Protection of chickens against infectious bronchitis by a recombinant fowlpox virus co-expressing IBV-S1 and chicken IFNγ

Wang, Yun Feng; Sun, Yong Ke; Tian, Zhan Cheng; Shi, Xing Ming; Tong, Guang Zhi; Liu, Sheng Wang; Zhi, Hai Dong; Kong, Xian Gang; Wang, Mei

doi:10.1016/j.vaccine.2009.09.065

Cited by 30 publications

(23 citation statements)

References 24 publications

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“…Fowlpox viruses that express the IBV S1 gene have been reported previously [30-32], and all of these vaccines have been described to confer protection against viral challenge with homotypic IBV strains and some heterotypic IBV strains in SPF chickens. However, the protective efficacy that is conferred by recombinant fowlpox viruses could be diminished in commercial chickens due to the presence of maternal antibodies against fowlpox virus [33,34].…”

Section: Discussionmentioning

confidence: 99%

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Protection conferred by a recombinant Marek’s disease virus that expresses the spike protein from infectious bronchitis virus in specific pathogen-free chicken

Zhang

YeZhen

et al. 2012

Virol J

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BackgroundIn many countries, the predominant field isolates of infectious bronchitis virus (IBV) have been classified as QX-like strains since 1996. However, no commercial vaccines that are specific for this type of IBV are currently available. Therefore, there is an urgent need to develop novel vaccines that prevent QX-like IBV infection.ResultsA recombinant Marek’s disease virus (MDV), rMDV-S1, that expresses the S1 subunit of the spike (S) protein from the QX-like infectious bronchitis virus (IBV) was constructed by inserting the IBV S1 gene into the genome of the CVI988/Rispens strain of MDV. Specific pathogen-free (SPF) chickens that were vaccinated with rMDV-S1 were protected when challenged with the QX-like IBV. They were observed to have mild clinical signs of disease, a short virus-shedding period and low mortality. Additionally, the rMDV-S1 conferred full protection to chickens against virulent MDV, as did the CVI988/Rispens strain.ConclusionsOur results demonstrate that rMDV-S1 is an effective and promising recombinant vaccine for the prevention of QX-like IBV infection.

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Section: Discussionmentioning

confidence: 99%

“…After 96 hours, the allantoic fluid was collected, and any pathological changes in the embryos were recorded. The samples were considered positive for IBV isolation if the embryos appeared to be congestive, dropsical or hemorrhagic or if they developed urate deposition [32]. Otherwise, the embryos were inoculated for three blind passages.…”

Section: Methodsmentioning

confidence: 99%

Protection conferred by a recombinant Marek’s disease virus that expresses the spike protein from infectious bronchitis virus in specific pathogen-free chicken

Zhang

YeZhen

et al. 2012

Virol J

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“…It consists of the N-terminal S1 and C-terminal S2 subunits, which are generated during post-translational cleavage of S protein (Jackwood et al, 2001). The S1 subunit is the main protein to induce the protective antibodies, virus-neutralization antibodies, hemagglutination inhibition antibodies, cross-reactivity ELISA antibodies and cell-mediated immune response (Cavanagh et al, 1997;Wang et al, 2009;Zhang et al, 2014). The S1 protein is involved in cell attachment and carries virus-neutralizing and serotype-specific http://dx.doi.org/10.1016/j.vetimm.2015.08.008 0165-2427/© 2015 Elsevier B.V. All rights reserved.…”

Section: Introductionmentioning

confidence: 99%

Two novel neutralizing antigenic epitopes of the s1 subunit protein of a QX-like avian infectious bronchitis virus strain Sczy3 as revealed using a phage display peptide library

Zou

Xia

Wang

et al. 2015

Veterinary Immunology and Immunopathology

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The spike (S) protein of the infectious bronchitis virus (IBV) plays a central role in the pathogenicity, the immune antibody production, serotype and the tissue tropism. In this study, we generate 11 monoclonal antibodies (mAbs) against S1 subunit of IBV Sczy3 strain, and two mAbs 1D5 and 6A12 were positive in indirect ELISA against both His-S1 protein and the purified whole viral antigen. MAb 6A12 and 1D5 could recognized by other 10 IBV strains (IBVs) from five different genotypes, except that 1D5 had a relatively low reaction with two of the 10 tested IBVs. End-point neutralizing assay performed in chicken embro kidney (CEK) cells revealed that the neutralization titer of 6A12 and 1D5 against Sczy3 reached 1:44.7 and 1:40.6, respectively. After screening a phage display peptide library and peptide scanning, we identified two linear B-cell epitopes that were recognized by the mAbs 1D5 and 6A12, which corresponded to the amino acid sequences (87)PPQGMAW(93) and (412)IQTRTEP(418), respectively, in the IBV S1 subunit. Sequences comparison revealed that epitope (412)IQTRTEP(418) was conserved among IBVs, while the epitope (87)PPQGMAW(93) was relatively variable among IBVs. The novel mAbs and the epitopes identified will be useful for developing diagnostic assays for IBV infections.

