Found 1 matching record:
Displaying record number 1862
Download this epitope
record as JSON.
MAb ID |
C8 (VHH C8) |
HXB2 Location |
Env |
Env Epitope Map
|
Author Location |
Env |
Research Contact |
Robin A Weiss, University Colledge London, London, UK, r.weiss@ucl.ac.uk |
Epitope |
|
Ab Type |
gp120 CD4BS |
Neutralizing |
P View neutralization details |
Species
(Isotype)
|
llama |
Patient |
|
Immunogen |
vaccine |
Keywords |
antibody binding site, antibody generation, binding affinity, kinetics, neutralization, subtype comparisons, vaccine antigen design, variant cross-reactivity |
Vaccine Details
Notes
Showing 3 of
3 notes.
-
C8: Novel llama VHH antibodies were derived by immunization of llamas with HIV-1 Env. The binding and neutralization potency of these new antibodies were compared with previously-characterized llama antibodies A12, D7, and C8, and human antibody b12. C8 neutralized 8/26 predominantly tier 2 viruses tested.
Strokappe2012
(neutralization, binding affinity)
-
C8 database comment: there are two distinct antibodies in the database named C8.
-
C8: C8 is a neutralizing VHH (nanobody) Ab devoid of light chains. It was isolated from sera from llamas, who produce immunoglobulins devoid of light chains, immunized with gp120 of HIV-1 CRF07_BC primary isolate CN54, following panning of phage libraries expressing VHH repertoire and a competitive elution with soluble CD4. It was hypothesized that the small size of the VHH, in combination with their protruding CDR3 loops, and their preference for cleft recognition and binding into active sites, may allow for recognition of conserved motifs on gp120 that are occluded from conventional Abs. C8 was able to neutralize HIV-1 primary isolates of subtypes B, C and CRF07_BC, but not subtypes A, D, and A/G. Compared to MAb b12, which neutralized 54% of viruses tested, C8 neutralized 35% of the viruses, but it neutralized a different spectrum of the viruses than b12. C8 showed high affinity binding to IIIB gp120, with a fast off-rate, and inhibited binding of sCD4 to IIIB gp120 and 92UG037 gp140 in a dose-dependent manner. C8 was found to compete with b12 for binding to gp120, and also with MAbs 654-D and GP68, indicating that its epitope overlaps the CD4bs. There was some inhibition observed of C8-gp120 binding by 2G12, 17b, and 447-52D, while 4E10 did not inhibit C8-gp120 binding. C8 was also able to inhibit binding of the other two VHH Abs isolated in this study, A12 and D7, indicating that their epitopes overlap.
Forsman2008
(antibody binding site, antibody generation, neutralization, vaccine antigen design, variant cross-reactivity, kinetics, binding affinity, subtype comparisons)
References
Showing 2 of
2 references.
Isolation Paper
Forsman2008
Anna Forsman, Els Beirnaert, Marlén M. I. Aasa-Chapman, Bart Hoorelbeke, Karolin Hijazi, Willie Koh, Vanessa Tack, Agnieszka Szynol, Charles Kelly, Áine McKnight, Theo Verrips, Hans de Haard, and Robin A Weiss. Llama Antibody Fragments with Cross-Subtype Human Immunodeficiency Virus Type 1 (HIV-1)-Neutralizing Properties and High Affinity for HIV-1 gp120. J. Virol., 82(24):12069-12081, Dec 2008. PubMed ID: 18842738.
Show all entries for this paper.
Strokappe2012
Nika Strokappe, Agnieszka Szynol, Marlèn Aasa-Chapman, Andrea Gorlani, Anna Forsman Quigley, David Lutje Hulsik, Lei Chen, Robin Weiss, Hans de Haard, and Theo Verrips. Llama Antibody Fragments Recognizing Various Epitopes of the CD4bs Neutralize a Broad Range of HIV-1 Subtypes A, B and C. PLoS One, 7(3):e33298, 15 Mar 2012. PubMed ID: 22438910.
Show all entries for this paper.