show all entries for this paper.

Bjorling1992 E. Bjorling, L. Goobar-Larson, G. Utter, E. Norby, and F. Chiodi. Four Distinct Antigenic Regions Are Present in the Primary Structure of HIV-1 and HIV-2 Proteinases. AIDS, 6:157-163, 1992. PubMed ID: 1373063. Show all entries for this paper.

Kanduc2008 Darja Kanduc, Rosario Serpico, Alberta Lucchese, and Yehuda Shoenfeld. Correlating Low-Similarity Peptide Sequences and HIV B-Cell Epitopes. Autoimmun. Rev., 7(4):291-296, Feb 2008. PubMed ID: 18295732. Show all entries for this paper.

Displaying record number 166

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MAb ID	F11.2.32
HXB2 Location	Pol(92-102) DNA(2358..2390)	Pol Epitope Map
Author Location	Protease(36-46 BH10)
Epitope	`MSLPGRWKPKM`	Epitope Alignment
Ab Type	flap region
Neutralizing
Species (Isotype)	mouse(IgG1κ)
Patient
Immunogen	vaccine
Keywords	drug resistance, review, structure

Vaccine Details

Vaccine type	protein
Vaccine strain	B clade BH10
Vaccine component	Protease

Notes

Showing 4 of 4 notes.

F11.2.32: The antibody fragment scFvF11.2.32 inhibits of wild-type Protease and also has an inhibitory effect on Protease variants resistant to active-site inhibitors used as anti-AIDS drugs. Bartonova2008 (drug resistance)
F11.2.32: Review of the implications of antibody structure and antigen peptide binding for the mechanisms of inhibition of protease activity by two MABs with different binding sites in protease. Rezacova2002 (review, structure)
F11.2.32: Crystal structure of a Fab peptide complex was obtained. Distortion may occur in the flap region of the protein, important for regulating access of substrate to the catalytic site. Lescar1999 (structure)
F11.2.32: Binding leads to significant inhibition in proteolytic activity -- crystal structure of Fab-peptide was determined to 2.2 A resolution -- bound peptide shows no structural similarity to the corresponding segment in native protease suggesting binding may distort protein structure. Lescar1997 (structure)

References

Showing 5 of 5 references.

Lescar1996 J. Lescar, R. Stouracova, M. M. Riottot, V. Chitarra, J. Brynda, M. Fabry, M. Horejsi, J. Sedlacek, and G. A. Bentley. Preliminary crystallographic studies of an anti-HIV-1 protease antibody which inhibits enzyme activity. Protein Sci., 5:966-968, 1996. PubMed ID: 8732768. Show all entries for this paper.

Lescar1997 J. Lescar, R. Stouracova, M. M. Riottot, V. Chitarra, J. Brynda, M. Fabry, M. Horejsi, J. Sedlacek, and G. A. Bentley. Three-Dimensional Structure of an Fab-Peptide Complex: Structural Basis of HIV-1 Protease Inhibition by a Monoclonal Antibody. J. Mol. Biol., 267:1207-1222, 1997. (Genbank: U62632 U62633) F11.2.32 is a MAb raised against HIV-1 protease which inhibits proteolytic activity. The structure of the complex of the Fab fragment and the synthetic peptide that it binds to, residues 36 to 46 of protease, have been determined at 2.2 AA resolution, and that of the Fab in the free state has been determined at 2.6 AA resolution. The conformation of the bound peptide shows no overall structural similarity to the corresponding segment in HIV-1 protease. PubMed ID: 9150407. Show all entries for this paper.

Lescar1999 J. Lescar, J. Brynda, P. Rezacova, R. Stouracova, M. M. Riottot, V. Chitarra, M. Fabry, M. Horejsi, J. Sedlacek, and G. A. Bentley. Inhibition of the HIV-1 and HIV-2 Proteases by a Monoclonal Antibody. Protein Sci., 8:2686-2696, 1999. PubMed ID: 10631984. Show all entries for this paper.

Rezacova2002 P. Rezacova, J. Brynda, M. Fabry, M. Horejsi, R. Stouracova, J. Lescar, V. Chitarra, M. M. Riottot, J. Sedlacek, and G. A. Bentley. Inhibition of HIV Protease by Monoclonal Antibodies. J. Mol. Recognit., 15(5):272-276, Sep-Oct 2002. PubMed ID: 12447903. Show all entries for this paper.

Bartonova2008 Vanda Bartoňová, Vlastimil Král, Irena Sieglová, Jiří Brynda, Milan Fábry, Magdalena Hořejší, Milan Kožíšek, Klára Grantz Šašková, Jan Konvalinka, Juraj Sedláček, and Pavlina Řezáčová. Potent Inhibition of Drug-Resistant HIV Protease Variants by Monoclonal Antibodies. Antiviral Res., 78(3):275-277, Jun 2008. PubMed ID: 18329737. Show all entries for this paper.