Fine mapping and conservation analysis of linear B-cell epitopes of peste des petits ruminants virus hemagglutinin protein

Yu, Ran; Zhu, Rui; Gao, Weixiang; Zhang, Ming; Dong, Shijuan; Chen, Bingqing; Yu, Li; Xie, Changzhan; Jiang, Fengying; Li, Zhen

doi:10.1016/j.vetmic.2017.07.008

Cited by 10 publications

(13 citation statements)

References 40 publications

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“…As such, the low homology in H proteins among the two PPRV strains under study could possibly account for the differences in immunogenicity observed for the two PPRV VLPs. The H protein of PPRV is a 609-residue type II integral membrane glycoprotein (Yu et al, 2017). The two PPRV strains under investigation differ by a total of 43 amino acids distributed among the N-terminal cytoplasmic tail (three mutants), stalk region (three mutants), and C-terminal globular head (37 mutants) containing the receptor binding site and immune epitopes, respectively (Figure 6; Colf et al, 2007;Yu et al, 2017).…”

Section: Discussionmentioning

confidence: 99%

Virus-Like Particles Derived From a Virulent Strain of Pest des Petits Ruminants Virus Elicit a More Vigorous Immune Response in Mice and Small Ruminants Than Those From a Vaccine Strain

Yan

et al. 2020

Front. Microbiol.

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Comparing the Immunogenicity of PPRV VLPs results demonstrated that the VLPs derived from the virulent lineage IV Tibet/30 strain were more immunogenic, inducing a more potent and robust humoral and cell-mediated immune response in vaccinated animals by comparison to the lineage II Nigeria 75/1 vaccine strain VLPs. In addition, VNA titers were significantly higher among animals vaccinated with the Tibet/30 VLPs by comparison to the Nigeria 75/1 VLPs. Taken together, these findings suggest that VLPs derived from the virulent lineage IV Tibet/30 strain are more immunogenic by comparison to those derived from the lineage II Nigeria 75/1 vaccine strain and thus represent a promising vaccine candidate for the control and eradication of PPR.

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Section: Discussionmentioning

confidence: 99%

Virus-Like Particles Derived From a Virulent Strain of Pest des Petits Ruminants Virus Elicit a More Vigorous Immune Response in Mice and Small Ruminants Than Those From a Vaccine Strain

Yan

et al. 2020

Front. Microbiol.

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“…Clearly, the key to achieve this goal is that entire IgG-epitomes of several target viral proteins and all type-specific BCEs in them can be revealed. Now, it is achievable since all linear BCEs present in a protein and type-specific BCEs in them has been able to be delineated using rabbit/murine pAbs using the BSP method specific for BCE mapping [35,36], which has been used in many studies of mapping BCEs on different viral protein using rabbit pAbs and BSPs [30,[48][49][50][51][52]. Our previous study has revealed three IgG-epitomes of E6, E7…”

Section: Discussionmentioning

confidence: 99%

“…Now, with the establishment of BSP methods specific for BCE mapping by BCEs mapped by rabbit pAbs to HPV58-L1 were reacted with murine pAbs to HPV58 L1-VLPs [30]. All 19 and 9/13 RR-BCEs on nucleoprotein (NP) and hemagglutinin (H) proteins of peste des petits ruminants virus (PPRV) were recognized by sera from goat with PPRV-positive, respectively [48,49]. Similarly, there was evidence that 3 of 4 RR-peptides on HPV18-E6 can be recognized by human sera to HPV18 in ELISA test [29].…”

Section: Discussionmentioning

confidence: 99%

Epitome mapping of E6 and E7 proteins from high-risk oncogenic HPV types 16, 18 and 45

