Induction of protective immunity in chickens vaccinated with infectious bronchitis virus S1 glycoprotein expressed by a recombinant baculovirus.

Song, Chang Seon; Lee, Youn Jeong; Lee, Chang Won; Sung, Hwan Woo; Kim, Jae Hong; Mo, In-Pil; Izumiya, Yoshihiro; Jang, Hyung Kwan; Mikami, Takeshi

doi:10.1099/0022-1317-79-4-719

Cited by 65 publications

(73 citation statements)

References 23 publications

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“…Other studies, using purified, inactivated IBV, have been successful in getting a degree of protection against respiratory tract protection, though usually at a rate of < 59% [12,51,93]; reviewed in more detail by [20]. Rather better protection with inactivated IBV has been achieved against losses in egg production [69].…”

Section: Inactivated Virus and Subunit Vaccinesmentioning

confidence: 99%

“…Induction of immunity by the S1 spike subunit has been studied with S1 prepared from purified virus [12,51] and expression using baculovirus [93]. Although protective immune responses were induced, multiple inoculations of subviral material were required and the percentage of protected chickens was too low (< 50%) for commercial application.…”

Section: Inactivated Virus and Subunit Vaccinesmentioning

confidence: 99%

“…This leaves us far short of understanding the molecular basis of cross-protection -or lack of itas cellular immune responses play a role in protection, and these are poorly understood. We do know that the S protein alone is sufficient to induce good protective immunity [12,20,46,51,53,93,96]. There is increasing evidence that only a few amino acid differences amongst S proteins are sufficient to have a detrimental impact on cross-protection.…”

Section: Introductionmentioning

confidence: 99%

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Coronavirus avian infectious bronchitis virus

2007

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-Infectious bronchitis virus (IBV), the coronavirus of the chicken (Gallus gallus), is one of the foremost causes of economic loss within the poultry industry, affecting the performance of both meat-type and egg-laying birds. The virus replicates not only in the epithelium of upper and lower respiratory tract tissues, but also in many tissues along the alimentary tract and elsewhere e.g. kidney, oviduct and testes. It can be detected in both respiratory and faecal material. There is increasing evidence that IBV can infect species of bird other than the chicken. Interestingly breeds of chicken vary with respect to the severity of infection with IBV, which may be related to the immune response. Probably the major reason for the high profile of IBV is the existence of a very large number of serotypes. Both live and inactivated IB vaccines are used extensively, the latter requiring priming by the former. Their effectiveness is diminished by poor cross-protection. The nature of the protective immune response to IBV is poorly understood. What is known is that the surface spike protein, indeed the amino-terminal S1 half, is sufficient to induce good protective immunity. There is increasing evidence that only a few amino acid differences amongst S proteins are sufficient to have a detrimental impact on cross-protection. Experimental vector IB vaccines and genetically manipulated IBVs -with heterologous spike protein genes -have produced promising results, including in the context of in ovo vaccination.

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Section: Inactivated Virus and Subunit Vaccinesmentioning

confidence: 99%

Section: Inactivated Virus and Subunit Vaccinesmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Coronavirus avian infectious bronchitis virus

2007

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“…The S1 and S2 domain of SARS-CoV S protein can be identified by sequence alignment with other coronavirus S proteins, especially with the more conserved S2 domain (8-10). The S protein is also the major antigenic determinant for coronaviruses (9,(11)(12)(13)(14). It has recently been demonstrated that the binding of the S1 domain to its receptor angiotensinconverting enzyme 2 (ACE2) on host cells is responsible for SARS-CoV entry into cells (15).…”

mentioning

confidence: 99%

Potent neutralization of severe acute respiratory syndrome (SARS) coronavirus by a human mAb to S1 protein that blocks receptor association

Sui

Murakami

et al. 2004

Proc. Natl. Acad. Sci. U.S.A.

