Teacher: In this task, you're given a paragraph and title from the research paper. Your task is to classify whether the given title is suitable or not for the research paper based on the given paragraph. Return "True" if title is proper according to paragraph else "False".
Teacher: Now, understand the problem? If you are still confused, see the following example:
Paragraph: The severe acute respiratory syndrome (SARS) epidemic originating from China in 2002 was caused by a previously uncharacterized coronavirus that could be identified by specific RT-PCR amplification. Efforts to control future SARS outbreaks depend on the accurate and early identification of SARS-CoV infected patients. A real-time fluorogenic RT-PCR assay based on the 3 -noncoding region (3 -NCR) of SARS-CoV genome was developed as a quantitative SARS diagnostic tool. The ideal amplification efficiency of a sensitive SARS-CoV RT-PCR assay should yield an E value (PCR product concentration increase per amplification cycle) equal to 2.0. It was demonstrated that the 3 -NCR SARS-CoV based RT-PCR reactions could be formulated to reach excellent E values of 1.81, or 91% amplification efficacy. The SARS-CoV cDNA preparations derived from viral RNA extract and the cloned recombinant plasmid both exhibit the identical amplification characteristics, i.e. amplification efficacy using the same PCR formulation developed in this study. The viral genomic copy (or genomic equivalences, GE) per infectious unit (GE/pfu) of SARS-CoV used in this study was also established to be approximate 1200-1600:1. The assay's detection sensitivity could reach 0.005 pfu or 6-8 GE per assay. It was preliminarily demonstrated that the assay could efficiently detect SARS-CoV from clinical specimens of SARS probable and suspected patients identified in Taiwan. The 3 -NCR based SARS-CoV assay demonstrated 100% diagnostic specificity testing samples of patients with acute respiratory disease from a non-SARS epidemic region.
Title: Development and evaluation of an efficient 3 -noncoding region-based SARS coronavirus (SARS-CoV) RT-PCR assay for detection of SARS-CoV
Solution: True
Reason: The answer is true because the title of the paragraph is correct where it described the development of 3 -noncoding region of SARS-CoV genome and assay efficiently detecting SARS-CoV from clinical specimens.

Now, solve this instance: Paragraph: 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.
Title: 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
Student:
False