Characterization of Two Neutralizing Antibodies against Rift Valley Fever Virus Gn Protein

Meng, Hao; Zhang, Guanying; Zhang, Shengnan; Chen, Zhengshan; Chi, Xiangyang; Ya, Dong; Fan, Pengfei; Liu, Yujiao; Chen, Yi; Song, Xiaohong; Liu, Shilin; Yu, Changming; Li, Jianmin; Xia, Xianzhu

doi:10.3390/v12030259

Cited by 12 publications

(11 citation statements)

References 35 publications

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“…We here fused the SpyCatcher domain to the N -terminus of Gn head , whereas fusion to the C -terminus of Gn head may have resulted in a more optimal presentation of the Gn subunit. Domain A (I) and domain B (III) were considered the dominant targets of neutralizing antibodies in a virion context [ 30 , 32 , 47 ]. Whether the individual subdomains A (I) and B (III) are potent immunogens capable of inducing protective immunity awaits further study.…”

Section: Discussionmentioning

confidence: 99%

Vaccine Efficacy of Self-Assembled Multimeric Protein Scaffold Particles Displaying the Glycoprotein Gn Head Domain of Rift Valley Fever Virus

et al. 2021

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Compared to free antigens, antigens immobilized on scaffolds, such as nanoparticles, generally show improved immunogenicity. Conventionally, antigens are conjugated to scaffolds through genetic fusion or chemical conjugation, which may result in impaired assembly or heterogeneous binding and orientation of the antigens. By combining two emerging technologies—i.e., self-assembling multimeric protein scaffold particles (MPSPs) and bacterial superglue—these shortcomings can be overcome and antigens can be bound on particles in their native conformation. In the present work, we assessed whether this technology could improve the immunogenicity of a candidate subunit vaccine against the zoonotic Rift Valley fever virus (RVFV). For this, the head domain of glycoprotein Gn, a known target of neutralizing antibodies, was coupled on various MPSPs to further assess immunogenicity and efficacy in vivo. The results showed that the Gn head domain, when bound to the lumazine synthase-based MPSP, reduced mortality in a lethal mouse model and protected lambs, the most susceptible RVFV target animals, from viremia and clinical signs after immunization. Furthermore, the same subunit coupled to two other MPSPs (Geobacillus stearothermophilus E2 or a modified KDPG Aldolase) provided full protection in lambs as well.

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Section: Discussionmentioning

confidence: 99%

Vaccine Efficacy of Self-Assembled Multimeric Protein Scaffold Particles Displaying the Glycoprotein Gn Head Domain of Rift Valley Fever Virus

et al. 2021

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“…Interestingly, antibodies exhibit much higher neutralizing activities in vitro and in vivo when they target G N rather than G C [ 88 , 89 , 90 ]. It has been proposed that anti-G N neutralizing antibodies block the fusogenic rearrangement of the G N -G C array by targeting the G N distal domain [ 91 , 92 ].…”

Section: Fusion and Penetration Of Phenuiviruses Into The Cytosolmentioning

confidence: 99%

Entry of Phenuiviruses into Mammalian Host Cells

Koch

Xin

Tischler

et al. 2021

Viruses

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Phenuiviridae is a large family of arthropod-borne viruses with over 100 species worldwide. Several cause severe diseases in both humans and livestock. Global warming and the apparent geographical expansion of arthropod vectors are good reasons to seriously consider these viruses potential agents of emerging diseases. With an increasing frequency and number of epidemics, some phenuiviruses represent a global threat to public and veterinary health. This review focuses on the early stage of phenuivirus infection in mammalian host cells. We address current knowledge on each step of the cell entry process, from virus binding to penetration into the cytosol. Virus receptors, endocytosis, and fusion mechanisms are discussed in light of the most recent progress on the entry of banda-, phlebo-, and uukuviruses, which together constitute the three prominent genera in the Phenuiviridae family.

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“…Previous studies have investigated the importance of neutralizing MAbs in protection from lethal RVFV disease. Neutralizing MAbs raised against Gn or Gc protect by various mechanisms of virus neutralization, including the blocking of attachment, entry, or fusion ( 19 – 21 , 23 ). When each MAb described in this study was mapped to its Gn binding domain, all except MAb-2 were found to bind linear epitopes.…”

Section: Discussionmentioning

confidence: 99%

“…Rabbit, human, monkey, and mouse MAbs directed against the two RVFV glycoproteins—Gn and Gc—have been recently developed and demonstrated protective efficacy in mice ( 19 – 23 ). Gn- and Gc-neutralizing MAbs have demonstrated protection in vivo by blocking attachment, entry, or fusion of RVFV ( 19 – 21 , 23 ).…”

Section: Introductionmentioning

confidence: 99%

Isotype-Specific Fc Effector Functions Enhance Antibody-Mediated Rift Valley Fever Virus Protection In Vivo

Cartwright

Barbeau

McElroy

2021

mSphere

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Characterization of Two Neutralizing Antibodies against Rift Valley Fever Virus Gn Protein

Cited by 12 publications

References 35 publications

Vaccine Efficacy of Self-Assembled Multimeric Protein Scaffold Particles Displaying the Glycoprotein Gn Head Domain of Rift Valley Fever Virus

Vaccine Efficacy of Self-Assembled Multimeric Protein Scaffold Particles Displaying the Glycoprotein Gn Head Domain of Rift Valley Fever Virus

Entry of Phenuiviruses into Mammalian Host Cells

Isotype-Specific Fc Effector Functions Enhance Antibody-Mediated Rift Valley Fever Virus Protection In Vivo

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