567

603

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Effective prophylaxis and antiviral therapies are urgently needed in the event of reemergence of the highly contagious and often fatal severe acute respiratory syndrome (SARS) coronavirus (SARSCoV) infection. We have identified eight recombinant human single-chain variable region fragments (scFvs) against the S1 domain of spike (S) protein of the SARS-CoV from two nonimmune human antibody libraries. One scFv 80R efficiently neutralized SARS-CoV and inhibited syncytia formation between cells expressing the S protein and those expressing the SARS-CoV receptor angiotensin-converting enzyme 2 (ACE2). Mapping of the 80R epitope showed it is located within the N-terminal 261-672 amino acids of S protein and is not glycosylation-dependent. 80R scFv competed with soluble ACE2 for association with the S1 domain and bound S1 with high affinity (equilibrium dissociation constant, K d ‫؍‬ 32.3 nM). A human IgG1 form of 80R bound S1 with a 20-fold higher affinity of 1.59 nM comparable to that of ACE2 (K d ‫؍‬ 1.70 nM), and neutralized virus 20-fold more efficiently than the 80R scFv. These data suggest that the 80R human monoclonal antibody may be a useful viral entry inhibitor for the emergency prophylaxis and treatment of SARS, and that the ACE2-binding site of S1 could be an attractive target for subunit vaccine and drug development.T he severe acute respiratory syndrome (SARS)-associated coronavirus (SARS-CoV), a newly emergent member in the family Coronaviridae, causes SARS for which there are no vaccines or effective therapies currently available (1-4). It has been reported that high titers of protecting IgG antibody to SARS-CoV are present in convalescent serum, and SARS patients show clinical improvement if they are given serum from previously infected patients (5, 6). These observations suggest that passive immunization with human monoclonal antibodies could be developed for the treatment of SARS (7). The spike (S) proteins of coronaviruses are large type-I transmembrane glycoproteins that are responsible for receptor binding and membrane fusion. Two functional domains at the amino (S1) and carboxy (S2) termini of the S protein are conserved among the coronaviruses. The S1 and S2 domain of SARS-CoV S protein can be identified by sequence alignment with other coronavirus S proteins, especially with the more conserved S2 domain (8-10). The S protein is also the major antigenic determinant for coronaviruses (9,(11)(12)(13)(14). It has recently been demonstrated that the binding of the S1 domain to its receptor angiotensinconverting enzyme 2 (ACE2) on host cells is responsible for SARS-CoV entry into cells (15). Therefore, we targeted the S1 protein for generation of neutralizing human monoclonal antibodies. Here we report the identification, production, and characterization of a neutralizing human monoclonal antibody 80R against SARS-CoV that blocks the binding of S1 to ACE2. Materials and MethodsExpression and Purification of SARS-CoV S1 and Truncated S1. Plasmids encoding SARS-CoV S protein residues 12-672, 12-327, o...

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“…Therefore, the BES is currently used widely for protein expression and vaccine production. There were a few studies on the expressing IBV structure proteins by BES [18,[30][31][32][33], but no previous study has focused on developing of subunit vaccine from baculovirus co-expressing S1 and N proteins of IBV and evaluating the immune response of this type of subunit vaccine. Hence, it is necessary to co-express the S1 and N proteins by BES and develop the subunit vaccine including these two proteins.…”

Section: Introductionmentioning

confidence: 99%

Greater Protection against Virulent Infectious Bronchitis Virus Challenge Conferred by Recombinant Baculovirus Co-expressing S1 and N Proteins

Yuan¹,

Zhang²,

He³

et al. 2018

Preprint

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Avian infectious bronchitis virus (IBV) is the causative agent of infectious bronchitis, which causes considerable economic losses to the poultry industry worldwide. It is imperative to develop safe and efficient candidate vaccines to control IBV infection. In the current study, recombinant baculoviruses co-expressing S1 and N proteins, mono-expressing S1 or N proteins alone of IBV were constructed and prepared into subunit vaccines rHBM-S1-N, rHBM-S1 and rHBM-N. The levels of immune protection of these subunit vaccines were evaluated by inoculating specific pathogen-free (SPF) chickens at 14 days of age, boosting with the same dose 14 days later, and following challenge with a virulent GX-YL5 strain of IBV 14 days post-booster (dpb). The commercial vaccine strain H120 was used as a control. The IBV-specific antibody levels as well as the percentages of CD4+ and CD8+ T lymphocytes were detected within 28 days post-vaccination (dpv). The morbidity, mortality, and re-isolation of virus from the tracheas and kidneys of challenged birds were evaluated at 5 days post-challenge (dpc). The results showed that the IBV-specific antibody levels and the percentages of CD4+ and CD8+ T lymphocyte in rHBM-S1-N group were higher than those of rHBM-S1 and rHBM-N groups, especially the cellular immunity response. At 5 dpc, the mortality, morbidity and virus re-isolation rate of rHBM-S1-N were slightly higher than those of H120 group, but were lower than those of rHBM-S1 group and rHBM-N group. The present study demonstrated that the protection of recombinant baculovirus co-expressing S1 and N proteins was better than that of recombinant baculoviruses mono-expressing S1 or N protein alone. Thus, the recombinant baculovirus co-expressing S1 and N proteins could serve as a potential IBV vaccine and this demonstrates that the bivalent subunit vaccine including the S1 and N proteins might be a strategy for the development of an IBV subunit vaccine.

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Induction of protective immunity in chickens vaccinated with infectious bronchitis virus S1 glycoprotein expressed by a recombinant baculovirus.

Cited by 65 publications

References 23 publications

Coronavirus avian infectious bronchitis virus

Coronavirus avian infectious bronchitis virus

Potent neutralization of severe acute respiratory syndrome (SARS) coronavirus by a human mAb to S1 protein that blocks receptor association

Greater Protection against Virulent Infectious Bronchitis Virus Challenge Conferred by Recombinant Baculovirus Co-expressing S1 and N Proteins

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