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“…Microscopic, proteomic, and ultrastructural evidence indicates that these proteins are secreted and exposed on the surface of the bacterium and extracellularly associated with the morula matrix and membrane (Popov et al, 2000; Doyle et al, 2006; Luo et al, 2008; Wakeel et al, 2009, 2010a; Zhu et al, 2009). Several functions have been associated with TRPs in pathogenic bacteria, including immune evasion, adhesion, actin nucleation, and other host–pathogen interactions (Gaillard et al, 1991; Wren, 1991; Kling et al, 1997; Jordan et al, 2003; Clifton et al, 2005; Palmer and Brayton, 2007; Shak et al, 2009; Wang et al, 2009). Recent studies have demonstrated that E. chaffeensis TRP47 interacts with a network of host cell proteins involved in signaling, modulation of gene expression, and intracellular vesicle trafficking (Wakeel et al, 2009) and is tyrosine phosphorylated (Wakeel et al, 2010a).…”

Section: Introductionmentioning

confidence: 99%

Ehrlichia chaffeensis Tandem Repeat Proteins and Ank200 are Type 1 Secretion System Substrates Related to the Repeats-in-Toxin Exoprotein Family

Wakeel¹,

Dulk‐Ras²,

Hooykaas³

et al. 2011

Front. Cell. Inf. Microbio.

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Ehrlichia chaffeensis has type 1 and 4 secretion systems (T1SS and T4SS), but the substrates have not been identified. Potential substrates include secreted tandem repeat protein (TRP) 47, TRP120, and TRP32, and the ankyrin repeat protein, Ank200, that are involved in molecular host–pathogen interactions including DNA binding and a network of protein–protein interactions with host targets associated with signaling, transcriptional regulation, vesicle trafficking, and apoptosis. In this study we report that E. chaffeensis TRP47, TRP32, TRP120, and Ank200 were not secreted in the Agrobacterium tumefaciens Cre recombinase reporter assay routinely used to identify T4SS substrates. In contrast, all TRPs and the Ank200 proteins were secreted by the Escherichia coli complemented with the hemolysin secretion system (T1SS), and secretion was reduced in a T1SS mutant (ΔTolC), demonstrating that these proteins are T1SS substrates. Moreover, T1SS secretion signals were identified in the C-terminal domains of the TRPs and Ank200, and a detailed bioinformatic analysis of E. chaffeensis TRPs and Ank200 revealed features consistent with those described in the repeats-in-toxins (RTX) family of exoproteins, including glycine- and aspartate-rich tandem repeats, homology with ATP-transporters, a non-cleavable C-terminal T1SS signal, acidic pIs, and functions consistent with other T1SS substrates. Using a heterologous E. coli T1SS, this investigation has identified the first Ehrlichia T1SS substrates supporting the conclusion that the T1SS and corresponding substrates are involved in molecular host–pathogen interactions that contribute to Ehrlichia pathobiology. Further investigation of the relationship between Ehrlichia TRPs, Ank200, and the RTX exoprotein family may lead to a greater understanding of the importance of T1SS substrates and specific functions of T1SS in the pathobiology of obligately intracellular bacteria.

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Protection of chickens against infectious bronchitis by a recombinant fowlpox virus co-expressing IBV-S1 and chicken IFNγ

Cited by 30 publications

References 24 publications

Protection conferred by a recombinant Marek’s disease virus that expresses the spike protein from infectious bronchitis virus in specific pathogen-free chicken

Protection conferred by a recombinant Marek’s disease virus that expresses the spike protein from infectious bronchitis virus in specific pathogen-free chicken

Two novel neutralizing antigenic epitopes of the s1 subunit protein of a QX-like avian infectious bronchitis virus strain Sczy3 as revealed using a phage display peptide library

Ehrlichia chaffeensis Tandem Repeat Proteins and Ank200 are Type 1 Secretion System Substrates Related to the Repeats-in-Toxin Exoprotein Family

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