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Displaying record number 37

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MAb ID	2A6
HXB2 Location	Gag	Gag Epitope Map
Author Location	p17
Research Contact	A. O. Arthur, Frederick Cancer Research and Development Center, Frederick, MD
Epitope
Ab Type
Neutralizing
Species (Isotype)
Patient
Immunogen
Keywords

Notes

Showing 1 of 1 note.

2A6: Part of a panel of 17 MAbs used as controls testing for the dual specificity of MAb G11H3 for both p17 and mycoplasma. Pincus1998

References

Showing 1 of 1 reference.

Pincus1998 S. H. Pincus, R. L. Cole, R. Watson-McKown, A. Pinter, W. Honnen, B. Cole, and K. S. Wise. Immunologic Cross-Reaction between HIV Type 1 p17 and Mycoplasma hyorhinis Variable Lipoprotein. AIDS Res. Hum. Retroviruses, 14:419-425, 1998. PubMed ID: 9546801. Show all entries for this paper.

Displaying record number 38

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MAb ID	G11H3 (12A-Gllh3)
HXB2 Location	Gag	Gag Epitope Map
Author Location	p17
Epitope
Ab Type
Neutralizing
Species (Isotype)	rat(IgG2a)
Patient
Immunogen
Keywords	antibody generation

Notes

Showing 2 of 2 notes.

Reacted strongly with live cells, but did not possess any measurable virus-neutralizing activities. Shang1991 (antibody generation)
G11H3: This MAb is cross-reactive between p17 and mycoplasma -- this antibody binds strain specifically to the variable lipoprotein (Vlp) F of M. hyorhinis, in the region of the carboxy-terminal repeat CGGSTPTPEQGNNQGGSTPTPEQGNSQVSK -- the p17 epitope is discontinuous, but p17 and Vlp F share the tetrapeptide SQVS. Pincus1998

References

Showing 2 of 2 references.

Isolation Paper
Shang1991 F. Shang, H. Huang, K. Revesz, H.-C. Chen, R. Herz, and A. Pinter. Characterization of monoclonal antibodies against the human immunodeficiency virus matrix protein, p17gag: identification of epitopes exposed at the surfaces of infected cells. J. Virol., 65:4798-4804, 1991. Six MAbs with linear epitopes were mapped. These Abs could only bind to HIV-infected cells that had been permeablized with acetone. Only G11g1 and G11h3, two antibodies that did not bind to peptides, but only to intact p17, could react with live HIV-1 infected cells. These antibodies were not neutralizing. PubMed ID: 1714518. Show all entries for this paper.

Displaying record number 488

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MAb ID	924
HXB2 Location	gp160(304-314) DNA(7134..7166)	gp160 Epitope Map
Author Location	gp120(309-318 IIIB)
Epitope	`RKSIRIQRGPG`	Epitope Alignment
Ab Type	gp120 V3 // V3 glycan (V3g)
Neutralizing
Species (Isotype)	mouse(IgG1κ)
Patient
Immunogen	vaccine
Keywords

Vaccine Details

Vaccine type	vaccinia
Vaccine strain	B clade IIIB
Vaccine component	gp160

Notes

Showing 6 of 6 notes.

924: A panel of immunotoxins were generated by linking Env MAbs to ricin A -- immunotoxins mediated cell killing, but killing was not directly proportional to binding. Pincus1996
924: MAbs against the glycosphingolipid GalCer block HIV infection of normally susceptible CD4 negative cells from the brain and colon -- this MAb can inhibit gp120 binding to GalCer in vitro. Cook1994
924: Ab response in IIIB lab workers was compared to gp160 LAI vaccine recipients -- MAb 924 was used as a control -- infected lab workers and a vaccinia gp160 vaccine had strong V3 MAb response, but alum absorbed rec gp160 did not generate anti-V3 response. Pincus1993a
924: MAb was coupled to ricin A chain (RAC) -- immunotoxin efficacy was not significantly decreased by sCD4, although the efficacy of gp41 MAb immunotoxins in vitro increased 30-fold by sCD4. Pincus1993
924: Epitope sequence is based on database count of a specified location -- 924-RAC immunotoxin is IIIB strain-specific. Pincus1991
924: HIV IIIB strain specific. Chesebro1988

References

Showing 7 of 7 references.

Chesebro1988 B. Chesebro and K. Wehrly. Development of a Sensitive Quantitative Focal Assay for Human Immunodeficiency Virus Infectivity. J. Virol., 62:3779-3788, 1988. PubMed ID: 3047430. Show all entries for this paper.

Pincus1991 S. H. Pincus, R. L. Cole, E. M. Hersh, D. Lake, Y. Masuho, P. J. Durda, and J. McClure. In Vitro Efficacy of Anti-HIV Immunotoxins Targeted by Various Antibodies to the Envelope Protein. J. Immunol., 146:4315-4324, 1991. Six MAbs, (907, 924, 110.1, 41.1, 86 and P5-3) and polyclonal pooled serum antibodies purified on gp160 were coupled to RAC to create immunotoxins. Only 41.1-RAC, an anti-gp41 MAb-immunotoxin and the polyclonal immunotoxin showed direct activity against multiple strains, and activity of an immunotoxin was found not to be directly correlated with cell surface binding. PubMed ID: 1710247. Show all entries for this paper.

Pincus1993 S. H. Pincus and J. McClure. Soluble CD4 Enhances the Efficacy of Immunotoxins Directed against gp41 of the Human Immunodeficiency Virus. Proc. Natl. Acad. Sci. U.S.A., 90:332-336, 1993. PubMed ID: 8419938. Show all entries for this paper.

