Variant-specific monoclonal and group-specific polyclonal human immunodeficiency virus type 1 neutralizing antibodies raised with synthetic peptides from the gp120 third variable domain

Laman, Jon D.; Schellekens, M.M.; Abacıoğlu, Yusuf Hakan; Lewis, George K.; Tersmette, M.; Fouchier, Ron A. M.; Langedijk, Johannes P. M.; Claassen, Eric; Boersma, W.J.A.

doi:10.1128/jvi.66.3.1823-1831.1992

Cited by 64 publications

(2 citation statements)

References 48 publications

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“…1C , left and middle). The EboGPΔM-V3 and EboGPΔM-V3-V5 chimeric proteins were recognized by specific anti-gp120 V3-neutralizing antibodies (W0-07 and 5F7) ( 36 ) ( Fig. 1C , right).…”

Section: Resultsmentioning

confidence: 99%

Development and Evaluation of an Ebola Virus Glycoprotein Mucin-Like Domain Replacement System as a New Dendritic Cell-Targeting Vaccine Approach against HIV-1

Wang

Azizi

et al. 2021

J Virol

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The development of efficient vaccine approaches against HIV infection remains challenging in the vaccine field. We herein developed an Ebola virus envelope glycoprotein (EboGP)-based chimeric fusion protein system and demonstrated that replacement of the mucin-like domain (MLD) of EboGP with HIV C2-V3-C3 (134 aa) or C2-V3-C3-V4-C4-V5-C5 (243 aa) polypeptides (EbGPΔM-V3 and EbGPΔM-V3-V5, respectively) still maintained the efficiency of EboGP-mediated viral entry into human macrophages and dendritic cells (DCs). Animal studies using mice revealed that immunization with virus-like particles (VLPs) containing the above chimeric proteins, especially EbGPΔM-V3, induced significantly more potent anti-HIV antibodies than HIV gp120 alone in mouse serum and vaginal fluid. Moreover, the splenocytes isolated from mice that immunized with VLPs containing EbGPΔM-V3 produced significantly higher levels of IFN-γ, IL-2, IL-4, IL-5 and MIP-1α. Additionally, we demonstrated that co-expression of EbGPΔM-V3 and the HIV Env glycoprotein in a recombinant vesicular stomatitis virus (rVSV) vector elicited robust anti-HIV antibodies that may have specifically recognized outside or inside the C2-V3-C3 region of HIV-1 gp120 and cross-reacted with the gp120 from different HIV strains. Thus, this study has demonstrated the great potential of this DC-targeting vaccine platform as a new vaccine approach for improving immunogen delivery and increasing vaccine efficacy. Importance Currently, there are more than 38.5 million reported cases of HIV globally. To date, there is no approved vaccine for HIV-1 infection. Thus, the development of an effective vaccine against HIV infection remains a global priority. This study revealed the efficacy of a novel Dendritic Cells (DC)-targeted vaccination approach against HIV-1. The results have clearly shown that the immunization of mice with virus-like particles (VLPs) and VSVs containing HIV Env and a fusion protein comprised of a DC-targeting domain of Ebola GP with HIV C2-V3-C3 polypeptides (EbGPΔM-V3) could induce robust immune responses against HIV-1 Env and/or Gag in sera and vaginal mucosa. These findings have provided a proof of concept of this novel and efficient DC-targeting vaccine approach in delivering various antigenic polypeptides of HIV-1 and/or other emergent infections to the host antigen-presenting cells to prevent HIV and other viral infections.

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“…1C , left and middle). The EboGPΔM-V3 and EboGPΔM-V3-V5 chimeric proteins were recognized by specific anti-gp120 V3-neutralizing antibodies (W0-07 and 5F7) ( 36 ) ( Fig. 1C , right).…”

Section: Resultsmentioning

confidence: 99%

Development and Evaluation of an Ebola Virus Glycoprotein Mucin-Like Domain Replacement System as a New Dendritic Cell-Targeting Vaccine Approach against HIV-1

Wang

Azizi

et al. 2021

J Virol

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“…with a myeloma cell line Sp2r0 followed by selection and limiting dilution as previously described in detail Ž . Laman et al, 1992 . ELISA to detect antibody levels in immunized mice, to select hybridomas, as well as for determining Mab subclass was performed as described Ž .…”

Section: Generation and Characterization Of Mabmentioning

confidence: 99%

Novel monoclonal antibodies against proteolipid protein peptide 139–151 demonstrate demyelination and myelin uptake by macrophages in MS and marmoset EAE lesions

Laman

Visser

Maassen

et al. 2001

Journal of Neuroimmunology

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Phage display of intact domains at high copy number: A system based on SOC, the small outer capsid protein of bacteriophage T4

et al. 1996

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Peptides fused to the coat proteins of filamentous phages have found widespread applications in antigen display, the construction of antibody libraries, and biopanning. However, such systems are limited in terms of the size and number of the peptides that may be incorporated without compromising the fusion proteins' capacity to self-assemble. We describe here a system in which the molecules to be displayed are bound to pre-assembled polymers. The polymers are T4 capsids and polyheads (tubular capsid variants) and the display molecules are derivatives of the dispensable capsid protein SOC. In one implementation, SOC and its fusion derivatives are expressed at high levels in Escherichia coli, purified in high yield, and then bound in vitro to separately isolated polyheads. In the other, a positive selection vector forces integration of the modified soc gene into a soc-deleted T4 genome, leading to in vivo binding of the display protein to progeny virions. The system is demonstrated as applied to C-terminal fusions to SOC of (1) a tetrapeptide; (2) the 43-residue V3 loop domain of gp120, the human immunodeficiency virus type-I (HIV-I) envelope glycoprotein; and (3) poliovirus VPl capsid protein (312 residues). SOC-V3 displaying phage were highly antigenic in mice and produced antibodies reactive with native gp120. That the fusion protein binds correctly to the surface lattice was attested in averaged electron micrographs of polyheads. The SOC display system is capable of presenting up to -I O 3 copies per capsid and >IO4 copies per polyhead of V3-sized domains. Phage displaying SOC-VPI were isolated from a 1:106 mixture by two cycles of a simple biopanning procedure, indicating that proteins of at least 35 kDa may be accommodated.Keywords: bacteriophage T4; capsid assembly; human immunodeficiency virus antigens; phage display; protein engineering Filamentous phage-based display systems (Smith, 1985) have found widespread use in molecular biology, including many immunologic applications such as antigen presentation and the immunoisolation of desired recombinants (biopanning) (Marks et al., 1992;Smith et al ., 1993;Williamson et al., 1993). However, with filamentous phages, peptides that may be displayed from the major coat protein are limited in size to 6-10 amino acid residues (Kishchenko et al., 1994;Iannolo et al., 1995), although somewhat

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Variant-specific monoclonal and group-specific polyclonal human immunodeficiency virus type 1 neutralizing antibodies raised with synthetic peptides from the gp120 third variable domain

Cited by 64 publications

References 48 publications

Development and Evaluation of an Ebola Virus Glycoprotein Mucin-Like Domain Replacement System as a New Dendritic Cell-Targeting Vaccine Approach against HIV-1

Development and Evaluation of an Ebola Virus Glycoprotein Mucin-Like Domain Replacement System as a New Dendritic Cell-Targeting Vaccine Approach against HIV-1

Novel monoclonal antibodies against proteolipid protein peptide 139–151 demonstrate demyelination and myelin uptake by macrophages in MS and marmoset EAE lesions

Phage display of intact domains at high copy number: A system based on SOC, the small outer capsid protein of bacteriophage T4

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