In this task, you're given a paragraph from the research paper and your task is to generate a suitable title for the research paper based on the given paper. Under 100 words is a good title length.

Q: Please cite this article as: El-Shall N.A., Shewita R.S., Abd El-Hack M.E., AlKahtane A., Alarifi S., Alkahtani S., Abdel-Daim M.M. & Sedeik M.E., Effect of essential oils on the immune response to some viral vaccines in broiler chickens, with special reference to Newcastle disease virus, Poultry Science (2020), doi: https://doi.(Mohamed E. Abd El-Hack). 21 (195228.82) did not significantly (p>0.05) improve growth performance compared to 41 the non-treated birds (NC and VC) (197019.56 and 190438.66). Essential oils 42 showed an antiviral effect on vNDv in vivo (in chickens) as a preventive measure 43 (PRV) as well as some therapeutic effect (TTT) through decreasing the viral shedding 44 titres (loNC 0 ), mortality rate, and severity of clinical signs and post mortem lesions, in 45 addition to serum malondialdhyde (MDA) level. Regarding the other viruses, the EOs 46 mixture did not improve the immune response to the AI and IB vaccines but age (2108341.05). The studied EOs mixture showed an immune stimulating response 49 to ND and IBD vaccines, antiviral effect against ND virus especially if administered 50 before the challenge, however it did not have a growth promoting effect. 51 52

A: Journal Pre-proof Effect of essential oils on the immune response to some viral vaccines in broiler chickens, with special reference to Newcastle disease virus Effect of essential oils on the immune response to some viral vaccines in broiler 3 chickens, with special reference to Newcastle disease virus 4
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Q: Campylobacter jejuni remains one of the major gut pathogens of our time. Its zoonotic nature and wide-spread distribution in industrialized countries calls for a quick and reliable diagnostic tool. Antibody-based detection presents a suitable means to identify pathogenic bacteria. However, the knowledge about immunodominant targets is limited. Thus, an approach is presented, which allows for the rapid screening of numerous cDNA derived expression clones to identify novel antigens. The deeper understanding of immunodominant proteins assists in the design of diagnostic tools and furthers the insight into the bacterium's pathogenicity as well as revealing potential candidates for vaccination. We have successfully screened 1536 clones of an expression library to identify 22 proteins that have not been described as immunodominant before. After subcloning the corresponding 22 genes and expression of full-length proteins, we investigated the immunodominant character by microarrays and ELISA. Subsequently, seven proteins were selected for epitope mapping. For cj0669 and cj0920c linear epitopes were identified. For cj0669, specificity assays revealed a specific linear epitope site. Consequently, an eleven amino acid residue sequence TLIKELKRLGI was analyzed via alanine scan, which revealed the glycine residue to be significant for binding of the antibody. The innovative approach presented herein of generating cDNAs of prokaryotes in combination with a microarray platform rendering time-consuming purification steps obsolete has helped to illuminate novel immunodominant proteins of C.jejuni. The findings of a specific linear epitope pave the way for a plethora of future research and the potential use in diagnostic applications such as serological screenings. Moreover, the current approach is easily adaptable to other highly relevant bacteria making it a formidable tool for the future discovery of antigens and potential biomarkers. Consequently, it is desirable to simplify the identification of structural epitopes, as this would extend the spectrum of novel epitopes to be detected.

A: Rapid Identification of Novel Immunodominant Proteins and Characterization of a Specific Linear Epitope of Campylobacter jejuni
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Q: Middle East respiratory syndrome coronavirus (MERS-CoV) has continuously posed a threat to public health worldwide, yet no therapeutics or vaccines are currently available to prevent or treat MERS-CoV infection. We previously identified a fusion inhibitory peptide (HR2P-M2) targeting the MERS-CoV S2 protein HR1 domain and a highly potent neutralizing monoclonal antibody (m336) specific to the S1 spike protein receptor-binding domain (RBD). However, m336 was found to have reduced efficacy against MERS-CoV strains with mutations in RBD, and HR2P-M2 showed low potency, thus limiting the clinical application of each when administered separately. However, we herein report that the combination of m336 and HR2P-M2 exhibited potent synergism in inhibiting MERS-CoV S protein-mediated cell-cell fusion and infection by MERS-CoV pseudoviruses with or without mutations in the RBD, resulting in the enhancement of antiviral activity in contrast to either one administered alone. Thus, this combinatorial strategy could be used in clinics for the urgent treatment of MERS-CoV-infected patients. Viruses 2019, 11, 31 2 of 12 between viral and cellular membranes through the interaction between its HR1 and HR2 domains and entry of the viral genetic materials into the host cell [5] [6] [7] [8] . Thus, both the RBD in S1 subunit and HR1 domain in S2 subunit can serve as important targets for development of antiviral agents against MERS-CoV infection. Recently, we identified a peptide derived from the HR2 domain of MERS-CoV S protein S2 subunit, designated HR2P, which could interact with the HR1 domain of S protein S2 subunit to form a six-helix bundle (6-HB) complex and block viral fusion and replication with IC 50 s ranging from 0.6 to 1 M [5]. By replacing amino acid residues at the i to i + 4 positions with a negatively charged amino acid (e.g., E) and a positively charged amino acid (e.g., K) in HR2P for introduction of intramolecular salt-bridges, the resultant peptide HR2P-M2 exhibited improved solubility, stability, and anti-MERS-CoV activity [5, 9] . However, its potency is still not strong enough to warrant clinical development. By screening an extra-large phage-displayed antibody Fab library, Ying et al. identified a human neutralizing monoclonal antibody (hmAb), m336, which is specific for the RBD in the S protein S1 subunit. It exhibited highly potent neutralizing activity against MERS-CoV infection, both in vitro and in vivo [10] [11] [12] [13] . X-ray crystallography has shown that the binding epitope of m336 on MERS-CoV S protein almost completely overlaps with the binding site of DPP4 [14] . However, the future clinical application of m336 could be limited by its inability to neutralize MERS-CoV strains with mutations in RBD, like the mouse neutralizing mAb Mersmab1 with similar weakness [15, 16] . In this study, we compared the sensitivity of a pseudotyped MERS-CoV wild-type strain with that of strains with key mutations, including D509G, D510G, Q522H, and I529T, which were detected in the RBD of some MERS-CoV strains isolated from different regions and at different times throughout the course of the MERS outbreak from 2012 to 2015 [17, 18] . We found that these strains with mutations in RBD were significantly less sensitive than the wild-type strain to the neutralizing activity of m336, while the pseudoviruses with or without mutations showed equal sensitivity to the fusion inhibitory activity of HR2P-M2. Interestingly, when m336 was combined with HR2P-M2, a strong synergism emerged against MERS-CoV S-mediated cell-cell fusion and infection by pseudotyped MERS-CoV strains with or without mutations in RBD, suggesting that this combinational therapy could be further developed for clinical use to treat patients infected by the MERS-CoV strains with or without mutations in RBD.

A:
Combining a Fusion Inhibitory Peptide Targeting the MERS-CoV S2 Protein HR1 Domain and a Neutralizing Antibody Specific for the S1 Protein Receptor-Binding Domain (RBD) Showed Potent Synergism against Pseudotyped MERS-CoV with or without Mutations in RBD
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