HIV-1 Broadly Neutralizing Antibodies: Identification, Development and Vaccine Evaluation

Zhang, Zaibao; Guan, Qian; Yuan, Hongyu

doi:10.4172/2155-6113.1000636

Cited by 5 publications

(4 citation statements)

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“…These bnAbs were raised from blood of HIV-1 infected patients and this information is tabulated in Table 1 . Generally, anti-HIV bnAbs can be categorized into two groups: first and second [ 63 ]. Both of these groups differ from the method used for generation of bnAbs and their functionalities.…”

Section: Development Of Hiv-1-neutralizing Antibodies Against Hiv/mentioning

confidence: 99%

“…Examples of “first-generation” antibodies are b12, 2G12, 4E10, and 2F5. These bnAbs were developed from Epstein-Barr virus- (EBV-) immortalized B cells and generated using phage-display methods [ 63 ]. Although these bnAbs resulted in 50%–88% of neutralization breadth, they are not ideal for antibody-based vaccine mainly due to the relatively low neutralization efficacy and limitation of method such as antibody specificity selection and lack of high throughput screening option [ 64 ].…”

Section: Development Of Hiv-1-neutralizing Antibodies Against Hiv/mentioning

confidence: 99%

“…This therapeutic modality may pose a higher value when used in combination with current anti-HIV therapies such as HAART or other antiviral small-molecule inhibitors. For example, it has been shown that the bnAb 3BNC117 when used in combination with HAART could enhance the host immune response against HIV-1 and leads to significant delay of viral rebound after treatment cessation [ 63 , 104 ]. Although the combination treatment of small-molecule inhibitors and antiviral antibodies has not been studied, it is speculated that it will drastically improve the neutralizing potency of the HIV-1.…”

Section: Future Perspectives and Conclusionmentioning

confidence: 99%

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Antibody-Mediated Therapy against HIV/AIDS: Where Are We Standing Now?

Awi

Teow

2018

Journal of Pathogens

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Acquired immunodeficiency syndrome (AIDS) cases are on the rise globally. To date, there is still no effective measure to eradicate the causative agent, human immunodeficiency virus (HIV). Highly active antiretroviral therapy (HAART) is being used in HIV/AIDS management, but it results in long-term medication and has major drawbacks such as multiple side effects, high cost, and increasing the generation rate of escape mutants. In addition, HAART does not control HIV-related complications, and hence more medications and further management are required. With this, other alternatives are urgently needed. In the past, small-molecule inhibitors have shown potent antiviral effects, and some of them are now being evaluated in clinical trials. The challenges in developing these small molecules for clinical use include the off-target effect, poor stability, and low bioavailability. On the other hand, antibody-mediated therapy has emerged as an important therapeutic modality for anti-HIV therapeutics development. Many antiviral antibodies, namely, broad neutralizing antibodies (bnAbs) against multiple strains of HIV, have shown promising effects in vitro and in animal studies; further studies are ongoing in clinical trials to evaluate their uses in clinical applications. This short review aims to discuss the current development of therapeutic antibodies against HIV and the challenges in adopting them for clinical use.

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Section: Development Of Hiv-1-neutralizing Antibodies Against Hiv/mentioning

confidence: 99%

Section: Development Of Hiv-1-neutralizing Antibodies Against Hiv/mentioning

confidence: 99%

Section: Future Perspectives and Conclusionmentioning

confidence: 99%

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Antibody-Mediated Therapy against HIV/AIDS: Where Are We Standing Now?

Awi

Teow

2018

Journal of Pathogens

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“…On each HIV virion, there are only about 8-14 envelope glycoprotein spikes (Zanetti et al, 2006 andZhu et al, 2006).The HIV-1 envelope glycoprotein composed of the receptor binding domain gp120 and the fusion protein subunit gp41 which catalyzes virus entry and is a major target for therapeutic intervention and for neutralizing antibodies (Buzon et al, 2010).Until recently, mapping and structural definition of the HIV-1 has allowed the identification of five sites of vulnerability to neutralizing antibodies on the HIV-1 trimeric complex. These five sites are (1) CD4 binding site (CD4bs), (2) N-glycan V1/V2 loop, (3) Nglycan V3 loop, (4) gp120/gp41 interface, (5) gp41(662-683) (van Gils and Sanders, 2013; Zhang et al, 2016).…”

Section: Introductionmentioning

confidence: 99%

Enhancement of Immune Response to Vaccines Against Hiv by Self-Boosting

Hussein

2018

Al-Azhar Bulletin of Science

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A major challenge for immunologists has been the development of vaccines able to augment both of humoral and cellular immune responses. One particularly promising approach is the prime-boost strategy, which has been shown to generate high levels of T-cell memory in animal models. In the present study, loaded liposomes were used to determine how does prime-boost strategy would be beneficial for generation of humoral and cellular responses. BALB/c mice were immunized with HIV-1 gp41 (662-683) liposomes and 30 days later they received the booster doseof the same immunogen. HIV-1 gp41 (662-683) specific humoralresponse was evaluated pre-prime, 30days post-prime and 30 days post-boost by ELISA. HIV-1 gp41 (662-683) specific antibodies sharply jumped after boosting by ~40 foldcompared to that generated by priming. Similarly, self-boosting generated considerably HIV-1 gp41 (662-683) specific antigen secreting plasma cells in bone marrow. Overall, the results suggest that self-boosting is very important for generation of specific humoral response for HIV-1 gp41 . This prime-boost strategy shows a promise to induce both of specific-antibodies and specific antibody secreting cells in bone marrowfor weak immunogens like HIV-1 gp41 . Bershteyn, A.; Hanson, M.C.; Crespo, M.P.; Moon, J.J.; Li, A.V.; Suh, H. andIrvine, D.J.(2012): Robust IgG responses to nanograms of antigen using a biomimetic lipid-coated particle vaccine. J. Control Release, 157(3): 354-365. Buzon, V.; Natrajan, G.; Schibli, D.; Campelo, F.; Kozlov, M.M. and Weissenhorn, W. (2010): Crystal structure of HIV-1 gp41 including both fusion peptide and membrane proximal external regions. PLoSPathog., 6(5): e1000880. Cardoso, R.M.; Zwick, M.B.; Stanfield, R.L.; Kunert, R; Binley, J.M.; Katinger, H.; Burton, D.R. and Wilson, I.A. (2005): Broadly neutralizing anti-HIV antibody 4E10 recognizes a helical conformation of a highly conserved fusion-associated motif in gp41. Immunity, 22(2): 163-173. CDC "Centers for disease control and prevention" (1981): Pneumocystis pneumonia--Los Angeles. Morb.Mortal. Wkly. Rep., 30: 250-252. Coffin, J.; Haase, A.; Levy, J.A.; Montagnier, L.; Oroszlan, S.; Teich, N.; Temin, H.; Toyoshima, K.; Varmus, H.; Vogt, P. and Weiss, R. (1986): What to call the AIDS virus?. Nature, 321(6065): 10. Denner, J. (2011): Towards an AIDS vaccine: the transmembrane envelope protein as target for broadly neutralizing antibodies. Hum. Vaccin., 7(suppl.): 4-9. Donius, L.R.; Cheng, Y.; Choi, J.; Sun, Z. Y.; Hanson, M.; Zhang, M.; Gierahn, T. M.; Marquez, S.; Uduman, M.; Kleinstein, S.H.; Irvine, D.; Love, J. C.; Reinherz, E. L.; and Kim, M. (2016):

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