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Vaccine Details

Notes

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• JM4: A panel of bnAbs were studied to assess ongoing adaptation of the HIV-1 species to the humoral immunity of the human population. Resistance to neutralization is increasing over time, but concerns only the external glycoprotein gp120, not the MPER, suggesting a high selective pressure on gp120. Almost all the identified major neutralization epitopes of gp120 are affected by this antigenic drift, suggesting that gp120 as a whole has progressively evolved in less than 3 decades. Bouvin-Pley2014 (neutralization)
• JM4: Mice twice-primed with DNA plasmids encoding HIV-1 gp120 and gag and given a double boost with HIV-1 virus-like particles (VLPs) i.e. DDVV immunization, elicited Env-specific antibody responses as well as Env- and Gag-specific CTL responses. In vivo electroporation (EP) was used to increase breadth and potency of response. Llama single domanin anti-gp120 (CD4+coreceptor) JM4 was used to prove that the VLP spike included the broad neutralization epitope recognized by it. Huang2017a (therapeutic vaccine, variant cross-reactivity)
• JM4: This study examined the neutralization of group N, O, and P primary isolates of HIV-1 by diverse antibodies. Cross-group neutralization was observed only with the bNAbs targeting the N160 glycan-V1/V2 site. Four group O isolates, 1 group N isolate, and the group P isolates were neutralized by PG9 and/or PG16 or PGT145 at low concentrations. None of the non-M primary isolates were neutralized by bNAbs targeting other regions, except 10E8, which weakly neutralized 2 group N isolates, and 35O22 which neutralized 1 group O isolate. Bispecific bNAbs (PG9-iMab and PG16-iMab) very efficiently neutralized all non-M isolates with IC₅₀ below 1 ug/mL, except for 2 group O strains. bNAb JM4SdAb was able to neutralize 1/16 tested non-M primary isolates at an IC₅₀< 10µg/ml, RBF208,M/O at 2.31 µg/ml. Morgand2015 (neutralization, subtype comparisons)
• JM4: A panel of single-domain Abs (sdAbs) that bind either to the CD4BS or CoRBS were selected using trimeric gp140 as immunogen and phage display protocol in llamas. These sdAbs efficiently neutralize a broad panel of envelops from subtypes A, C, G, CRF01_AE, CRF02_AG including Tier3 viruses. JM4 exhibited binding to free or miniCD4-crosslinked gp120 and gp140; neutralized 7 of the 11 tier 1B, 2 and 3 viruses tested and outperform bnAbs such as 2G12, b12, 2F5, 4E10 and PG9. Matz2013 (antibody generation, vaccine antigen design, broad neutralizer, recombinant antibodies)
• JM4: X-ray crystallography, surface plasmon resonance and pseudovirus neutralization were used to characterize a heavy chain only llama antibody, named JM4. The full-length IgG2b and IgG3 versions of JM4 that target the coreceptor-binding site and potently neutralize over 95% of circulating HIV-1 isolates. The single-domain (VHH) version of JM4 neutralized less well than the full-length IgG2b version of JM4. JM4 targets a hybrid epitope on gp120 that combines elements from both the CD4 binding region and the coreceptor binding surface. JM4 epitope overlaps most extensively with the CD4 binding site of b12 and very little with VRC01, although the sites are in close proximity. JM4 epitope overlaps with the CD4i binding site of 17b, X5, 48d and 412d. JM4 IgG2b was able to potently neutralize the HIV-1 isolates that were resistant to VRC01, PG9 and PGT128. Acharya2013 (antibody binding site, antibody generation, structure, broad neutralizer)

References

Showing 5 of 5 references.

Isolation Paper
Matz2013 Julie Matz, Pascal Kessler, Jérôme Bouchet, Olivier Combes, Oscar Henrique Pereira Ramos, Francis Barin, Daniel Baty, Loïc Martin, Serge Benichou, and Patrick Chames. Straightforward Selection of Broadly Neutralizing Single-Domain Antibodies Targeting the Conserved CD4 and Coreceptor Binding Sites of HIV-1 gp120. J. Virol., 87(2):1137-1149, Jan 2013. PubMed ID: 23152508. Show all entries for this paper.

Acharya2013 Priyamvada Acharya, Timothy S. Luongo, Ivelin S. Georgiev, Julie Matz, Stephen D. Schmidt, Mark K. Louder, Pascal Kessler, Yongping Yang, Krisha McKee, Sijy O'Dell, Lei Chen, Daniel Baty, Patrick Chames, Loic Martin, John R. Mascola, and Peter D. Kwong. Heavy Chain-Only IgG2b Llama Antibody Effects Near-Pan HIV-1 Neutralization by Recognizing a CD4-Induced Epitope That Includes Elements of Coreceptor- and CD4-Binding Sites. J. Virol., 87(18):10173-10181, Sep 2013. PubMed ID: 23843638. Show all entries for this paper.

Bouvin-Pley2014 M. Bouvin-Pley, M. Morgand, L. Meyer, C. Goujard, A. Moreau, H. Mouquet, M. Nussenzweig, C. Pace, D. Ho, P. J. Bjorkman, D. Baty, P. Chames, M. Pancera, P. D. Kwong, P. Poignard, F. Barin, and M. Braibant. Drift of the HIV-1 Envelope Glycoprotein gp120 Toward Increased Neutralization Resistance over the Course of the Epidemic: A Comprehensive Study Using the Most Potent and Broadly Neutralizing Monoclonal Antibodies. J. Virol., 88(23):13910-13917, Dec 2014. PubMed ID: 25231299. Show all entries for this paper.

Huang2017a Xun Huang, Qianqian Zhu, Xiaoxing Huang, Lifei Yang, Yufeng Song, Ping Zhu, and Paul Zhou. In Vivo Electroporation in DNA-VLP Prime-Boost Preferentially Enhances HIV-1 Envelope-Specific IgG2a, Neutralizing Antibody and CD8 T Cell Responses. Vaccine, 35(16):2042-2051, 11 Apr 2017. PubMed ID: 28318765. Show all entries for this paper.

Morgand2015 Marion Morgand, Mélanie Bouvin-Pley, Jean-Christophe Plantier, Alain Moreau, Elodie Alessandri, François Simon, Craig S. Pace, Marie Pancera, David D. Ho, Pascal Poignard, Pamela J. Bjorkman, Hugo Mouquet, Michel C. Nussenzweig, Peter D. Kwong, Daniel Baty, Patrick Chames, Martine Braibant, and Francis Barin. A V1V2 Neutralizing Epitope Is Conserved in Divergent Non-M Groups of HIV-1. J. Acquir. Immune Defic. Syndr., 21 Sep 2015. PubMed ID: 26413851. Show all entries for this paper.