Pincus1993a S. H. Pincus, K. G. Messer, D. H. Schwartz, G. K. Lewis, B. S. Graham, W. A. Blattner, and G. Fisher. Differences in the Antibody Response to Human Immunodeficiency Virus-1 Envelope Glycoprotein (gp160) in Infected Laboratory Workers and Vaccinees. J. Clin. Invest., 91:1987-1996, 1993. PubMed ID: 7683694. Show all entries for this paper.

Cook1994 D. G. Cook, J. Fantini, S. L. Spitalnik, and F. Gonzalez-Scarano. Binding of Human Immunodeficiency Virus Type 1 HIV-1 gp120 to Galactosylceramide (GalCer): Relationship to the V3 Loop. Virol., 201:206-214, 1994. Antibodies against GalCer can block infection of CD4-negative cells from the brain and colon that are susceptible to HIV infection. This paper explores the ability of a panel of MAbs to inhibit binding of gp120 to GalCer, and also of the binding of GalCer to inhibit MAb-gp120 interaction. MAbs to the V3 loop and GalCer showed mutual inhibition of binding to gp120, and anti-CD4 binding site MAbs showed reduced inhibition. N- and C-terminal MAbs didn't influence GalCer binding. PubMed ID: 8184533. Show all entries for this paper.

Pincus1996 S. H. Pincus, K. Wehrly, R. Cole, H. Fang, G. K. Lewis, J. McClure, A. J. Conley, B. Wahren, M. R. Posner, A. L. Notkins, S. A. Tilley, A. Pinter, L. Eiden, M. Teintze, D. Dorward, and V. V. Tolstikov. In Vitro Effects of Anti-HIV Immunotoxins Directed against Multiple Epitopes on HIV Type 1 Envelope Glycoprotein 160. AIDS Res. Hum. Retroviruses, 12:1041-1051, 1996. A panel of anti-gp160 MAbs to was used to construct anti-HIV immunotoxins by coupling antibodies to ricin A chain (RAC). The ability of the immunotoxins to kill HIV-1-infected cells was tested in tissue culture. Immunotoxins that bind epitopes on the cell surface killed infected cells, although killing was not directly proportional to binding. The activity of anti-gp41 immunotoxins was markedly enhanced in the presence of sCD4. PubMed ID: 8827220. Show all entries for this paper.

Displaying record number 799

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MAb ID	41-1 (41.1, gp41-1)
HXB2 Location	gp160(579-608) DNA(7959..8048)	gp160 Epitope Map
Author Location	gp41(584-609 LAV)
Epitope	`RILAVERYLKDQQLLGIWGCSGKLICTTAV`	Epitope Alignment
Ab Type
Neutralizing
Species (Isotype)	mouse(IgG1κ)
Patient
Immunogen	vaccine
Keywords	antibody binding site, antibody generation

Vaccine Details

Vaccine type	protein
Vaccine component	gp160

Notes

Showing 7 of 7 notes.

41-1: Called 41.1, and described as a human MAb, binding 579-604 -- a panel of immunotoxins was generated by linking Env MAbs to ricin A -- immunotoxins mediated cell killing, but killing was not directly proportional to binding. Pincus1996
41-1: Did not require the C-C disulfide bridge and loop formation, can bind simultaneously with 9-11. MAb 4-1 is described as being raised against gp160 in mouse, cited to Dr K. Shriver, Genetic Systems Corp, Seattle WA (no published reference given, but Shriver was a coauthor of Gosting1987). Mani1994
41-1: Called 41.1, and described as a human MAb -- cross-competes with 41.4 -- sCD4 enhances the efficacy of immunotoxins in vitro 30-fold -- MAb was coupled to ricin A chain (RAC). Pincus1993
41-1: Described as mouse MAb 41.1 cited to Gostling1987. Efficacious as an immunotoxin when coupled to RAC -- gave linear epitope as gp160 579-603. Pincus1991
41-1: Broadly reactive. Gosting1987 (antibody binding site, antibody generation)
41-1 database comment: Also called 41.1, although possibly not, the literature is confusing because two gp41 MAbs that bind to this region with similar names (dash versus period) are listed as murine and human.
41-1 database comment: This antibody to gp41(584-609) Mani1994 seems to have been named the same as a different MAb to gp41(735-752 IIIB) Dalgleish1988.

References

Showing 7 of 7 references.

Isolation Paper
Gosting1987 L. H. Gosting, J. McClure, E. S. Dickinson, S. M. Watanabe, K. Shriver, and L. C. Goldstein. Monoclonal antibodies to gp110 and gp41 of human immunodeficiency virus. J. Clin. Microbiol., 25:845-848, 1987. PubMed ID: 2438302. Show all entries for this paper.

Thomas1988 E. Kinney Thomas, J. N. Weber, J. McClure, P. R. Clapham, M. C. Singhal, M. K. Shriver, and R. A. Weiss. Neutralizing Monoclonal Antibodies to the AIDS Virus. AIDS, 2:25-29, 1988. PubMed ID: 2451922. Show all entries for this paper.

Mani1994 J.-C. Mani, V. Marchi, and C. Cucurou. Effect of HIV-1 Peptide Presentation on the Affinity Constants of Two Monoclonal Antibodies Determined by BIAcore Technology. Mol. Immunol., 31:439-444, 1994. Two MAbs are described; one 41-1 did not require the Cys-Cys disulfide bridge and loop formation, the other 9-11 depends on loop formation. PubMed ID: 7514268. Show all entries for this paper.