Tang

Wang

et al. 2020

Preprint

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Background It is crucial to reveal entire epitomes of more target homologous proteins and specificity of each mapped B cell epitope (BCE) within them for the development of high-risk (hr-) human papillomavirus (HPV) type-specific diagnostic reagents. Methods Recombinant E6 and -E7 oncoproteins from HPV16/18/45 were immunized mice to prepare Rabbit antisera. Overlapping 16mer/8mer-peptides for two rounds of antigenic peptide and fine BCE motif mapping were expressed as GST188 fusion proteins. Fine BCEs were delineated by Western blot and sequence alignment. Results In this work, we decoded six epitomes of E6 and E7 oncoproteins from three HPV types 16, 18 and 45 that are the most common hr-HPVs in cervical cancer patients worldwide, in which total 35 fine BCEs (8, 6 and 4 for E6; 7, 6 and 4 for E7) were mapped using rabbit antisera to respective recombinant proteins. The specificity of each mapped BCE among 20 defined or possible hr-HPVs was delineated by sequence alignment based on BCE minimal motif. According to similarities of immune responses to E6/E7 existed among rabbit and humans, 7 human-recognizing (HR) BCE motifs in HR-peptides of HPV16/18-E6 and E7 proteins were delimitated by comparing with corresponding rabbit-recognizing BCEs. Also, the unique BCE distribution within three delineated E7 epitomes was confirmed, in which almost mapped BCEs were clustered at the first half of the molecules, suggesting that it may be a common characteristic of hr-HPV E7 proteins. Conclusions The results would form the basis for identifying HR-BCEs and developing serodiagnostic reagents used in HPV-based cervical cancer screening and HPV-positive women managing.

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“…For rational vaccine design or development of diagnostic tools, it is necessary to map the specific and conserved BCEs of target proteins [ 21 ]. Also, multi-epitope-based vaccines offer numerous advantages compared to the complete protein, including cost-effective production, stability under different conditions and multivalency [ 24 ]. Recently, Zhao et al [ 33 ] constructed a recombinant epitope vaccine that contains six immunodominant epitopes, and they demonstrated its capacity to induce a robust IgG specific response.…”

Section: Discussionmentioning

confidence: 99%

“…Serum samples of a healthy rabbit and a healthy sheep with no history of CCHFV infection were used as negative controls in the western blotting assay. Escherichia coli BL21 (DE3) competent cells were used to express 16/8mer peptides fused with a truncated GST188 protein (i.e., with the initial 188 aa of GST) [ 24 ]. Goat anti-rabbit and mouse anti-goat IgG conjugated to horseradish peroxidase (HRP) were purchased from Beijing TransGen Biotech, Co., Ltd. (China).…”

Section: Methodsmentioning

confidence: 99%

Mapping of B-cell epitopes on the N- terminal and C-terminal segment of nucleocapsid protein from Crimean-Congo hemorrhagic fever virus

Moming¹,

Tuoken²,

Yue³

et al. 2018

PLoS ONE

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Crimean-Congo hemorrhagic fever virus (CCHFV) is a tick-borne pathogen that causes severe disease in humans. CCHFV is widely distributed in more than 30 countries and distinct regions, which means that it poses a serious threat to human health. The nucleocapsid protein (NP) encoded by the CCHFV S gene is the primary detectable antigen in infected cells, which makes it an important viral antigen and a clinical diagnostic target. In this study, the modified biosynthetic peptide (BSP) method was used to identify the fine epitopes on the N- and C- terminals of NP from the CCHFV YL04057 strain using rabbit antiserum against CCHFV-NP. Nine epitopes were identified: E1a (178NLILNRGG185), E1b (184GGDENP189), E2 (352PLKWGKK358), E3 (363FADDS367), E4 (399NPDDAA404), E5a (447DIVASEHL454), E5b (452EHLLHQSL459), E6 (464SPFQNAY470) and E7 (475NATSANII482). Western blotting analysis showed that each epitope interacted with the positive serum of sheep that had been naturally infected with CCHFV. Amino acid sequence alignment between each epitope and their homologous proteins showed that they were almost 100% conserved among 12 CCHFV sequences from different lineages, except for epitopes E1a, E1b and E2. Three-dimensional structural modeling analysis showed that all identified epitopes were located on the surface of the NP “head” domain. This study identified fine epitopes on the N- and C- terminals of NP, which will increase the understanding of the structure and function of NP, and it could lay the foundation for the design and development of a CCHFV multi-epitope peptide vaccine and detection antigen.

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Fine mapping and conservation analysis of linear B-cell epitopes of peste des petits ruminants virus hemagglutinin protein

Cited by 10 publications

References 40 publications

Virus-Like Particles Derived From a Virulent Strain of Pest des Petits Ruminants Virus Elicit a More Vigorous Immune Response in Mice and Small Ruminants Than Those From a Vaccine Strain

Virus-Like Particles Derived From a Virulent Strain of Pest des Petits Ruminants Virus Elicit a More Vigorous Immune Response in Mice and Small Ruminants Than Those From a Vaccine Strain

Epitome mapping of E6 and E7 proteins from high-risk oncogenic HPV types 16, 18 and 45

Mapping of B-cell epitopes on the N- terminal and C-terminal segment of nucleocapsid protein from Crimean-Congo hemorrhagic fever virus

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