Identification of amino acids involved in a serotype and neutralization specific epitope with in the s1 subunit of avian infectious bronchitis virus

Moore, Kristi M.; Jackwood, Mark W.; Hilt, Deborah A.

doi:10.1007/s007050050239

Cited by 118 publications

(115 citation statements)

References 19 publications

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“…The results confirmed that S1 protein and N protein play a major role in humoral and cellular immune responses, respectively, which were in accord with the previous investigations [23,26,36]. The immune efficacy of subunit vaccine rHBM-S1-N was better than that of subunit vaccines rHBM-S1 or rHBM-S1-N in humoral and cellular immune responses.…”

Section: Discussionsupporting

confidence: 81%

“…The S glycoprotein is post-translationally cleaved into S1 and S2 subunits [21]. S1 protein determines the antigenicity and immunogenicity of the virus and plays an important role in the induction of specific neutralizing antibody and hemagglutination inhibition antibody, tissue affinity and cell adsorption, which can induce the body to produce humoral immune response [22][23][24]. N protein plays an extremely important role in the replication and assembly of IBV with its good immunogenicity, which can induce the body to produce cellular immune response [25][26][27].…”

Section: Introductionmentioning

confidence: 99%

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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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Section: Discussionsupporting

confidence: 81%

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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“…The arginine residue encoded by this codon in the ArkDPI field isolate and the predominant vaccine populations may be associated with a neutralizing epitope. Moore et al (1997) found that 13 of 14 neutralizing antibodyresistant mutants of ArkDPI had a change in codon 386. However, most of the resistant mutants also had a mutation in codon 304, and all of the resistant mutants with a histidine codon at position 386 (like minor subpopulations of vaccine A) also had a change in codon 304 not found in vaccine A.…”

Section: Discussionmentioning

confidence: 99%

Rapid selection in chickens of subpopulations within ArkDPI-derived infectious bronchitis virus vaccines

Santen

Toro

2008

Avian Pathology

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We examined spike (S) gene sequences of the virus populations of four different commercial ArkDPI-derived infectious bronchitis coronavirus vaccines before and during a single passage in specific pathogen free chickens. We found different degrees of genetic heterogeneity among the four vaccines before passage in chickens, ranging from no apparent heterogeneity to heterogeneity in 20 positions in the S gene. In all except one position, nucleotide differences were non-synonymous. The majority of amino acid differences were in the S1 subunit of the protein. For three of the four ArkDPI-derived vaccines, a single subpopulation with an S gene sequence distinct from the vaccine majority consensus at 5 to 11 codons was selected in chickens within 3 days after ocular vaccination. In contrast, we obtained no evidence for selection of specific subpopulations of the fourth ArkDPI-derived vaccine or Massachusetts or DE072 serotype vaccines. The virus subpopulations within each vaccine selected by chickens are similar in their S1 gene sequences, but distinct in the 3? portion of the S2 subunit gene for each of the three vaccines. In the S1 gene, the selected subpopulations are more similar to the virulent parental ArkDPI isolate than to the predominant vaccine population. The different proportions of distinct subpopulations in Ark vaccines apparently more fit for replication in the respiratory tract of chickens might cause different degrees of damage to respiratory epithelium and/or immune responses in vaccinated chickens. Sequence comparisons provided no evidence to support that ArkDPI-like field isolates were derived directly from host-selected vaccine virus subpopulations.

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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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Identification of amino acids involved in a serotype and neutralization specific epitope with in the s1 subunit of avian infectious bronchitis virus

Cited by 118 publications

References 19 publications

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

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

Rapid selection in chickens of subpopulations within ArkDPI-derived infectious bronchitis virus vaccines

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

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