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MAb ID	178.1 (178.1.1)
HXB2 Location	gp160(305-309) DNA(7137..7151)	gp160 Epitope Map
Author Location	gp120(305-309 BH10)
Research Contact	C. Thiriart, Smith Kline and MRC AIDS reagent project
Epitope	`KSIRI`	Epitope Alignment
Ab Type	gp120 V3 // V3 glycan (V3g)
Neutralizing	L
Species (Isotype)	mouse(IgG2a)
Patient
Immunogen	vaccine
Keywords	antibody binding site, antibody interactions, contact residues, dendritic cells, neutralization, novel epitope, optimal epitope

Vaccine Details

Vaccine type	protein
Vaccine strain	B clade IIIB
Vaccine component	Env

Notes

Showing 7 of 7 notes.

178.1: mAbs binding to the tip of a loop on the principal neutralizing domain (PND) of HIV-1, strain HTLV IIIB, were fine-mapped by Pepscan analysis to their optimal epitopes and their affinity studied. Epitope KSIRIQRGP was found to bind 178.1 (amino acid 305-313) with the optimal core being KSIRI. 307I had no contribution to binding, but all other core residues had major contributions to binding and antigenicity. 178.1 neutralizes HIV clone HX10 but not HXB3. As compared to mAbs 110.5 and 110.6, 178.1 had about 6x lower neutralizing activity. Langedijk1992 (antibody binding site, antibody interactions, optimal epitope, contact residues, novel epitope)
178.1.1: This Ab did not inhibit HIV-1 BaL replication in macrophages or in PHA-stimulated PBMCs. Holl2006 (neutralization, dendritic cells)
178.1: UK Medical Research Council AIDS reagent: ARP331.
178.1: 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 -- binding of GalCer to gp120 inhibited but did not completely block MAb binding. Cook1994
178.1: gp41 amino acid substitutions 668 (N/S) and 675 (I/M) in gp41 interfere with 5023s neutralization potency, region 662-675 is ELDKWANLWNWFNI. Back1993
178.1: Called 178.1.1 -- conformational, does not bind well to denatured gp120. Moore1993a
178.1: Reacts to gp120 and gp160 in RIPA EIA and immunoblot. Thiriart1989

References

Showing 6 of 6 references.

Back1993 N. K. T. Back, L. Smit, M. Schutten, P. L. Nara, M. Tersmette, and J. Goudsmit. Mutations in Human Immunodeficiency Virus Type 1 gp41 Affect Sensitivity to Neutralization by gp120 Antibodies. J. Virol., 67:6897-6902, 1993. Three closely related clones were derived from a neutralization resistant IIIB isolate that had been passaged in a chimpanzee. gp41 mutations were shown to profoundly alter the ability of V3 loop MAbs 5023 and 178.1 to neutralize. Critical substitutions in gp41 were 668 and 675, close to the immunogenic domain 662-668, or ELDKWAS. Less profound inhibition was observed for the anti-CD4 binding site MAb GP13. PubMed ID: 8411395. 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.

Holl2006 Vincent Holl, Maryse Peressin, Thomas Decoville, Sylvie Schmidt, Susan Zolla-Pazner, Anne-Marie Aubertin, and Christiane Moog. Nonneutralizing Antibodies Are Able To Inhibit Human Immunodeficiency Virus Type 1 Replication in Macrophages and Immature Dendritic Cells. J. Virol., 80(12):6177-6181, Jun 2006. PubMed ID: 16731957. Show all entries for this paper.

Langedijk1992 J. P. M. Langedijk, N. K. T. Back, E. Kinney-Thomas, C. Bruck, M. Francotte, J. Goudsmit, and R. H. Meloen. Comparison and Fine Mapping of Both High and Low Neutralizing Monoclonal Antibodies against the Principal Neutralization Domain of HIV-1. Arch. Virol., 126:129-146, 1992. PubMed ID: 1381908. Show all entries for this paper.

Moore1993a J. P. Moore and D. D. Ho. Antibodies to discontinuous or conformationally sensitive epitopes on the gp120 glycoprotein of human immunodeficiency virus type 1 are highly prevalent in sera of infected humans. J. Virol., 67:863-875, 1993. CD4BS antibodies are prevalent in HIV-1-positive sera, while neutralizing MAbs to C4, V2, and V3 and MAbs to linear epitopes are less common. Most linear epitope MAbs in human sera are directed against the V3 region, and cross-reactive MAbs tend to be directed against discontinuous epitopes. PubMed ID: 7678308. Show all entries for this paper.

Thiriart1989 C. Thiriart, M. Francotte, J. Cohen, C. Collignon, A. Delers, S. Kummert, C. Molitor, D. Gilles, P. Roelants, F. Van Wijnendaele, M. De Wilde, and C. Bruck. Several Antigenic Determinants Exposed on the gp120 Moiety of HIV-1 gp160 Are Hidden on the Mature gp120. J. Immunol., 143:1832-1836, 1989. PubMed ID: 2476484. Show all entries for this paper.