Chimeric VLPs with GII.3 P2 domain in a backbone of GII.4 VP1 confers novel HBGA binding ability

Huo, Yuqi; Wang, Wenhui; Ling, Tong; Wan, Xin; Ding, Li; Shen, Shuo; Huo, Jin-Ling; Zhang, Shanfeng; Wang, Mingchen; Wang, Yumei; Liu, Yubing

doi:10.1016/j.virusres.2016.08.006

Cited by 5 publications

(5 citation statements)

References 26 publications

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“…Indirect enzyme-linked immunosorbent assay (ELISA) showed that mAbs 1F7, 1F11, and 2B6 bound to GII.6-JN and GII.6-AB VP1 proteins but not GII.6-KU VP1 proteins (data not shown). Based on literature, the blocking epitope is primarily located in the P2 domain ( Parra et al., 2012 ; Huo et al., 2016 ). Sequence alignment showed that there were limited amino acid (aa) variations within the P2 domain of the three VP1 proteins.…”

Section: Resultsmentioning

confidence: 99%

Identification of a GII.6 norovirus blockade antibody epitope

Huo

Liu

2023

Virus Research

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Section: Resultsmentioning

confidence: 99%

Identification of a GII.6 norovirus blockade antibody epitope

Huo

Liu

2023

Virus Research

Self Cite

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“…Wells added with VLPs containing without VLPs mouse serum was selected as control. The blocking index was calculated in % as (mean OD without VLP sera-mean OD with VLP sera)/mean OD without VLP sera × 100% [24].…”

Section: Methodsmentioning

confidence: 99%

Immunogenicity and protective potency of Norovirus GII.17 virus-like particle-based vaccine

Chen

Tai

Yuan³

et al. 2018

Preprint

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Noroviruses (NoVs) are a major cause of acute viral gastroenteritis in adults and children worldwide. Lacking of cell culture system and animals models that must be considered the virus like particles (VLPs) used as an effective vaccine development. In the present study, we investigated the expression of the major capsid protein (VP1) of Genogroup II, genotype 17 (GII.17) NoV using recombinant baculovirus system in insect cells and saliva binding blockade assay to detect their protective potency. Our results showed that GII.17 VLPs could be successfully generated in sf9 insect cells and electron microscopic revealed that GII.17 VLPs was visualized as spherical particles of -35nm in diameter. Immunized mouse with purified VLPs produced GII.17 specific sera and could efficiently block GII.17 VLPs binding to saliva histo-blood group antigens (HBGAs). Together, these results suggested that GII.17 VLPs represent a promising vaccine candidate against NoV GII.17 infection and strongly support further preclinical and clinical studies.

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“…Wells added with VLPs that did not contain VLPs in the mice serum were selected as controls. The blocking index was calculated in % as (mean OD without VLP sera-mean OD with VLP sera)/mean OD without VLP sera 9 100% (Huo et al 2016b).…”

Section: Gii17 Vlps-hbgas Binding Blockade Assaymentioning

confidence: 99%

Immunogenicity and protective potency of Norovirus GII.17 virus-like particle-based vaccine

Chen

Tai

Yuan³

et al. 2020

Biotechnol Lett

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Objectives Noroviruses (NoVs) are major cause of acute viral gastroenteritis in worldwide, and the lack of a cell culture system that must be considered the virus like particles (VLPs) are used as an effective vaccine development. Materials and methods In the present study, we investigated the expression of the major capsid protein (VP1) of the Genogroup II, genotype 17 (GII.17) NoV, using recombinant baculovirus system in insect cells, as well as a saliva binding blockade assay to detect their protective potency. Results Our results showed that GII.17 VLPs could be successfully generated in sf9 insect cells, and electron microscopic revealed that GII.17 VLPs appeared as spherical particles with a-35 nm diameter. Immunized mice with purified VLPs produced GII.17 specific sera and could efficiently block GII.17 VLPs binding to the saliva histo-blood group antigens (HBGAs). Conclusions Together, these results suggested that GII.17 VLPs represent a promising vaccine candidate against NoV GII.17 infection and strongly support further preclinical and clinical studies. Keywords Norovirus GII.17 Á Saliva histo-blood group antigens (HBGAs) Á sf9 cells Á Vaccine Á Virus like particles (VLPs) Wei Chen and Tao Kang have equally contribution to the paper.

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Chimeric VLPs with GII.3 P2 domain in a backbone of GII.4 VP1 confers novel HBGA binding ability

Cited by 5 publications

References 26 publications

Identification of a GII.6 norovirus blockade antibody epitope

Identification of a GII.6 norovirus blockade antibody epitope

Immunogenicity and protective potency of Norovirus GII.17 virus-like particle-based vaccine

Immunogenicity and protective potency of Norovirus GII.17 virus-like particle-based vaccine

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